URT2_DESRO
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 25-MAY-2022, entry version 132.
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; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC 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 vampire
RT 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; DOI=10.1016/s0021-9258(19)84664-1;
RA Gardell S.J., Duong L.T., Diehl R.E., York J.D., Hare T.R., Register R.B.,
RA Jacobs J.W., Dixon R.A.F., Friedman P.A.;
RT "Isolation, characterization, and cDNA cloning of a vampire bat salivary
RT 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., 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 agent.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form
CC plasmin.; EC=3.4.21.68;
CC -!- ACTIVITY REGULATION: Activity toward plasminogen is stimulated in the
CC presence of fibrin I.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: The fibronectin type-I domain mediates binding to fibrin, and
CC the kringle domain apparently mediates fibrin-induced stimulation of
CC activity.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; M63988; AAA31593.1; -; mRNA.
DR EMBL; J05082; AAA31596.1; -; mRNA.
DR PIR; A34369; A34369.
DR PIR; JS0598; JS0598.
DR AlphaFoldDB; P15638; -.
DR SMR; P15638; -.
DR MEROPS; S01.239; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0031639; P:plasminogen activation; IEA:InterPro.
DR GO; GO:0014909; P:smooth muscle cell migration; IEA:InterPro.
DR CDD; cd00061; FN1; 1.
DR CDD; cd00108; KR; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.40.20.10; -; 1.
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; IPR043504; Peptidase_S1_PA_chymotrypsin.
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; PTHR24264:SF42; PTHR24264:SF42; 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; Glycoprotein;
KW Hydrolase; Kringle; Plasminogen activation; Protease; Secreted;
KW Serine protease; Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..477
FT /note="Salivary plasminogen activator alpha 2"
FT /id="PRO_0000028341"
FT DOMAIN 40..82
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 83..121
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 128..209
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 226..476
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 272
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 321
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 428
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..72
FT /evidence="ECO:0000250"
FT DISULFID 70..79
FT /evidence="ECO:0000250"
FT DISULFID 87..98
FT /evidence="ECO:0000250"
FT DISULFID 92..109
FT /evidence="ECO:0000250"
FT DISULFID 111..120
FT /evidence="ECO:0000250"
FT DISULFID 128..209
FT /evidence="ECO:0000250"
FT DISULFID 149..191
FT /evidence="ECO:0000250"
FT DISULFID 180..204
FT /evidence="ECO:0000250"
FT DISULFID 214..345
FT /evidence="ECO:0000250"
FT DISULFID 257..273
FT /evidence="ECO:0000250"
FT DISULFID 265..334
FT /evidence="ECO:0000250"
FT DISULFID 359..434
FT /evidence="ECO:0000250"
FT DISULFID 391..407
FT /evidence="ECO:0000250"
FT DISULFID 424..452
FT /evidence="ECO:0000250"
FT CONFLICT 403
FT /note="N -> K (in Ref. 2; AAA31596)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="Y -> H (in Ref. 2; AAA31596)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="M -> R (in Ref. 2; AAA31596)"
FT /evidence="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
