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Database: UniProt
Entry: P98121
LinkDB: P98121
Original site: P98121 
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   05-DEC-2018, entry version 111.
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;
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   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   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; M63989; AAA31594.1; -; mRNA.
DR   PIR; JS0599; JS0599.
DR   ProteinModelPortal; P98121; -.
DR   SMR; P98121; -.
DR   MEROPS; S01.232; -.
DR   PRIDE; P98121; -.
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; 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; 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; 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       {ECO:0000255}.
FT   CHAIN        37    431       Salivary plasminogen activator beta.
FT                                /FTId=PRO_0000028342.
FT   DOMAIN       37     75       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       82    163       Kringle. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00121}.
FT   DOMAIN      180    430       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    226    226       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    275    275       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    382    382       Charge relay system. {ECO:0000250}.
FT   CARBOHYD    139    139       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    352    352       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     41     52       {ECO:0000250}.
FT   DISULFID     46     63       {ECO:0000250}.
FT   DISULFID     65     74       {ECO:0000250}.
FT   DISULFID     82    163       {ECO:0000250}.
FT   DISULFID    103    145       {ECO:0000250}.
FT   DISULFID    134    158       {ECO:0000250}.
FT   DISULFID    168    299       {ECO:0000250}.
FT   DISULFID    211    227       {ECO:0000250}.
FT   DISULFID    219    288       {ECO:0000250}.
FT   DISULFID    313    388       {ECO:0000250}.
FT   DISULFID    345    361       {ECO:0000250}.
FT   DISULFID    378    406       {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
//
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