ID F1NWX6_CHICK Unreviewed; 802 AA.
AC F1NWX6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Plasminogen {ECO:0000256|ARBA:ARBA00020043, ECO:0000256|PIRNR:PIRNR001150};
DE EC=3.4.21.7 {ECO:0000256|ARBA:ARBA00012184, ECO:0000256|PIRNR:PIRNR001150};
GN Name=PLG {ECO:0000313|Ensembl:ENSGALP00010009576.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00010009576.1, ECO:0000313|Proteomes:UP000000539};
RN [1] {ECO:0000313|Ensembl:ENSGALP00010009576.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010009576.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a
CC proteolytic factor in a variety of other processes including embryonic
CC development, tissue remodeling, tumor invasion, and inflammation. In
CC ovulation, weakens the walls of the Graafian follicle. It activates the
CC urokinase-type plasminogen activator, collagenases and several
CC complement zymogens, such as C1 and C5. Cleavage of fibronectin and
CC laminin leads to cell detachment and apoptosis. Also cleaves fibrin,
CC thrombospondin and von Willebrand factor. Its role in tissue remodeling
CC and tumor invasion may be modulated by CSPG4. Binds to cells.
CC {ECO:0000256|ARBA:ARBA00025229, ECO:0000256|PIRNR:PIRNR001150}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher
CC selectivity than trypsin. Converts fibrin into soluble products.;
CC EC=3.4.21.7; Evidence={ECO:0000256|ARBA:ARBA00000717,
CC ECO:0000256|PIRNR:PIRNR001150};
CC -!- ACTIVITY REGULATION: Converted into plasmin by plasminogen activators,
CC both plasminogen and its activator being bound to fibrin.
CC {ECO:0000256|PIRNR:PIRNR001150}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|PIRNR:PIRNR001150}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC {ECO:0000256|PIRNR:PIRNR001150}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR RefSeq; XP_419618.2; XM_419618.5.
DR AlphaFoldDB; F1NWX6; -.
DR SMR; F1NWX6; -.
DR STRING; 9031.ENSGALP00000006818; -.
DR PaxDb; 9031-ENSGALP00000006818; -.
DR Ensembl; ENSGALT00010017241.1; ENSGALP00010009576.1; ENSGALG00010007226.1.
DR GeneID; 421580; -.
DR KEGG; gga:421580; -.
DR CTD; 5340; -.
DR VEuPathDB; HostDB:geneid_421580; -.
DR GeneTree; ENSGT00940000155208; -.
DR InParanoid; F1NWX6; -.
DR OMA; NSQTPHA; -.
DR OrthoDB; 211181at2759; -.
DR Reactome; R-GGA-114608; Platelet degranulation.
DR Reactome; R-GGA-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-GGA-186797; Signaling by PDGF.
DR Reactome; R-GGA-75205; Dissolution of Fibrin Clot.
DR Reactome; R-GGA-8964041; LDL remodeling.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000004293; Expressed in liver and 6 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-UniRule.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-UniRule.
DR CDD; cd00108; KR; 5.
DR CDD; cd01099; PAN_AP_HGF; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 4.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR023317; Pept_S1A_plasmin.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24261:SF13; PLASMINOGEN; 1.
DR PANTHER; PTHR24261; PLASMINOGEN-RELATED; 1.
DR Pfam; PF00051; Kringle; 5.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001150; Plasmin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00130; KR; 5.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57414; Hairpin loop containing domain-like; 1.
DR SUPFAM; SSF57440; Kringle-like; 5.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00021; KRINGLE_1; 5.
DR PROSITE; PS50070; KRINGLE_2; 5.
DR PROSITE; PS50948; PAN; 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 Blood coagulation {ECO:0000256|ARBA:ARBA00023084,
KW ECO:0000256|PIRNR:PIRNR001150};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Fibrinolysis {ECO:0000256|ARBA:ARBA00023281,
KW ECO:0000256|PIRNR:PIRNR001150};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696, ECO:0000256|PIRNR:PIRNR001150};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001150};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|PIRNR:PIRNR001150};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1NWX6};
KW Reference proteome {ECO:0000313|Proteomes:UP000000539};
KW Secreted {ECO:0000256|PIRNR:PIRNR001150};
KW Serine protease {ECO:0000256|PIRNR:PIRNR001150};
KW Tissue remodeling {ECO:0000256|ARBA:ARBA00023148,
KW ECO:0000256|PIRNR:PIRNR001150}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DISULFID 185..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 206..245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 234..257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 275..352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 296..335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 324..347
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 374..451
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 395..434
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 423..446
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 802 AA; 90764 MW; 9C952CCB62151BDC CRC64;
MGISKATLLL LFLLSSVQGS ILDNYVRTEG AWLLNSKKET YKTSSKEECA EQCETETKFP
CRAFLFTSKD QQCITLAENT KTAVLFRRTN AVLYEKRIYL LECKKGRGKD YRGTEAKTQK
GVACQKWADT APHKPNYTPE KHPSAGLEEN YCRNPDNDEK GPWCYTTDPN TRFDYCNIPE
CEVECMHCSG ENYHGVVATT ASGLECQRWD SQLPHSHGYL PENFPEKDLK MNYCRNPDGE
PRPWCFTTNP NKRWEFCDIP RCTTPPPVPA PGRQCLSGRG EDYRGKISVT ESGNTCQHWS
AQFPHKHART PENYPCKNLE ENYCRNPDGE QMPWCYTTNA TARWEYCTIP SCDGKEPDTP
AVDQPEQAQA TEECYQGNGV SYRGTASFTI TGKKCQAWNS MSPHRHNKTS EHFPNADLRQ
NYCRNPDADS RPWCYTTDPS VRWEYCNLKR CSDNIQTILP KPPQTTLEPN PDCIHSNGID
YRGTVARTAR GRICQEWSSQ TPHKHDYFTP RTHPKSGLEK NYCRNPDGDV NGPWCYTTDP
RKAWEYCDIP KCSPAQYECG KAKVRPKLCA QRIVAGCISH PHSWPWQISL RTSYGLHFCG
GTLIDPKWVL TAAHCLEKSL RPSSYKVYLG LHEERALESS VQKRDVEKLF KEPHGQDIAL
LKLRSPAVIT DQVIPVCLPK ENAVLGGREE CYVTGWGDTK GTPGQGYLKE TGFPVIENKI
CNRPEFLNGR VKKHELCAGN IHGGTDTCQG DSGGPLVCLD QDKFVQHGVT SWGLGCALPM
KPGVYVRVSA YIPWIKSIME NN
//
