GenomeNet

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   26-NOV-2014, entry version 103.
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       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- SIMILARITY: Contains 1 EGF-like domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00076}.
CC   -!- SIMILARITY: Contains 1 fibronectin type-I domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00478}.
CC   -!- SIMILARITY: Contains 1 kringle domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00121}.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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       {ECO:0000255}.
FT   CHAIN        37    477       Salivary plasminogen activator alpha 1.
FT                                /FTId=PRO_0000028340.
FT   DOMAIN       40     82       Fibronectin type-I. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00478}.
FT   DOMAIN       83    121       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      128    209       Kringle. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00121}.
FT   DOMAIN      226    476       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
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       {ECO:0000250}.
FT   DISULFID     70     79       {ECO:0000250}.
FT   DISULFID     87     98       {ECO:0000250}.
FT   DISULFID     92    109       {ECO:0000250}.
FT   DISULFID    111    120       {ECO:0000250}.
FT   DISULFID    128    209       {ECO:0000250}.
FT   DISULFID    149    191       {ECO:0000250}.
FT   DISULFID    180    204       {ECO:0000250}.
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       {ECO:0000244|PDB:1A5I}.
FT   STRAND      240    245       {ECO:0000244|PDB:1A5I}.
FT   STRAND      248    251       {ECO:0000244|PDB:1A5I}.
FT   STRAND      254    263       {ECO:0000244|PDB:1A5I}.
FT   STRAND      266    269       {ECO:0000244|PDB:1A5I}.
FT   HELIX       271    273       {ECO:0000244|PDB:1A5I}.
FT   TURN        280    282       {ECO:0000244|PDB:1A5I}.
FT   STRAND      284    288       {ECO:0000244|PDB:1A5I}.
FT   STRAND      290    294       {ECO:0000244|PDB:1A5I}.
FT   STRAND      300    309       {ECO:0000244|PDB:1A5I}.
FT   TURN        315    317       {ECO:0000244|PDB:1A5I}.
FT   STRAND      323    328       {ECO:0000244|PDB:1A5I}.
FT   STRAND      330    332       {ECO:0000244|PDB:1A5I}.
FT   STRAND      358    364       {ECO:0000244|PDB:1A5I}.
FT   STRAND      366    370       {ECO:0000244|PDB:1A5I}.
FT   STRAND      379    385       {ECO:0000244|PDB:1A5I}.
FT   HELIX       388    390       {ECO:0000244|PDB:1A5I}.
FT   TURN        393    398       {ECO:0000244|PDB:1A5I}.
FT   STRAND      405    409       {ECO:0000244|PDB:1A5I}.
FT   STRAND      414    416       {ECO:0000244|PDB:1A5I}.
FT   STRAND      431    436       {ECO:0000244|PDB:1A5I}.
FT   STRAND      439    448       {ECO:0000244|PDB:1A5I}.
FT   STRAND      450    453       {ECO:0000244|PDB:1A5I}.
FT   STRAND      459    463       {ECO:0000244|PDB:1A5I}.
FT   HELIX       464    467       {ECO:0000244|PDB:1A5I}.
FT   HELIX       468    474       {ECO:0000244|PDB:1A5I}.
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
//
DBGET integrated database retrieval system