ID A0A8C5ICZ5_JUNHY Unreviewed; 558 AA.
AC A0A8C5ICZ5;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=Plasminogen activator {ECO:0000256|PIRNR:PIRNR001145};
DE EC=3.4.21.68 {ECO:0000256|PIRNR:PIRNR001145};
OS Junco hyemalis (Dark-eyed junco).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Passerellidae; Junco.
OX NCBI_TaxID=40217 {ECO:0000313|Ensembl:ENSJHYP00000002464.1, ECO:0000313|Proteomes:UP000694408};
RN [1] {ECO:0000313|Ensembl:ENSJHYP00000002464.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSJHYP00000002464.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) 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 {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|PIRNR:PIRNR001145}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A8C5ICZ5; -.
DR Ensembl; ENSJHYT00000003068.1; ENSJHYP00000002464.1; ENSJHYG00000002078.1.
DR OMA; WCYIFKA; -.
DR Proteomes; UP000694408; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:1901701; P:cellular response to oxygen-containing compound; IEA:UniProtKB-ARBA.
DR GO; GO:0031639; P:plasminogen activation; IEA:InterPro.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:TreeGrafter.
DR GO; GO:0033993; P:response to lipid; IEA:UniProtKB-ARBA.
DR GO; GO:0014909; P:smooth muscle cell migration; IEA:TreeGrafter.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00108; KR; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR FunFam; 2.40.10.10:FF:000003; Transmembrane serine protease 3; 1.
DR FunFam; 2.40.20.10:FF:000001; Urokinase-type plasminogen activator; 2.
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.
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; IPR050127; Serine_Proteases_S1.
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; 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; SM00058; FN1; 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; PS01253; FN1_1; 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 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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000694408};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, 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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..558
FT /note="Plasminogen activator"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034341504"
FT DOMAIN 82..121
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 127..209
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 216..298
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 313..557
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 359
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT ACT_SITE 408
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT ACT_SITE 509
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT DISULFID 43..71
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 69..78
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 86..97
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 91..109
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 111..120
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3,
FT ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 128..209
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 149..191
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 180..204
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 217..298
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 238..280
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 269..293
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 301..432
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 344..360
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 352..421
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 446..515
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 478..494
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 505..533
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
SQ SEQUENCE 558 AA; 62609 MW; AA9AFA2D2C596A28 CRC64;
MWKTLRMEGK LPCLLLLVGA IMTAQCQGLR TRFKRGARSR AICTDNSSAE IYQHGGIWLR
LSGSRIEYCR CDSGRSWCHT VPATVCTRNK CYNGGQCSQA YYSPQLFICQ CQPGFSGKQC
EIDTGVKCYK DTGVTYRGTW STTESGAECL NWNSDGLVNR RYSGHREDAA ELGLGNHNYC
RNPDEDSRPW CYIYKGGRYT WEHCSVPSCS KVRNTNCSSG RGTDYRGSHS VTSSGATCLK
WNSLILINKV YTAWRRDAYQ LGLGSHNFCR NPDNDSKPWC HVLKGNQLTW EYCNVPNCST
CGLRQRRARQ FRIKGGSSTD IAAHPWQAAI FVKYHRVAGE HFLCGGILIS SCWVLSAAHC
FEEGFRTNQL KIVLGRTSRA TPEENEQTFQ VKKYIVHQRF DPETFNNDIA LLQLGSDAEE
CAVATGTVGT ACLPSPELQL PDWTECEISG YGKSEEFSPF YSEHLKEGHV RLFPASRCTA
QHLDNRTVTE NMICAGDTRN LDDACKGDSG GPLVCLKDER MYLIGIISWG IGCGRKDIPG
VYTKVIRYLG WIQDTMKL
//
