ID A0A3Q2G1T0_CYPVA Unreviewed; 563 AA.
AC A0A3Q2G1T0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Plasminogen activator {ECO:0000256|PIRNR:PIRNR001145};
DE EC=3.4.21.68 {ECO:0000256|PIRNR:PIRNR001145};
GN Name=PLAT {ECO:0000313|Ensembl:ENSCVAP00000015830.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000015830.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000015830.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form
CC plasmin.; EC=3.4.21.68; Evidence={ECO:0000256|ARBA:ARBA00001538,
CC ECO:0000256|PIRNR:PIRNR001145};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|PIRNR:PIRNR001145}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_015238032.1; XM_015382546.1.
DR AlphaFoldDB; A0A3Q2G1T0; -.
DR Ensembl; ENSCVAT00000031680.1; ENSCVAP00000015830.1; ENSCVAG00000018691.1.
DR GeneID; 107089642; -.
DR CTD; 5327; -.
DR GeneTree; ENSGT00940000158930; -.
DR OMA; WCYIFKA; -.
DR OrthoDB; 4629979at2759; -.
DR Proteomes; UP000265020; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0031639; P:plasminogen activation; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00108; KR; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR026280; Tissue_plasm_act.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24264:SF42; TISSUE-TYPE PLASMINOGEN ACTIVATOR; 1.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00051; Kringle; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001145; Tissue_plasm_act; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00130; KR; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57440; Kringle-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS00021; KRINGLE_1; 2.
DR PROSITE; PS50070; KRINGLE_2; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Digestion {ECO:0000256|ARBA:ARBA00022757};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR001145-3};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001145};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Plasminogen activation {ECO:0000256|ARBA:ARBA00023202,
KW ECO:0000256|PIRNR:PIRNR001145};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR001145};
KW Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW Secreted {ECO:0000256|PIRNR:PIRNR001145};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR001145};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..563
FT /note="Plasminogen activator"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018758297"
FT DOMAIN 60..98
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 104..186
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 193..275
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 315..559
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 361
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT ACT_SITE 410
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT ACT_SITE 511
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT DISULFID 64..75
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 69..86
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3,
FT ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 88..97
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3,
FT ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 105..186
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 126..168
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 157..181
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 194..275
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 215..257
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 246..270
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 300..434
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 346..362
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 354..423
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 448..517
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 480..496
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 507..535
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
SQ SEQUENCE 563 AA; 63211 MW; F7E4163046A68AAF CRC64;
MRSLIQGIFI LSALCCSLAD NVEVLRTKRG TRFYRGEPAR QPARRTLLIV QLKKPSPSYE
TSYCYVSQCY NGGTCKEAVY SSDYICQCPP GFSGTQCEIN TNEKCIVGQG EGYRGTRSIS
QTGAECINWN STTLRGRRFT ARKSDARSLG LGNHNFCRNP DQDSLPWCFI YKGTQIGWEY
CSLPKCPQDN NTECAVGLGQ NYRGTASVTN SGSTCLPWDS PVVRRKLNNA WRSNALELGL
SNHNFCRNPD GDEAPWCHTY KNMLLTWEHC DIPKCSKRPS VITTPGIRAP TTNNNNGATC
GKRLDNTLNR RAFRMFGGRY SDITEQPWQA LINVYQARLR KHFHRCGGVL IDSCWVLSAA
HCFEISDKAD KLEVVLGRTF RKQNSSSEQI FKVEKYWIHE KFNYETFDND IAILKLQTDI
GICAVDSPEV HPACLPESGL VLPDWTECEI SGYGKNSEFS DEYSEQVKRG HVRLWPKERC
VPEVLSGRTV TSNMLCAGDT RGLDDACKGD SGGPLVCRNK DRMTLMGVIS WGDGCGQKDK
PGVYTRVSHY IDWINDIIKA NPV
//
