ID A0A060WC27_ONCMY Unreviewed; 598 AA.
AC A0A060WC27;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=t-plasminogen activator {ECO:0000256|ARBA:ARBA00013193};
DE EC=3.4.21.68 {ECO:0000256|ARBA:ARBA00013193};
GN ORFNames=GSONMT00067688001 {ECO:0000313|EMBL:CDQ62744.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ62744.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ62744.1, ECO:0000313|Proteomes:UP000193380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; FR904416; CDQ62744.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060WC27; -.
DR STRING; 8022.A0A060WC27; -.
DR PaxDb; 8022-A0A060WC27; -.
DR Proteomes; UP000193380; Chromosome 6.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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; 2.10.70.10; Complement Module, domain 1; 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; 1.
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; SSF57603; FnI-like domain; 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 4: Predicted;
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|RuleBase:RU363034};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Plasminogen activation {ECO:0000256|ARBA:ARBA00023202};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000193380};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..598
FT /note="t-plasminogen activator"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001594741"
FT DOMAIN 78..116
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 122..204
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 212..294
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 349..594
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 322..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 396
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT ACT_SITE 445
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT ACT_SITE 546
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT DISULFID 38..66
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 64..74
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 82..93
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 87..104
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3,
FT ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 106..115
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3,
FT ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 123..204
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 144..186
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 175..199
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 213..294
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 234..276
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 265..289
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 336..469
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 381..397
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 389..458
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 483..552
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 515..531
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 542..570
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
SQ SEQUENCE 598 AA; 67121 MW; 2C32BF4EE4AF2C7A CRC64;
MARILGLLLF LSALCCSLAD NIELRRAKRG TRYYRARCVD GQSAAVRGYG DTWMRWRGQR
VEYCRCASQG RERCHYVPVI TCYQSRCYNG GTCKEAVYSS DFLCQCPPGF TGAQCEINTN
EKCVVGQGKG YRGTWSISRI GSECINWNST TLRGKKFTAK KPEANSLGLG NHNFCRNPDN
DTKPWCYVYK GNQIVWEFCT LSSCPADQRS VECVQASGQT YRGTKAVTKR GSSCLPWDSP
LITRKFYNAW RSDARQLGLG SHNFCRNPDG DLSPWCHVYK NMKLTWELCD ITKCSEYPVT
LIVVISVVCF LARRPTTITT LGPRAPTSNN NNRGTCGQRA DNNLPSFRIL GGARKSDITE
QPWQAAINVY RPRNKAHFFQ CGGVLIDSCW VLSAAHCFDD GFKPERLQVV LGRTFRKNSS
GSEQIFEVEK YWSHEKYNKT TFDNDIVLMK LKSDIGLCAV NAPEVLPACL PDPGLVLPDW
TECEISGYGK EKEFDAIYSE RVKRGHVRLW PQDRCVPHVL SERVVTSNML CAGDTRGLDD
ACKGDSGGPL VCPKDGRMTL MGLISWGDGC GKKDKPGVYT RVTQYTDWIS SKKQETSQ
//
