URTB_DESRO
ID URTB_DESRO Reviewed; 431 AA.
AC P98121;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Salivary plasminogen activator beta;
DE EC=3.4.21.68;
DE AltName: Full=DSPA beta;
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}.
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DR EMBL; M63989; AAA31594.1; -; mRNA.
DR PIR; JS0599; JS0599.
DR AlphaFoldDB; P98121; -.
DR SMR; P98121; -.
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; 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; 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; 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; 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; 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; EGF-like domain; Glycoprotein; Hydrolase; Kringle;
KW Plasminogen activation; Protease; Secreted; Serine protease; Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..431
FT /note="Salivary plasminogen activator beta"
FT /id="PRO_0000028342"
FT DOMAIN 37..75
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 82..163
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 180..430
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 382
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..52
FT /evidence="ECO:0000250"
FT DISULFID 46..63
FT /evidence="ECO:0000250"
FT DISULFID 65..74
FT /evidence="ECO:0000250"
FT DISULFID 82..163
FT /evidence="ECO:0000250"
FT DISULFID 103..145
FT /evidence="ECO:0000250"
FT DISULFID 134..158
FT /evidence="ECO:0000250"
FT DISULFID 168..299
FT /evidence="ECO:0000250"
FT DISULFID 211..227
FT /evidence="ECO:0000250"
FT DISULFID 219..288
FT /evidence="ECO:0000250"
FT DISULFID 313..388
FT /evidence="ECO:0000250"
FT DISULFID 345..361
FT /evidence="ECO:0000250"
FT DISULFID 378..406
FT /evidence="ECO:0000250"
SQ SEQUENCE 431 AA; 48222 MW; 699B5E675B162CBF CRC64;
MVNTMKTKLL CVLLLCGAVF SLPRQETYRQ LARGSRAYGG CSELRCFNGG TCWQAASFSD
FVCQCPKGYT GKQCEVDTHA TCYKDQGVTY RGTWSTSESG AQCINWNSNL LTRRTYNGRR
SDAITLGLGN HNYCRNPDNN SKPWCYVIKA SKFILEFCSV PVCSKATCGL RKYKEPQLHS
TGGLFTDITS HPWQAAIFAQ NRRSSGERFL CGGILISSCW VLTAAHCFQE RYPPQHLRVV
LGRTYRVKPG KEEQTFEVEK CIIHEEFDDD TYNNDIALLQ LKSGSPQCAQ ESDSVRAICL
PEANLQLPDW TECELSGYGK HKSSSPFYSE QLKEGHVRLY PSSRCTSKFL FNKTVTNNML
CAGDTRSGEI YPNVHDACQG DSGGPLVCMN DNHMTLLGII SWGVGCGEKD IPGVYTKVTN
YLGWIRDNMR P
