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Database: UniProt
Entry: P98119
LinkDB: P98119
Original site: P98119 
ID   URT1_DESRO              Reviewed;         477 AA.
AC   P98119;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-OCT-2013, entry version 99.
DE   RecName: Full=Salivary plasminogen activator alpha 1;
DE            EC=3.4.21.68;
DE   AltName: Full=DSPA alpha-1;
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).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RC   TISSUE=Salivary gland;
RX   PubMed=9354616; DOI=10.1021/bi971129x;
RA   Renatus M., Stubbs M.T., Huber R., Bringmann P., Donner P.,
RA   Schleuning W.-D., Bode W.;
RT   "Catalytic domain structure of vampire bat plasminogen activator: a
RT   molecular paradigm for proteolysis without activation cleavage.";
RL   Biochemistry 36:13483-13493(1997).
CC   -!- FUNCTION: Probably essential to support the feeding habits of this
CC       exclusively haematophagous animal. Potent thrombolytic agent.
CC   -!- CATALYTIC ACTIVITY: Specific cleavage of Arg-|-Val bond in
CC       plasminogen to form plasmin.
CC   -!- ENZYME 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   -!- SIMILARITY: Contains 1 EGF-like domain.
CC   -!- SIMILARITY: Contains 1 fibronectin type-I domain.
CC   -!- SIMILARITY: Contains 1 kringle domain.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
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DR   EMBL; M63987; AAA31591.1; -; mRNA.
DR   EMBL; M63986; AAA31592.1; -; mRNA.
DR   PIR; JS0597; JS0597.
DR   PDB; 1A5I; X-ray; 2.90 A; A=213-477.
DR   PDBsum; 1A5I; -.
DR   ProteinModelPortal; P98119; -.
DR   SMR; P98119; 37-127, 213-477.
DR   MEROPS; S01.239; -.
DR   UniCarbKB; P98119; -.
DR   HOVERGEN; HBG008633; -.
DR   EvolutionaryTrace; P98119; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.20.10; -; 1.
DR   InterPro; IPR000742; EG-like_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000083; Fibronectin_type1.
DR   InterPro; IPR000001; Kringle.
DR   InterPro; IPR013806; Kringle-like.
DR   InterPro; IPR018056; Kringle_CS.
DR   InterPro; IPR001254; Peptidase_S1.
DR   InterPro; IPR018114; Peptidase_S1_AS.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR009003; Trypsin-like_Pept_dom.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00039; fn1; 1.
DR   Pfam; PF00051; Kringle; 1.
DR   Pfam; PF00089; Trypsin; 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   3D-structure; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Hydrolase; Kringle; Plasminogen activation; Protease; Secreted;
KW   Serine protease; Signal.
FT   SIGNAL        1     36       Potential.
FT   CHAIN        37    477       Salivary plasminogen activator alpha 1.
FT                                /FTId=PRO_0000028340.
FT   DOMAIN       40     82       Fibronectin type-I.
FT   DOMAIN       83    121       EGF-like.
FT   DOMAIN      128    209       Kringle.
FT   DOMAIN      226    476       Peptidase S1.
FT   ACT_SITE    272    272       Charge relay system.
FT   ACT_SITE    321    321       Charge relay system.
FT   ACT_SITE    428    428       Charge relay system.
FT   CARBOHYD    153    153       N-linked (GlcNAc...).
FT                                /FTId=CAR_000027.
FT   CARBOHYD    398    398       N-linked (GlcNAc...).
FT                                /FTId=CAR_000028.
FT   DISULFID     42     72       By similarity.
FT   DISULFID     70     79       By similarity.
FT   DISULFID     87     98       By similarity.
FT   DISULFID     92    109       By similarity.
FT   DISULFID    111    120       By similarity.
FT   DISULFID    128    209       By similarity.
FT   DISULFID    149    191       By similarity.
FT   DISULFID    180    204       By similarity.
FT   DISULFID    214    345
FT   DISULFID    257    273
FT   DISULFID    265    334
FT   DISULFID    359    434
FT   DISULFID    391    407
FT   DISULFID    424    452
FT   HELIX       234    236
FT   STRAND      240    245
FT   STRAND      248    251
FT   STRAND      254    263
FT   STRAND      266    269
FT   HELIX       271    273
FT   TURN        280    282
FT   STRAND      284    288
FT   STRAND      290    294
FT   STRAND      300    309
FT   TURN        315    317
FT   STRAND      323    328
FT   STRAND      330    332
FT   STRAND      358    364
FT   STRAND      366    370
FT   STRAND      379    385
FT   HELIX       388    390
FT   TURN        393    398
FT   STRAND      405    409
FT   STRAND      414    416
FT   STRAND      431    436
FT   STRAND      439    448
FT   STRAND      450    453
FT   STRAND      459    463
FT   HELIX       464    467
FT   HELIX       468    474
SQ   SEQUENCE   477 AA;  53616 MW;  AA06FD1739C10E5E CRC64;
     MVNTMKTKLL CVLLLCGAVF SLPRQETYRQ LARGSRAYGV ACKDEITQMT YRRQESWLRP
     EVRSKRVEHC QCDRGQARCH TVPVNSCSEP RCFNGGTCWQ AVYFSDFVCQ CPAGYTGKRC
     EVDTRATCYE GQGVTYRGTW STAESRVECI NWNSSLLTRR TYNGRMPDAF NLGLGNHNYC
     RNPNGAPKPW CYVIKAGKFT SESCSVPVCS KATCGLRKYK EPQLHSTGGL FTDITSHPWQ
     AAIFAQNRRS SGERFLCGGI LISSCWVLTA AHCFQESYLP DQLKVVLGRT YRVKPGEEEQ
     TFKVKKYIVH KEFDDDTYNN DIALLQLKSD SPQCAQESDS VRAICLPEAN LQLPDWTECE
     LSGYGKHKSS SPFYSEQLKE GHVRLYPSSR CAPKFLFNKT VTNNMLCAGD TRSGEIYPNV
     HDACQGDSGG PLVCMNDNHM TLLGIISWGV GCGEKDVPGV YTKVTNYLGW IRDNMHL
//
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