URTG_DESRO
ID URTG_DESRO Reviewed; 394 AA.
AC P49150;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Salivary plasminogen activator gamma;
DE EC=3.4.21.68;
DE AltName: Full=DSPA gamma;
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 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 -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M63990; AAA31595.1; -; mRNA.
DR PIR; JS0600; JS0600.
DR AlphaFoldDB; P49150; -.
DR SMR; P49150; -.
DR MEROPS; S01.232; -.
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; 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; 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; 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; PF00051; Kringle; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00130; KR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57440; SSF57440; 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 Disulfide bond; Glycoprotein; Hydrolase; Kringle; Plasminogen activation;
KW Protease; Secreted; Serine protease; Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..394
FT /note="Salivary plasminogen activator gamma"
FT /id="PRO_0000028343"
FT DOMAIN 45..126
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 143..393
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 189
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 238
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 345
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..126
FT /evidence="ECO:0000250"
FT DISULFID 66..108
FT /evidence="ECO:0000250"
FT DISULFID 97..121
FT /evidence="ECO:0000250"
FT DISULFID 131..262
FT /evidence="ECO:0000250"
FT DISULFID 174..190
FT /evidence="ECO:0000250"
FT DISULFID 182..251
FT /evidence="ECO:0000250"
FT DISULFID 276..351
FT /evidence="ECO:0000250"
FT DISULFID 308..324
FT /evidence="ECO:0000250"
FT DISULFID 341..369
FT /evidence="ECO:0000250"
SQ SEQUENCE 394 AA; 44105 MW; 9CCD6F52F3D81FCD CRC64;
MVNTMKTKLL CVLLLCGAVF SLPRQETYRQ LARGSRAYGD PHATCYKDQG VTYRGTWSTS
ESGAQCINWN SNLLIRRTYN GRMPEAVKLG LGNHNYCRNP DGASKPWCYV IKARKFTSES
CSVPVCSKAT CGLRKYKEPQ LHSTGGLFTD ITSHPWQAAI FAQNRRSSGE RFLCGGILIS
SCWVLTAAHC FQERYPPQHL RVVLGRTYRV KPGKEEQTFE VEKCIVHEEF DDDTYNNDIA
LLQLKSGSPQ CAQESDSVRA ICLPEANLQL PDWTECELSG YGKHKSSSPF YSEQLKEGHV
RLYPSSRCTS KFLFNKTVTN NMLCAGDTRS GEIYPNVHDA CQGDSGGPLV CMNDNHMTLL
GIISWGVGCG EKDIPGVYTK VTNYLGWIRD NMRP
