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Salivary plasminogen activator alpha 1 (EC 3.4.21.68) (DSPA alpha-1)

 URT1_DESRO              Reviewed;         477 AA.
P98119;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
12-SEP-2018, entry version 123.
RecName: Full=Salivary plasminogen activator alpha 1;
EC=3.4.21.68;
AltName: Full=DSPA alpha-1;
Flags: Precursor;
Desmodus rotundus (Vampire bat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera;
Phyllostomidae; Desmodontinae; Desmodus.
NCBI_TaxID=9430;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Salivary gland;
PubMed=1937019; DOI=10.1016/0378-1119(91)90155-5;
Kraetzschmar J., Haendler B., Langer G., Boidol W., Bringmann P.,
Alagon A., Donner P., Schleuning W.-D.;
"The plasminogen activator family from the salivary gland of the
vampire bat Desmodus rotundus: cloning and expression.";
Gene 105:229-237(1991).
[2]
CHARACTERIZATION.
PubMed=1309059; DOI=10.1111/j.1749-6632.1992.tb51639.x;
Schleuning W.-D., Alagon A., Boidol W., Bringmann P., Petri T.,
Kraetzschmar J., Haendler B., Langer G., Baldus B., Witt W.,
Donner P.;
"Plasminogen activators from the saliva of Desmodus rotundus (common
vampire bat): unique fibrin specificity.";
Ann. N. Y. Acad. Sci. 667:395-403(1992).
[3]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
TISSUE=Salivary gland;
PubMed=9354616; DOI=10.1021/bi971129x;
Renatus M., Stubbs M.T., Huber R., Bringmann P., Donner P.,
Schleuning W.-D., Bode W.;
"Catalytic domain structure of vampire bat plasminogen activator: a
molecular paradigm for proteolysis without activation cleavage.";
Biochemistry 36:13483-13493(1997).
-!- FUNCTION: Probably essential to support the feeding habits of this
exclusively haematophagous animal. Potent thrombolytic agent.
-!- CATALYTIC ACTIVITY: Specific cleavage of Arg-|-Val bond in
plasminogen to form plasmin.
-!- ACTIVITY REGULATION: Activity toward plasminogen is stimulated in
the presence of fibrin I.
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Secreted.
-!- DOMAIN: The fibronectin type-I domain mediates binding to fibrin,
and the kringle domain apparently mediates fibrin-induced
stimulation of activity.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-----------------------------------------------------------------------
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EMBL; M63987; AAA31591.1; -; mRNA.
EMBL; M63986; AAA31592.1; -; mRNA.
PIR; JS0597; JS0597.
PDB; 1A5I; X-ray; 2.90 A; A=213-477.
PDBsum; 1A5I; -.
ProteinModelPortal; P98119; -.
SMR; P98119; -.
ELM; P98119; -.
MEROPS; S01.239; -.
GlyConnect; 544; -.
UniCarbKB; P98119; -.
HOVERGEN; HBG008633; -.
EvolutionaryTrace; P98119; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0031639; P:plasminogen activation; IEA:InterPro.
CDD; cd00061; FN1; 1.
CDD; cd00108; KR; 1.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.20.10; -; 1.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000083; Fibronectin_type1.
InterPro; IPR000001; Kringle.
InterPro; IPR013806; Kringle-like.
InterPro; IPR018056; Kringle_CS.
InterPro; IPR038178; Kringle_sf.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR026280; Tissue_plasm_act.
InterPro; IPR034811; tPA.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR44617; PTHR44617; 2.
Pfam; PF00008; EGF; 1.
Pfam; PF00039; fn1; 1.
Pfam; PF00051; Kringle; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001145; Tissue_plasm_act; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00181; EGF; 1.
SMART; SM00179; EGF_CA; 1.
SMART; SM00058; FN1; 1.
SMART; SM00130; KR; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57440; SSF57440; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS01253; FN1_1; 1.
PROSITE; PS51091; FN1_2; 1.
PROSITE; PS00021; KRINGLE_1; 1.
PROSITE; PS50070; KRINGLE_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Disulfide bond; EGF-like domain; Glycoprotein;
Hydrolase; Kringle; Plasminogen activation; Protease; Secreted;
Serine protease; Signal.
SIGNAL 1 36 {ECO:0000255}.
CHAIN 37 477 Salivary plasminogen activator alpha 1.
/FTId=PRO_0000028340.
DOMAIN 40 82 Fibronectin type-I. {ECO:0000255|PROSITE-
ProRule:PRU00478}.
DOMAIN 83 121 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 128 209 Kringle. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 226 476 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 272 272 Charge relay system.
ACT_SITE 321 321 Charge relay system.
ACT_SITE 428 428 Charge relay system.
CARBOHYD 153 153 N-linked (GlcNAc...) asparagine.
/FTId=CAR_000027.
CARBOHYD 398 398 N-linked (GlcNAc...) asparagine.
/FTId=CAR_000028.
DISULFID 42 72 {ECO:0000250}.
DISULFID 70 79 {ECO:0000250}.
DISULFID 87 98 {ECO:0000250}.
DISULFID 92 109 {ECO:0000250}.
DISULFID 111 120 {ECO:0000250}.
DISULFID 128 209 {ECO:0000250}.
DISULFID 149 191 {ECO:0000250}.
DISULFID 180 204 {ECO:0000250}.
DISULFID 214 345
DISULFID 257 273
DISULFID 265 334
DISULFID 359 434
DISULFID 391 407
DISULFID 424 452
HELIX 234 236 {ECO:0000244|PDB:1A5I}.
STRAND 240 245 {ECO:0000244|PDB:1A5I}.
STRAND 248 251 {ECO:0000244|PDB:1A5I}.
STRAND 254 263 {ECO:0000244|PDB:1A5I}.
STRAND 266 269 {ECO:0000244|PDB:1A5I}.
HELIX 271 273 {ECO:0000244|PDB:1A5I}.
TURN 280 282 {ECO:0000244|PDB:1A5I}.
STRAND 284 288 {ECO:0000244|PDB:1A5I}.
STRAND 290 294 {ECO:0000244|PDB:1A5I}.
STRAND 300 309 {ECO:0000244|PDB:1A5I}.
TURN 315 317 {ECO:0000244|PDB:1A5I}.
STRAND 323 328 {ECO:0000244|PDB:1A5I}.
STRAND 330 332 {ECO:0000244|PDB:1A5I}.
STRAND 358 364 {ECO:0000244|PDB:1A5I}.
STRAND 366 370 {ECO:0000244|PDB:1A5I}.
STRAND 379 385 {ECO:0000244|PDB:1A5I}.
HELIX 388 390 {ECO:0000244|PDB:1A5I}.
TURN 393 398 {ECO:0000244|PDB:1A5I}.
STRAND 405 409 {ECO:0000244|PDB:1A5I}.
STRAND 414 416 {ECO:0000244|PDB:1A5I}.
STRAND 431 436 {ECO:0000244|PDB:1A5I}.
STRAND 439 448 {ECO:0000244|PDB:1A5I}.
STRAND 450 453 {ECO:0000244|PDB:1A5I}.
STRAND 459 463 {ECO:0000244|PDB:1A5I}.
HELIX 464 467 {ECO:0000244|PDB:1A5I}.
HELIX 468 474 {ECO:0000244|PDB:1A5I}.
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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