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Database: UniProt
Entry: V8NWH8_OPHHA
LinkDB: V8NWH8_OPHHA
Original site: V8NWH8_OPHHA 
ID   V8NWH8_OPHHA            Unreviewed;       368 AA.
AC   V8NWH8;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Urokinase-type plasminogen activator {ECO:0000256|ARBA:ARBA00019414};
DE            EC=3.4.21.73 {ECO:0000256|ARBA:ARBA00013183};
DE   Flags: Fragment;
GN   Name=PLAU {ECO:0000313|EMBL:ETE66008.1};
GN   ORFNames=L345_08212 {ECO:0000313|EMBL:ETE66008.1};
OS   Ophiophagus hannah (King cobra) (Naja hannah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX   NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE66008.1, ECO:0000313|Proteomes:UP000018936};
RN   [1] {ECO:0000313|EMBL:ETE66008.1, ECO:0000313|Proteomes:UP000018936}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Blood {ECO:0000313|EMBL:ETE66008.1};
RX   PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA   Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA   McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA   Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA   de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA   Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA   Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA   Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT   "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT   snake venom system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC   -!- FUNCTION: Specifically cleaves the zymogen plasminogen to form the
CC       active enzyme plasmin. {ECO:0000256|ARBA:ARBA00004018}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form
CC         plasmin.; EC=3.4.21.73; Evidence={ECO:0000256|ARBA:ARBA00000942};
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000256|ARBA:ARBA00009228}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETE66008.1}.
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DR   EMBL; AZIM01001690; ETE66008.1; -; Genomic_DNA.
DR   AlphaFoldDB; V8NWH8; -.
DR   Proteomes; UP000018936; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035821; P:modulation of process of another organism; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00108; KR; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000001; Kringle.
DR   InterPro; IPR013806; Kringle-like.
DR   InterPro; IPR018056; Kringle_CS.
DR   InterPro; IPR038178; Kringle_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR   PANTHER; PTHR24264:SF38; UROKINASE-TYPE PLASMINOGEN ACTIVATOR; 1.
DR   Pfam; PF00051; Kringle; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00018; KRINGLE.
DR   SMART; SM00130; KR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57440; Kringle-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS00021; KRINGLE_1; 1.
DR   PROSITE; PS50070; KRINGLE_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Kinase {ECO:0000313|EMBL:ETE66008.1};
KW   Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW   ProRule:PRU00121}; Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Transferase {ECO:0000313|EMBL:ETE66008.1}.
FT   DOMAIN          1..33
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          39..121
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          140..357
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        23..32
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ETE66008.1"
SQ   SEQUENCE   368 AA;  41143 MW;  71AE4D882321AA1A CRC64;
     CGCLNGGTCL TYGLFSQIKF CLCPEGYDGD HCEIDVETRC YTGDGTDYRG TESKNENGEK
     CMFWDSHLVK RRPYNAHMEN SLELGLGRHN YCRNPDGRSK PWCYVRKGYL TSTTSCDIPT
     CQNGRTCGQR NLSRNFKIVG GLTAPIESQP WIASIFHSRG NHGSDTSRLI VRLGRSATNA
     SNANDQEFSV ERLIIHEAFS QQNRDYNNDI ALIKIRSSSG QCAKESDIVK TICLPSDNLM
     LRDHSHCEVS GYGKQSKTAI YYSRVLKSAS VQLIPQSTCK GYYKGHKVNE NMLCASDPEW
     KTDSCSGDSG GPLTCMSNGR MLLYGIISWG DGCAKERKPG VYTRVSRYIP WIDANMNSIH
     FKSLYPPK
//
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