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multi_ex.txt
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multi_ex.txt
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ID TPA_HUMAN Reviewed; 562 AA.
AC P00750; A8K022; B2R8E8; Q15103; Q503B0; Q6PJA5; Q7Z7N2; Q86YK8;
AC Q9BU99; Q9BZW1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 05-OCT-2010, entry version 160.
DE RecName: Full=Tissue-type plasminogen activator;
DE Short=t-PA;
DE Short=t-plasminogen activator;
DE Short=tPA;
DE EC=3.4.21.68;
DE AltName: INN=Alteplase;
DE AltName: INN=Reteplase;
DE Contains:
DE RecName: Full=Tissue-type plasminogen activator chain A;
DE Contains:
DE RecName: Full=Tissue-type plasminogen activator chain B;
DE Flags: Precursor;
GN Name=PLAT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Melanoma;
RX MEDLINE=83115262; PubMed=6337343; DOI=10.1038/301214a0;
RA Pennica D., Holmes W.E., Kohr W.J., Harkins R.N., Vehar G.A.,
RA Ward C.A., Bennett W.F., Yelverton E., Seeburg P.H., Heyneker H.L.,
RA Goeddel D.V., Collen D.;
RT "Cloning and expression of human tissue-type plasminogen activator
RT cDNA in E. coli.";
RL Nature 301:214-221(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=84298137; PubMed=6089198; DOI=10.1073/pnas.81.17.5355;
RA Ny T., Elgh F., Lund B.;
RT "The structure of the human tissue-type plasminogen activator gene:
RT correlation of intron and exon structures to functional and structural
RT domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:5355-5359(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=86196143; PubMed=3009482;
RA Friezner Degen S.J., Rajput B., Reich E.;
RT "The human tissue plasminogen activator gene.";
RL J. Biol. Chem. 261:6972-6985(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX MEDLINE=86284200; PubMed=3090401;
RA Harris T.J., Patel T., Marston F.A., Little S., Emtage J.S.,
RA Opdenakker G., Volckaert G., Rombauts W., Billiau A., Somer P.;
RT "Cloning of cDNA coding for human tissue-type plasminogen activator
RT and its expression in Escherichia coli.";
RL Mol. Biol. Med. 3:279-292(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX MEDLINE=88054470; PubMed=2824147;
RA Reddy V.B., Garramone A.J., Sasak H., Wei C.-M., Watkins P., Galli J.,
RA Hsiung N.;
RT "Expression of human uterine tissue-type plasminogen activator in
RT mouse cells using BPV vectors.";
RL DNA 6:461-472(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal lung;
RX MEDLINE=88262579; PubMed=3133640; DOI=10.1093/nar/16.12.5695;
RA Sasaki H., Saito Y., Hayashi M., Otsuka K., Niwa M.;
RT "Nucleotide sequence of the tissue-type plasminogen activator cDNA
RT from human fetal lung cells.";
RL Nucleic Acids Res. 16:5695-5695(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Umbilical vein;
RX MEDLINE=90192129; PubMed=2107528; DOI=10.1093/nar/18.4.1086;
RA Siebert P.D., Fong K.;
RT "Variant tissue-type plasminogen activator (PLAT) cDNA obtained from
RT human endothelial cells.";
RL Nucleic Acids Res. 18:1086-1086(1990).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA Dou D.;
RT "A brain-type plasminogen activator.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Liu Y., Xu L., Zeng Y., He X.;
RT "cDNA of tissue plasminogen activator.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-34; SER-136;
RP THR-146 AND TRP-164.
RG SeattleSNPs variation discovery resource;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
RX MEDLINE=85289338; PubMed=3161893;
RA Fisher R., Waller E.K., Grossi G., Thompson D., Tizard R.,
RA Schleuning W.-D.;
RT "Isolation and characterization of the human tissue-type plasminogen
RT activator structural gene including its 5' flanking region.";
RL J. Biol. Chem. 260:11223-11230(1985).
RN [16]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-562.
RX MEDLINE=91291340; PubMed=1368681;
RA Itagaki Y., Yasuda H., Morinaga T., Mitsuda S., Higashio K.;
RT "Purification and characterization of tissue plasminogen activator
RT secreted by human embryonic lung diploid fibroblasts, IMR-90 cells.";
RL Agric. Biol. Chem. 55:1225-1232(1991).
RN [17]
RP PROTEIN SEQUENCE OF 33-52 AND 311-330.
RC TISSUE=Melanoma;
RX MEDLINE=83209620; PubMed=6682760;
RX DOI=10.1111/j.1432-1033.1983.tb07418.x;
RA Wallen P., Pohl G., Bergsdorf N., Raanby M., Ny T., Joernvall H.;
RT "Purification and characterization of a melanoma cell plasminogen
RT activator.";
RL Eur. J. Biochem. 132:681-686(1983).
RN [18]
RP PROTEIN SEQUENCE OF 36-562.
RC TISSUE=Melanoma;
RX MEDLINE=85000468; PubMed=6433976; DOI=10.1021/bi00311a020;
RA Pohl G., Kaellstroem M., Bergsdorf N., Wallen P., Joernvall H.;
RT "Tissue plasminogen activator: peptide analyses confirm an indirectly
RT derived amino acid sequence, identify the active site serine residue,
RT establish glycosylation sites, and localize variant differences.";
RL Biochemistry 23:3701-3707(1984).
RN [19]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 251-358.
RX MEDLINE=83169656; PubMed=6572897; DOI=10.1073/pnas.80.2.349;
RA Edlund T., Ny T., Raanby M., Heden L.-O., Palm G., Holmgren E.,
RA Josephson S.;
RT "Isolation of cDNA sequences coding for a part of human tissue
RT plasminogen activator.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:349-352(1983).
RN [20]
RP PARTIAL PROTEIN SEQUENCE, AND SIGNAL SEQUENCE CLEAVAGE SITE.
RA Jalah R., Pavlakis G.N., Felber B.J.;
RL Submitted (JUL-2007) to UniProtKB.
RN [21]
RP STRUCTURE OF CARBOHYDRATES.
RX MEDLINE=90092112; PubMed=2513186;
RX DOI=10.1111/j.1432-1033.1989.tb15206.x;
RA Pfeiffer G., Schmidt M., Strube K.-H., Geyer R.;
RT "Carbohydrate structure of recombinant human uterine tissue
RT plasminogen activator expressed in mouse epithelial cells.";
RL Eur. J. Biochem. 186:273-286(1989).
RN [22]
RP GLYCOSYLATION AT THR-96.
RX MEDLINE=91159408; PubMed=1900431; DOI=10.1021/bi00223a004;
RA Harris R.J., Leonard C.K., Guzzetta A.W., Spellman M.W.;
RT "Tissue plasminogen activator has an O-linked fucose attached to
RT threonine-61 in the epidermal growth factor domain.";
RL Biochemistry 30:2311-2314(1991).
RN [23]
RP DISULFIDE BONDS IN KRINGLE 2.
RX MEDLINE=91244765; PubMed=1645336;
RA Vlahos C.J., Wilhelm O.G., Hassell T., Jaskunas S.R., Bang N.U.;
RT "Disulfide pairing of the recombinant kringle-2 domain of tissue
RT plasminogen activator produced in Escherichia coli.";
RL J. Biol. Chem. 266:10070-10072(1991).
RN [24]
RP INTERACTION WITH LRP1B.
RX MEDLINE=21369943; PubMed=11384978; DOI=10.1074/jbc.M102727200;
RA Liu C.-X., Li Y., Obermoeller-McCormick L.M., Schwartz A.L., Bu G.;
RT "The putative tumor suppressor LRP1B, a novel member of the low
RT density lipoprotein (LDL) receptor family, exhibits both overlapping
RT and distinct properties with the LDL receptor-related protein.";
RL J. Biol. Chem. 276:28889-28896(2001).
RN [25]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [26]
RP STRUCTURE BY NMR OF KRINGLE 2.
RX MEDLINE=90122799; PubMed=2558718; DOI=10.1021/bi00450a016;
RA Byeon I.-J.L., Kelley R.F., Llinas M.;
RT "1H NMR structural characterization of a recombinant kringle 2 domain
RT from human tissue-type plasminogen activator.";
RL Biochemistry 28:9350-9360(1989).
RN [27]
RP STRUCTURE BY NMR OF KRINGLE 2.
RX MEDLINE=91200042; PubMed=1901789;
RX DOI=10.1111/j.1432-1033.1991.tb15894.x;
RA Byeon I.-J.L., Kelley R.F., Llinas M.;
RT "Kringle-2 domain of the tissue-type plasminogen activator. 1H-NMR
RT assignments and secondary structure.";
RL Eur. J. Biochem. 197:155-165(1991).
RN [28]
RP STRUCTURE BY NMR OF KRINGLE 2.
RX MEDLINE=92106329; PubMed=1762144; DOI=10.1016/0022-2836(91)90592-T;
RA Byeon I.-J.L., Llinas M.;
RT "Solution structure of the tissue-type plasminogen activator kringle 2
RT domain complexed to 6-aminohexanoic acid an antifibrinolytic drug.";
RL J. Mol. Biol. 222:1035-1051(1991).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF KRINGLE 2.
RX MEDLINE=92118803; PubMed=1310033; DOI=10.1021/bi00116a037;
RA de Vos A., Ultsch M.H., Kelley R.F., Padmanabhan K., Tulinskly A.,
RA Westbrook M.L., Kossiakof A.A.;
RT "Crystal structure of the kringle 2 domain of tissue plasminogen
RT activator at 2.4-A resolution.";
RL Biochemistry 31:270-279(1992).
RN [30]
RP STRUCTURE BY NMR OF 38-85.
RX MEDLINE=92292163; PubMed=1602484; DOI=10.1016/0022-2836(92)90403-7;
RA Downing A.K., Driscoll P.C., Harvey T.S., Dudgeon T.J., Smith B.O.,
RA Baron M., Campbell I.D.;
RT "Solution structure of the fibrin binding finger domain of tissue-type
RT plasminogen activator determined by 1H nuclear magnetic resonance.";
RL J. Mol. Biol. 225:821-833(1992).
RN [31]
RP STRUCTURE BY NMR OF 36-126.
RX MEDLINE=96027104; PubMed=7582899; DOI=10.1016/S0969-2126(01)00217-9;
RA Smith B.O., Downing A.K., Driscoll P.C., Dudgeon T.J., Campbell I.D.;
RT "The solution structure and backbone dynamics of the fibronectin type
RT I and epidermal growth factor-like pair of modules of tissue-type
RT plasminogen activator.";
RL Structure 3:823-833(1995).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF CATALYTIC DOMAIN.
RX MEDLINE=96200985; PubMed=8613982; DOI=10.1006/jmbi.1996.0238;
RA Lamba D., Bauer M., Huber R., Fischer S., Rudolph R., Kohnert U.,
RA Bode W.;
RT "The 2.3 A crystal structure of the catalytic domain of recombinant
RT two-chain human tissue-type plasminogen activator.";
RL J. Mol. Biol. 258:117-135(1996).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF CATALYTIC DOMAIN.
RX MEDLINE=97449126; PubMed=9305622; DOI=10.1093/emboj/16.16.4797;
RA Renatus M., Engh R.A., Stubbs M.T., Huber R., Fischer S., Kohnert U.,
RA Bode W.;
RT "Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray
RT crystal structure of single-chain human tPA.";
RL EMBO J. 16:4797-4805(1997).
CC -!- FUNCTION: Converts the abundant, but inactive, zymogen plasminogen
CC to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By
CC controlling plasmin-mediated proteolysis, it plays an important
CC role in tissue remodeling and degradation, in cell migration and
CC many other physiopathological events. Play a direct role in
CC facilitating neuronal migration.
CC -!- CATALYTIC ACTIVITY: Specific cleavage of Arg-|-Val bond in
CC plasminogen to form plasmin.
CC -!- SUBUNIT: Heterodimer of chain A and chain B held by a disulfide
CC bond. Binds to fibrin with high affinity. This interaction leads
CC to an increase in the catalytic efficiency of the enzyme between
CC 100-fold and 1000-fold, due to an increase in affinity for
CC plasminogen. Similarly, binding to heparin increases the
CC activation of plasminogen. Binds to annexin A2, cytokeratin-8,
CC fibronectin and laminin. Binds to mannose receptor and the low-
CC density lipoprotein receptor-related protein (LRP1); these
CC proteins are involved in TPA clearance. Yet unidentified
CC interactions on endothelial cells and vascular smooth muscle cells
CC (VSMC) lead to a 100-fold stimulation of plasminogen activation.
CC In addition, binding to VSMC reduces TPA inhibition by PAI-1 by
CC 30-fold. Binds LRP1B; binding is followed by internalization and
CC degradation.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Long;
CC IsoId=P00750-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P00750-2; Sequence=VSP_005411, VSP_005412;
CC Note=May be produced at very low levels due to a premature stop
CC codon in the mRNA, leading to nonsense-mediated mRNA decay;
CC Name=3;
CC IsoId=P00750-3; Sequence=VSP_015957;
CC Note=No experimental confirmation available;
CC Name=4; Synonyms=Neonatal;
CC IsoId=P00750-4; Sequence=VSP_028029, VSP_028030;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Synthesized in numerous tissues (including
CC tumors) and secreted into most extracellular body fluids, such as
CC plasma, uterine fluid, saliva, gingival crevicular fluid, tears,
CC seminal fluid, and milk.
CC -!- DOMAIN: Both FN1 and one of the kringle domains are required for
CC binding to fibrin.
CC -!- DOMAIN: Both FN1 and EGF-like domains are important for binding to
CC LRP1.
CC -!- DOMAIN: The FN1 domain mediates binding to annexin A2.
CC -!- DOMAIN: The second kringle domain is implicated in binding to
CC cytokeratin-8 and to the endothelial cell surface binding site.
CC -!- PTM: The single chain, almost fully active enzyme, can be further
CC processed into a two-chain fully active form by a cleavage after
CC Arg-310 catalyzed by plasmin, tissue kallikrein or factor Xa.
CC -!- PTM: Differential cell-specific N-linked glycosylation gives rise
CC to two glycoforms, type I (glycosylated at Asn-219) and type II
CC (not glycosylated at Asn-219). The single chain type I glycoform
CC is less readily converted into the two-chain form by plasmin, and
CC the two-chain type I glycoform has a lower activity than the two-
CC chain type II glycoform in the presence of fibrin.
CC -!- PTM: N-glycosylation of Asn-152; the bound oligomannosidic glycan
CC is involved in the interaction with the mannose receptor.
CC -!- PTM: Characterization of O-linked glycan was studied in Bowes
CC melanoma cell line.
CC -!- DISEASE: Note=Increased activity of TPA results in increased
CC fibrinolysis of fibrin blood clots that is associated with
CC excessive bleeding. Defective release of TPA results in
CC hypofibrinolysis that can lead to thrombosis or embolism.
CC -!- PHARMACEUTICAL: Available under the names Activase (Genentech) and
CC Retavase (Centocor and Roche) [Retavase is a fragment of TPA that
CC contains kringle 2 and the protease domain; it was also known as
CC BM 06.022]. Used in Acute Myocardial Infarction (AMI), in Acute
CC Ischemic Stroke (AIS) and Pulmonary Embolism (PE) to initiate
CC fibrinolysis.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC -!- SIMILARITY: Contains 1 EGF-like domain.
CC -!- SIMILARITY: Contains 1 fibronectin type-I domain.
CC -!- SIMILARITY: Contains 2 kringle domains.
CC -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Tissue plasminogen activator
CC entry;
CC URL="http://en.wikipedia.org/wiki/Tissue_plasminogen_Activator";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/plat/";
CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC polymorphism database;
CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=PLAT";
CC -!- WEB RESOURCE: Name=Activase; Note=Clinical information on
CC Activase;
CC URL="http://www.gene.com/gene/products/information/cardiovascular/activase/index.jsp";
CC -!- WEB RESOURCE: Name=Retavase; Note=Clinical information on
CC Retavase;
CC URL="http://www.retavase.com/pdf/Retavase_PI.pdf";
CC -----------------------------------------------------------------------
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CC -----------------------------------------------------------------------
DR EMBL; L00153; AAB59510.1; -; Genomic_DNA.
DR EMBL; L00141; AAB59510.1; JOINED; Genomic_DNA.
DR EMBL; L00142; AAB59510.1; JOINED; Genomic_DNA.
DR EMBL; L00143; AAB59510.1; JOINED; Genomic_DNA.
DR EMBL; L00144; AAB59510.1; JOINED; Genomic_DNA.
DR EMBL; L00145; AAB59510.1; JOINED; Genomic_DNA.
DR EMBL; L00146; AAB59510.1; JOINED; Genomic_DNA.
DR EMBL; L00147; AAB59510.1; JOINED; Genomic_DNA.
DR EMBL; L00148; AAB59510.1; JOINED; Genomic_DNA.
DR EMBL; L00149; AAB59510.1; JOINED; Genomic_DNA.
DR EMBL; L00150; AAB59510.1; JOINED; Genomic_DNA.
DR EMBL; L00151; AAB59510.1; JOINED; Genomic_DNA.
DR EMBL; K03021; AAA98809.1; -; Genomic_DNA.
DR EMBL; M15518; AAA60111.1; -; mRNA.
DR EMBL; M18182; AAA36800.1; -; mRNA.
DR EMBL; X07393; CAA30302.1; -; mRNA.
DR EMBL; X13097; CAA31489.1; -; mRNA.
DR EMBL; AF260825; AAK11956.1; -; mRNA.
DR EMBL; AY221101; AAO34406.1; -; mRNA.
DR EMBL; AK289387; BAF82076.1; -; mRNA.
DR EMBL; AK290575; BAF83264.1; -; mRNA.
DR EMBL; AK313342; BAG36145.1; -; mRNA.
DR EMBL; BT007060; AAP35709.1; -; mRNA.
DR EMBL; AY291060; AAP34246.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63235.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63233.1; -; Genomic_DNA.
DR EMBL; BC002795; AAH02795.3; -; mRNA.
DR EMBL; BC007231; AAH07231.1; -; mRNA.
DR EMBL; BC013968; AAH13968.3; -; mRNA.
DR EMBL; BC018636; AAH18636.3; -; mRNA.
DR EMBL; BC095403; AAH95403.1; -; mRNA.
DR EMBL; M11890; AAA61213.1; -; Genomic_DNA.
DR EMBL; M11889; AAA61213.1; JOINED; Genomic_DNA.
DR EMBL; D01096; BAA00881.1; -; mRNA.
DR EMBL; V00570; CAA23833.1; -; mRNA.
DR IPI; IPI00019590; -.
DR IPI; IPI00479511; -.
DR IPI; IPI00910450; -.
DR IPI; IPI00953228; -.
DR PIR; A94004; UKHUT.
DR PIR; I38098; I38098.
DR RefSeq; NP_000921.1; -.
DR RefSeq; NP_127509.1; -.
DR UniGene; Hs.491582; -.
DR PDB; 1A5H; X-ray; 2.90 A; A/B=311-562, C/D=298-304.
DR PDB; 1BDA; X-ray; 3.35 A; A/B=298-562.
DR PDB; 1PK2; NMR; -; A=209-298.
DR PDB; 1PML; X-ray; 2.38 A; A/B/C=213-298.
DR PDB; 1RTF; X-ray; 2.30 A; B=311-562.
DR PDB; 1TPG; NMR; -; A=36-126.
DR PDB; 1TPK; X-ray; 2.40 A; A/B/C=211-298.
DR PDB; 1TPM; NMR; -; A=36-85.
DR PDB; 1TPN; NMR; -; A=36-85.
DR PDBsum; 1A5H; -.
DR PDBsum; 1BDA; -.
DR PDBsum; 1PK2; -.
DR PDBsum; 1PML; -.
DR PDBsum; 1RTF; -.
DR PDBsum; 1TPG; -.
DR PDBsum; 1TPK; -.
DR PDBsum; 1TPM; -.
DR PDBsum; 1TPN; -.
DR ProteinModelPortal; P00750; -.
DR SMR; P00750; 126-210, 174-299, 212-334.
DR STRING; P00750; -.
DR MEROPS; S01.232; -.
DR GlycoSuiteDB; P00750; -.
DR PRIDE; P00750; -.
DR Ensembl; ENST00000220809; ENSP00000220809; ENSG00000104368.
DR GeneID; 5327; -.
DR KEGG; hsa:5327; -.
DR UCSC; uc003xos.2; human.
DR UCSC; uc003xot.2; human.
DR UCSC; uc010lxf.1; human.
DR CTD; 5327; -.
DR GeneCards; GC08M042050; -.
DR H-InvDB; HIX0007476; -.
DR HGNC; HGNC:9051; PLAT.
DR HPA; CAB009335; -.
DR HPA; HPA003412; -.
DR MIM; 173370; gene.
DR PharmGKB; PA33381; -.
DR eggNOG; prNOG16610; -.
DR HOVERGEN; HBG008633; -.
DR InParanoid; P00750; -.
DR OMA; TCGLRQY; -.
DR OrthoDB; EOG9TQPVK; -.
DR PhylomeDB; P00750; -.
DR BRENDA; 3.4.21.68; 247.
DR Pathway_Interaction_DB; amb2_neutrophils_pathway; amb2 Integrin signaling.
DR Reactome; REACT_16888; Signaling by PDGF.
DR Reactome; REACT_604; Hemostasis.
DR DrugBank; DB00009; Alteplase.
DR DrugBank; DB00513; Aminocaproic Acid.
DR DrugBank; DB00029; Anistreplase.
DR DrugBank; DB01088; Iloprost.
DR DrugBank; DB00015; Reteplase.
DR DrugBank; DB00031; Tenecteplase.
DR DrugBank; DB00302; Tranexamic Acid.
DR DrugBank; DB00013; Urokinase.
DR NextBio; 20622; -.
DR PMAP-CutDB; P00750; -.
DR ArrayExpress; P00750; -.
DR Bgee; P00750; -.
DR Genevestigator; P00750; -.
DR GermOnline; ENSG00000104368; Homo sapiens.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005515; F:protein binding; IPI:BHF-UCL.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
DR GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
DR GO; GO:0045861; P:negative regulation of proteolysis; IDA:BHF-UCL.
DR GO; GO:0006464; P:protein modification process; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR InterPro; IPR016060; Complement_control_module.
DR InterPro; IPR006209; EGF.
DR InterPro; IPR006210; EGF-like.
DR InterPro; IPR013032; EGF-like_reg_CS.
DR InterPro; IPR000742; EGF_3.
DR InterPro; IPR000083; Fibrnctn1.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR018114; Peptidase_S1/S6_AS.
DR InterPro; IPR001254; Peptidase_S1_S6.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR009003; Ser/Cys_Pept_Trypsin-like.
DR Gene3D; G3DSA:2.10.70.10; Complement_control_module; 1.
DR Gene3D; G3DSA:2.40.20.10; Kringle; 2.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00039; fn1; 1.
DR Pfam; PF00051; Kringle; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00058; FN1; 1.
DR SMART; SM00130; KR; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57440; Kringle-like; 2.
DR SUPFAM; SSF50494; Pept_Ser_Cys; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01253; FN1_1; 1.
DR PROSITE; PS51091; FN1_2; 1.
DR PROSITE; PS00021; KRINGLE_1; 2.
DR PROSITE; PS50070; KRINGLE_2; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing;
KW Cleavage on pair of basic residues; Complete proteome;
KW Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Glycoprotein; Hydrolase; Kringle; Pharmaceutical;
KW Plasminogen activation; Polymorphism; Protease; Repeat; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1 22
FT PROPEP 23 32
FT /FTId=PRO_0000028348.
FT PROPEP 33 35 Removed by plasmin.
FT /FTId=PRO_0000028349.
FT CHAIN 36 562 Tissue-type plasminogen activator.
FT /FTId=PRO_0000028350.
FT CHAIN 36 310 Tissue-type plasminogen activator chain
FT A.
FT /FTId=PRO_0000028351.
FT CHAIN 311 562 Tissue-type plasminogen activator chain
FT B.
FT /FTId=PRO_0000028352.
FT DOMAIN 39 81 Fibronectin type-I.
FT DOMAIN 82 120 EGF-like.
FT DOMAIN 127 208 Kringle 1.
FT DOMAIN 215 296 Kringle 2.
FT DOMAIN 311 561 Peptidase S1.
FT REGION 42 52 Important for binding to annexin A2.
FT ACT_SITE 357 357 Charge relay system.
FT ACT_SITE 406 406 Charge relay system.
FT ACT_SITE 513 513 Charge relay system.
FT SITE 102 102 Important for binding to LRP1.
FT SITE 253 253 Not glycosylated.
FT SITE 464 464 Important for single-chain activity.
FT SITE 512 512 Important for single-chain activity.
FT CARBOHYD 96 96 O-linked (Fuc).
FT /FTId=CAR_000029.
FT CARBOHYD 152 152 N-linked (GlcNAc...).
FT CARBOHYD 219 219 N-linked (GlcNAc...); partial.
FT /FTId=CAR_000030.
FT CARBOHYD 483 483 N-linked (GlcNAc...).
FT /FTId=CAR_000031.
FT DISULFID 41 71
FT DISULFID 69 78
FT DISULFID 86 97
FT DISULFID 91 108
FT DISULFID 110 119
FT DISULFID 127 208 By similarity.
FT DISULFID 148 190 By similarity.
FT DISULFID 179 203 By similarity.
FT DISULFID 215 296
FT DISULFID 236 278
FT DISULFID 267 291
FT DISULFID 299 430 Interchain (between A and B chains).
FT DISULFID 342 358 By similarity.
FT DISULFID 350 419 By similarity.
FT DISULFID 444 519 By similarity.
FT DISULFID 476 492 By similarity.
FT DISULFID 509 537 By similarity.
FT VAR_SEQ 1 40 MDAMKRGLCCVLLLCGAVFVSPSQEIHARFRRGARSYQVI
FT -> MAS (in isoform 4).
FT /FTId=VSP_028029.
FT VAR_SEQ 39 85 VICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCH
FT SVPVKS -> G (in isoform 3).
FT /FTId=VSP_015957.
FT VAR_SEQ 79 208 Missing (in isoform 4).
FT /FTId=VSP_028030.
FT VAR_SEQ 269 291 NPDGDAKPWCHVLKNRRLTWEYC -> TGRSVSSPATASMR
FT PCPLSIRSG (in isoform 2).
FT /FTId=VSP_005411.
FT VAR_SEQ 292 562 Missing (in isoform 2).
FT /FTId=VSP_005412.
FT VARIANT 34 34 A -> D (in dbSNP:rs8178733).
FT /FTId=VAR_020181.
FT VARIANT 136 136 R -> S (in dbSNP:rs8178747).
FT /FTId=VAR_038732.
FT VARIANT 146 146 A -> T (in dbSNP:rs8178748).
FT /FTId=VAR_038733.
FT VARIANT 164 164 R -> W (in dbSNP:rs2020921).
FT /FTId=VAR_011783.
FT CONFLICT 93 93 N -> T (in Ref. 2; AAB59510).
FT CONFLICT 159 160 KP -> NA (in Ref. 7; CAA31489).
FT CONFLICT 247 247 K -> N (in Ref. 9; AAO34406).
FT CONFLICT 283 283 N -> S (in Ref. 14; AAH95403).
FT CONFLICT 333 334 RR -> EE (in Ref. 8; AAK11956).
FT CONFLICT 389 389 V -> C (in Ref. 8; AAK11956).
FT STRAND 44 46
FT STRAND 55 59
FT STRAND 61 64
FT STRAND 66 70
FT STRAND 72 74
FT STRAND 83 85
FT STRAND 96 104
FT STRAND 106 109
FT STRAND 115 118
FT HELIX 242 244
FT STRAND 248 250
FT HELIX 256 259
FT STRAND 262 264
FT STRAND 277 282
FT STRAND 285 291
FT STRAND 312 316
FT HELIX 319 321
FT STRAND 325 331
FT STRAND 338 346
FT STRAND 348 354
FT HELIX 356 359
FT HELIX 365 367
FT STRAND 368 373
FT STRAND 375 379
FT STRAND 385 394
FT TURN 400 402
FT STRAND 408 412
FT STRAND 415 417
FT STRAND 443 449
FT STRAND 464 470
FT HELIX 473 475
FT TURN 478 483
FT STRAND 490 494
FT STRAND 516 521
FT STRAND 524 533
FT STRAND 535 538
FT STRAND 544 548
FT HELIX 549 552
FT HELIX 553 559
SQ SEQUENCE 562 AA; 62917 MW; B7EC9B1A5E3FDC4D CRC64;
MDAMKRGLCC VLLLCGAVFV SPSQEIHARF RRGARSYQVI CRDEKTQMIY QQHQSWLRPV
LRSNRVEYCW CNSGRAQCHS VPVKSCSEPR CFNGGTCQQA LYFSDFVCQC PEGFAGKCCE
IDTRATCYED QGISYRGTWS TAESGAECTN WNSSALAQKP YSGRRPDAIR LGLGNHNYCR
NPDRDSKPWC YVFKAGKYSS EFCSTPACSE GNSDCYFGNG SAYRGTHSLT ESGASCLPWN
SMILIGKVYT AQNPSAQALG LGKHNYCRNP DGDAKPWCHV LKNRRLTWEY CDVPSCSTCG
LRQYSQPQFR IKGGLFADIA SHPWQAAIFA KHRRSPGERF LCGGILISSC WILSAAHCFQ
ERFPPHHLTV ILGRTYRVVP GEEEQKFEVE KYIVHKEFDD DTYDNDIALL QLKSDSSRCA
QESSVVRTVC LPPADLQLPD WTECELSGYG KHEALSPFYS ERLKEAHVRL YPSSRCTSQH
LLNRTVTDNM LCAGDTRSGG PQANLHDACQ GDSGGPLVCL NDGRMTLVGI ISWGLGCGQK
DVPGVYTKVT NYLDWIRDNM RP
//
ID CBBQ_CHRVI Reviewed; 74 AA.
AC P56540;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 10-AUG-2010, entry version 31.
DE RecName: Full=Protein CbbQ;
DE Flags: Fragment;
GN Name=cbbQ;
OS Chromatium vinosum (Allochromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Chromatiaceae; Allochromatium.
OX NCBI_TaxID=1049;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=89213919; PubMed=2708310;
RA Viale A.M., Kobayashi H., Akazawa T.;
RT "Expressed genes for plant-type ribulose 1,5-bisphosphate
RT carboxylase/oxygenase in the photosynthetic bacterium Chromatium
RT vinosum, which possesses two complete sets of the genes.";
RL J. Bacteriol. 171:2391-2400(1989).
RN [2]
RP IDENTIFICATION.
RX MEDLINE=95189107; PubMed=7883189; DOI=10.1016/0378-1119(94)00808-6;
RA Yokoyama K., Hayashi N.R., Arai H., Chung S.Y., Igarashi Y.,
RA Kodama T.;
RT "Genes encoding RubisCO in Pseudomonas hydrogenothermophila are
RT followed by a novel cbbQ gene similar to nirQ of the denitrification
RT gene cluster from Pseudomonas species.";
RL Gene 153:75-79(1995).
CC -!- FUNCTION: May affect the post-translational activation and/or
CC assembly of the oligomeric structure of RuBisCO.
CC -!- SIMILARITY: Belongs to the CbbQ/NirQ/NorQ/GpvN family.
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DR EMBL; M26396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR ProteinModelPortal; P56540; -.
DR SMR; P56540; 10-72.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR InterPro; IPR011704; ATPase_AAA-5.
DR Pfam; PF07728; AAA_5; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding.
FT CHAIN 1 >74 Protein CbbQ.
FT /FTId=PRO_0000219562.
FT NP_BIND 41 48 ATP (Potential).
FT NON_TER 74 74
SQ SEQUENCE 74 AA; 8377 MW; B7AB23BF4DEA291C CRC64;
MSDIDRNQFL IDHEPYYRPV SNEVALYEAA YAARMPVMLK GPTGCGKTRF VEYMAWKLGK
PLITVACNED MTAS
//
ID CBBQ_PSEHY Reviewed; 267 AA.
AC Q51858;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 10-AUG-2010, entry version 36.
DE RecName: Full=Protein CbbQ;
GN Name=cbbQ;
OS Pseudomonas hydrogenothermophila.
OC Bacteria; Proteobacteria; Betaproteobacteria; Hydrogenophilales;
OC Hydrogenophilaceae; Hydrogenophilus.
OX NCBI_TaxID=297;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TH-1;
RX MEDLINE=95189107; PubMed=7883189; DOI=10.1016/0378-1119(94)00808-6;
RA Yokoyama K., Hayashi N.R., Arai H., Chung S.Y., Igarashi Y.,
RA Kodama T.;
RT "Genes encoding RubisCO in Pseudomonas hydrogenothermophila are
RT followed by a novel cbbQ gene similar to nirQ of the denitrification
RT gene cluster from Pseudomonas species.";
RL Gene 153:75-79(1995).
CC -!- FUNCTION: May affect the post-translational activation and/or
CC assembly of the oligomeric structure of RuBisCO.
CC -!- SIMILARITY: Belongs to the CbbQ/NirQ/NorQ/GpvN family.
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CC -----------------------------------------------------------------------
DR EMBL; D30764; BAA06439.1; -; Genomic_DNA.
DR ProteinModelPortal; Q51858; -.
DR SMR; Q51858; 21-191.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR InterPro; IPR011704; ATPase_AAA-5.
DR InterPro; IPR013615; CbbQ_C.
DR Pfam; PF07728; AAA_5; 1.
DR Pfam; PF08406; CbbQ_C; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding.
FT CHAIN 1 267 Protein CbbQ.
FT /FTId=PRO_0000219563.
FT NP_BIND 39 46 ATP (Potential).
FT NP_BIND 99 106 ATP (Potential).
SQ SEQUENCE 267 AA; 29613 MW; EA99FE2DB05B0118 CRC64;
MDLRNQYLVR SEPYYHAVGD EIERFEAAYA NRIPMMLKGP TGCGKSRFVE YMAWKLGKPL
ITVACNEDMT AADLVGRFLL DKEGTRWQDG PLTTAARIGA ICYLDEVVEA RQDTTVVIHP
LTDHRRILPL DKKGEVVEAH PDFQIVISYN PGYQSAMKDL KTSTKQRFAA MDFDYPAPEV
ESEIVAHESG VDAATAKKLV EVAIRSRHLK GHGLDEGIST RLLVYAGSLI TKGIAPLIAC
EMALICPITD DPDLRYALRA AAQTLFA
//
ID NIRQ_PSEAE Reviewed; 260 AA.
AC Q51481;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 10-AUG-2010, entry version 66.
DE RecName: Full=Denitrification regulatory protein nirQ;
GN Name=nirQ; OrderedLocusNames=PA0520;
OS Pseudomonas aeruginosa.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAO1161;
RX MEDLINE=94362287; PubMed=7765251;
RA Arai H., Igarashi Y., Kodama T.;
RT "Structure and ANR-dependent transcription of the nir genes for
RT denitrification from Pseudomonas aeruginosa.";
RL Biosci. Biotechnol. Biochem. 58:1286-1291(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
RX MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT opportunistic pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Activator of nitrite and nitric oxide reductases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- INDUCTION: Under denitrifying conditions.
CC -!- SIMILARITY: Belongs to the CbbQ/NirQ/NorQ/GpvN family.
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DR EMBL; D37883; BAA07123.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG03909.1; -; Genomic_DNA.
DR PIR; JC2288; JC2288.
DR RefSeq; NP_249211.1; -.
DR ProteinModelPortal; Q51481; -.
DR SMR; Q51481; 14-183.
DR GeneID; 882214; -.
DR GenomeReviews; AE004091_GR; PA0520.
DR KEGG; pae:PA0520; -.
DR NMPDR; fig|208964.1.peg.521; -.
DR PseudoCAP; PA0520; -.
DR HOGENOM; HBG295312; -.
DR OMA; HEARILV; -.
DR ProtClustDB; CLSK865916; -.
DR BioCyc; PAER208964:PA0520-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR InterPro; IPR011704; ATPase_AAA-5.
DR InterPro; IPR013615; CbbQ_C.
DR Pfam; PF07728; AAA_5; 1.
DR Pfam; PF08406; CbbQ_C; 1.
PE 2: Evidence at transcript level;
KW Activator; ATP-binding; Complete proteome; Cytoplasm; DNA-binding;
KW Nucleotide-binding; Transcription; Transcription regulation.
FT CHAIN 1 260 Denitrification regulatory protein nirQ.
FT /FTId=PRO_0000219569.
FT NP_BIND 32 39 ATP (Potential).
FT NP_BIND 92 99 ATP (Potential).
FT DNA_BIND 234 253 H-T-H motif (Potential).
SQ SEQUENCE 260 AA; 28904 MW; 3FD36F19BEBA38B5 CRC64;
MRDATPFYEA TGHEIEVFER AWRHGLPVLL KGPTGCGKTR FVQYMARRLE LPLYSVACHD
DLGAADLLGR HLIGADGTWW QDGPLTRAVR EGGICYLDEV VEARQDTTVA IHPLADDRRE
LYLERTGETL QAPPSFMLVV SYNPGYQNLL KGLKPSTRQR FVALRFDYPA AQQEARILVG
ESGCAETLAQ RLVQLGQALR RLEQHDLEEV ASTRLLIFAA RLIGDGMDPR EACRVALAEP
LSDDPATVAA LMDIVDLHVA
//
ID CHDH_HUMAN Reviewed; 594 AA.
AC Q8NE62; Q9NY17;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 05-OCT-2010, entry version 72.
DE RecName: Full=Choline dehydrogenase, mitochondrial;
DE Short=CDH;
DE Short=CHD;
DE EC=1.1.99.1;
DE Flags: Precursor;
GN Name=CHDH;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-78.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 113-594.
RC TISSUE=Kidney;
RA Bugert P., Hanke S., Chudek J., Kovacs G.;
RT "Analysis of a putative tumor suppressor gene region of 100 kb at
RT chromosome 3p21.1 in conventional renal cell carcinoma.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: Choline + acceptor = betaine aldehyde +
CC reduced acceptor.
CC -!- COFACTOR: FAD (By similarity).
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis
CC via choline pathway; betaine aldehyde from choline (cytochrome c
CC reductase route): step 1/1.
CC -!- SUBCELLULAR LOCATION: Mitochondrion (Potential).
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
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DR EMBL; AC012467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034502; AAH34502.1; -; mRNA.
DR EMBL; AJ272267; CAB75961.1; -; mRNA.
DR IPI; IPI00168603; -.
DR RefSeq; NP_060867.2; -.
DR UniGene; Hs.126688; -.
DR ProteinModelPortal; Q8NE62; -.
DR STRING; Q8NE62; -.
DR PhosphoSite; Q8NE62; -.
DR Ensembl; ENST00000315251; ENSP00000319851; ENSG00000016391.
DR GeneID; 55349; -.
DR KEGG; hsa:55349; -.
DR UCSC; uc003dgz.1; human.
DR CTD; 55349; -.
DR GeneCards; GC03M053826; -.
DR HGNC; HGNC:24288; CHDH.
DR PharmGKB; PA134873121; -.
DR eggNOG; prNOG07180; -.
DR HOGENOM; HBG734713; -.
DR HOVERGEN; HBG023639; -.
DR InParanoid; Q8NE62; -.
DR OMA; SRDEYSY; -.
DR OrthoDB; EOG9962C6; -.
DR PhylomeDB; Q8NE62; -.
DR BRENDA; 1.1.99.1; 247.
DR DrugBank; DB00122; Choline.
DR NextBio; 59691; -.
DR ArrayExpress; Q8NE62; -.
DR Bgee; Q8NE62; -.
DR CleanEx; HS_CHDH; -.
DR Genevestigator; Q8NE62; -.
DR GermOnline; ENSG00000016391; Homo sapiens.
DR GO; GO:0008812; F:choline dehydrogenase activity; IEA:EC.
DR GO; GO:0050660; F:FAD or FADH2 binding; IEA:InterPro.
DR GO; GO:0006066; P:alcohol metabolic process; IEA:InterPro.
DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Complete proteome; FAD; Flavoprotein; Mitochondrion;
KW Oxidoreductase; Polymorphism; Transit peptide.
FT TRANSIT 1 ? Mitochondrion (Potential).
FT CHAIN ? 594 Choline dehydrogenase, mitochondrial.
FT /FTId=PRO_0000012329.
FT NP_BIND 42 71 FAD (By similarity).
FT ACT_SITE 511 511 By similarity.
FT MOD_RES 496 496 N6-acetyllysine (By similarity).
FT VARIANT 40 40 E -> A (in dbSNP:rs9001).
FT /FTId=VAR_020421.
FT VARIANT 78 78 L -> R (in dbSNP:rs12676).
FT /FTId=VAR_055097.
FT VARIANT 441 441 N -> S (in dbSNP:rs34974961).
FT /FTId=VAR_049357.
FT CONFLICT 113 113 R -> A (in Ref. 3; CAB75961).
SQ SEQUENCE 594 AA; 65358 MW; E9764CD0F325A501 CRC64;
MWCLLRGLGR PGALARGALG QQQSLGARAL ASAGSESRDE YSYVVVGAGS AGCVLAGRLT
EDPAERVLLL EAGPKDVLAG SKRLSWKIHM PAALVANLCD DRYNWCYHTE VQRGLDGRVL
YWPRGRVWGG SSSLNAMVYV RGHAEDYERW QRQGARGWDY AHCLPYFRKA QGHELGASRY
RGADGPLRVS RGKTNHPLHC AFLEATQQAG YPLTEDMNGF QQEGFGWMDM TIHEGKRWSA
ACAYLHPALS RTNLKAEAET LVSRVLFEGT RAVGVEYVKN GQSHRAYASK EVILSGGAIN
SPQLLMLSGI GNADDLKKLG IPVVCHLPGV GQNLQDHLEI YIQQACTRPI TLHSAQKPLR
KVCIGLEWLW KFTGEGATAH LETGGFIRSQ PGVPHPDIQF HFLPSQVIDH GRVPTQQEAY
QVHVGPMRGT SVGWLKLRSA NPQDHPVIQP NYLSTETDIE DFRLCVKLTR EIFAQEALAP