URT1_DESRO
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 25-MAY-2022, entry version 134.
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; 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).
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:
CC Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form
CC plasmin.; EC=3.4.21.68;
CC -!- ACTIVITY REGULATION: Activity toward plasminogen is stimulated in the
CC presence of fibrin I.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: The fibronectin type-I domain mediates binding to fibrin, and
CC the kringle domain apparently mediates fibrin-induced stimulation of
CC activity.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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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 AlphaFoldDB; P98119; -.
DR SMR; P98119; -.
DR ELM; P98119; -.
DR MEROPS; S01.239; -.
DR GlyConnect; 544; 37 N-Linked glycans (2 sites).
DR EvolutionaryTrace; P98119; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; cd00061; FN1; 1.
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; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000083; Fibronectin_type1.
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; PF00039; fn1; 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; SM00179; EGF_CA; 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; Hydrolase;
KW Kringle; Plasminogen activation; Protease; Secreted; Serine protease;
KW Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..477
FT /note="Salivary plasminogen activator alpha 1"
FT /id="PRO_0000028340"
FT DOMAIN 40..82
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 83..121
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 128..209
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 226..476
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 272
FT /note="Charge relay system"
FT ACT_SITE 321
FT /note="Charge relay system"
FT ACT_SITE 428
FT /note="Charge relay system"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /id="CAR_000027"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /id="CAR_000028"
FT DISULFID 42..72
FT /evidence="ECO:0000250"
FT DISULFID 70..79
FT /evidence="ECO:0000250"
FT DISULFID 87..98
FT /evidence="ECO:0000250"
FT DISULFID 92..109
FT /evidence="ECO:0000250"
FT DISULFID 111..120
FT /evidence="ECO:0000250"
FT DISULFID 128..209
FT /evidence="ECO:0000250"
FT DISULFID 149..191
FT /evidence="ECO:0000250"
FT DISULFID 180..204
FT /evidence="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
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 254..263
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:1A5I"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:1A5I"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 300..309
FT /evidence="ECO:0007829|PDB:1A5I"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 379..385
FT /evidence="ECO:0007829|PDB:1A5I"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:1A5I"
FT TURN 393..398
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 439..448
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 450..453
FT /evidence="ECO:0007829|PDB:1A5I"
FT STRAND 459..463
FT /evidence="ECO:0007829|PDB:1A5I"
FT HELIX 464..467
FT /evidence="ECO:0007829|PDB:1A5I"
FT HELIX 468..474
FT /evidence="ECO:0007829|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
