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Database: UniProt
Entry: P15638
LinkDB: P15638
Original site: P15638 
ID   URT2_DESRO              Reviewed;         477 AA.
AC   P15638;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   05-DEC-2018, entry version 125.
DE   RecName: Full=Salivary plasminogen activator alpha 2;
DE            EC=3.4.21.68;
DE   AltName: Full=BAT-PA;
DE   AltName: Full=DSPA alpha-2;
DE   AltName: Full=T-plasminogen activator;
DE   Flags: Precursor;
OS   Desmodus rotundus (Vampire bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera;
OC   Phyllostomidae; Desmodontinae; Desmodus.
OX   NCBI_TaxID=9430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=1937019; DOI=10.1016/0378-1119(91)90155-5;
RA   Kraetzschmar J., Haendler B., Langer G., Boidol W., Bringmann P.,
RA   Alagon A., Donner P., Schleuning W.-D.;
RT   "The plasminogen activator family from the salivary gland of the
RT   vampire bat Desmodus rotundus: cloning and expression.";
RL   Gene 105:229-237(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Salivary gland;
RX   PubMed=2509450;
RA   Gardell S.J., Duong L.T., Diehl R.E., York J.D., Hare T.R.,
RA   Register R.B., Jacobs J.W., Dixon R.A.F., Friedman P.A.;
RT   "Isolation, characterization, and cDNA cloning of a vampire bat
RT   salivary plasminogen activator.";
RL   J. Biol. Chem. 264:17947-17952(1989).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=1309059; DOI=10.1111/j.1749-6632.1992.tb51639.x;
RA   Schleuning W.-D., Alagon A., Boidol W., Bringmann P., Petri T.,
RA   Kraetzschmar J., Haendler B., Langer G., Baldus B., Witt W.,
RA   Donner P.;
RT   "Plasminogen activators from the saliva of Desmodus rotundus (common
RT   vampire bat): unique fibrin specificity.";
RL   Ann. N. Y. Acad. Sci. 667:395-403(1992).
CC   -!- FUNCTION: Probably essential to support the feeding habits of this
CC       exclusively haematophagous animal. Probable potent thrombolytic
CC       agent.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to
CC         form plasmin.; EC=3.4.21.68;
CC   -!- ACTIVITY REGULATION: Activity toward plasminogen is stimulated in
CC       the presence of fibrin I.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DOMAIN: The fibronectin type-I domain mediates binding to fibrin,
CC       and the kringle domain apparently mediates fibrin-induced
CC       stimulation of activity.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; M63988; AAA31593.1; -; mRNA.
DR   EMBL; J05082; AAA31596.1; -; mRNA.
DR   PIR; A34369; A34369.
DR   PIR; JS0598; JS0598.
DR   ProteinModelPortal; P15638; -.
DR   SMR; P15638; -.
DR   MEROPS; S01.239; -.
DR   PRIDE; P15638; -.
DR   HOVERGEN; HBG008633; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0031639; P:plasminogen activation; IEA:InterPro.
DR   CDD; cd00061; FN1; 1.
DR   CDD; cd00108; KR; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.20.10; -; 1.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000083; Fibronectin_type1.
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; IPR001314; Peptidase_S1A.
DR   InterPro; IPR026280; Tissue_plasm_act.
DR   InterPro; IPR034811; tPA.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR44617; PTHR44617; 2.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00039; fn1; 1.
DR   Pfam; PF00051; Kringle; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001145; Tissue_plasm_act; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00058; FN1; 1.
DR   SMART; SM00130; KR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57440; SSF57440; 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; 1.
DR   PROSITE; PS50070; KRINGLE_2; 1.
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   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Hydrolase; Kringle; Plasminogen activation; Protease;
KW   Secreted; Serine protease; Signal.
FT   SIGNAL        1     36       {ECO:0000255}.
FT   CHAIN        37    477       Salivary plasminogen activator alpha 2.
FT                                /FTId=PRO_0000028341.
FT   DOMAIN       40     82       Fibronectin type-I. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00478}.
FT   DOMAIN       83    121       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      128    209       Kringle. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00121}.
FT   DOMAIN      226    476       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    272    272       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    321    321       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    428    428       Charge relay system. {ECO:0000250}.
FT   CARBOHYD    185    185       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    398    398       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     42     72       {ECO:0000250}.
FT   DISULFID     70     79       {ECO:0000250}.
FT   DISULFID     87     98       {ECO:0000250}.
FT   DISULFID     92    109       {ECO:0000250}.
FT   DISULFID    111    120       {ECO:0000250}.
FT   DISULFID    128    209       {ECO:0000250}.
FT   DISULFID    149    191       {ECO:0000250}.
FT   DISULFID    180    204       {ECO:0000250}.
FT   DISULFID    214    345       {ECO:0000250}.
FT   DISULFID    257    273       {ECO:0000250}.
FT   DISULFID    265    334       {ECO:0000250}.
FT   DISULFID    359    434       {ECO:0000250}.
FT   DISULFID    391    407       {ECO:0000250}.
FT   DISULFID    424    452       {ECO:0000250}.
FT   CONFLICT    403    403       N -> K (in Ref. 2; AAA31596).
FT                                {ECO:0000305}.
FT   CONFLICT    417    417       Y -> H (in Ref. 2; AAA31596).
FT                                {ECO:0000305}.
FT   CONFLICT    435    435       M -> R (in Ref. 2; AAA31596).
FT                                {ECO:0000305}.
SQ   SEQUENCE   477 AA;  53719 MW;  17486555C0E5077C CRC64;
     MVNTMKTKLL CVLLLCGAVF SLPRQETYRQ LARGSRAYGV ACRDEKTQMI YQQQESWLRP
     EVRSKRVEHC RCDRGLAQCH TVPVKSCSEL RCFNGGTCWQ AASFSDFVCQ CPKGYTGKQC
     EVDTHATCYK DQGVTYRGTW STSESGAQCI NWNSNLLTRR TYNGRRSDAI TLGLGNHNYC
     RNPDNNSKPW CYVIKASKFI LEFCSVPVCS KATCGLRKYK EPQLHSTGGL FTDITSHPWQ
     AAIFAQNRRS SGERFLCGGI LISSCWVLTA AHCFQERYPP QHLRVVLGRT YRVKPGKEEQ
     TFEVEKCIVH EEFDDDTYNN DIALLQLKSG SPQCAQESDS VRAICLPEAN LQLPDWTECE
     LSGYGKHKSS SPFYSEQLKE GHVRLYPSSR CTSKFLFNKT VTNNMLCAGD TRSGEIYPNV
     HDACQGDSGG PLVCMNDNHM TLLGIISWGV GCGEKDIPGV YTKVTNYLGW IRDNMRP
//
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