ID A0A287A481_PIG Unreviewed; 814 AA.
AC A0A287A481;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 29.
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:ENSSSCP00000038571.2,
GN ECO:0000313|VGNC:VGNC:111814};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000038571.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000038571.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000038571.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000038571.2}
RP IDENTIFICATION.
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 -!- SUBUNIT: Interacts with CSPG4 and AMOT. Interacts (via the Kringle
CC domains) with HRG; the interaction tethers PLG to the cell surface and
CC enhances its activation. Interacts (via Kringle 4 domain) with ADA; the
CC interaction stimulates PLG activation when in complex with DPP4.
CC Angiostatin: Interacts with ATP5F1A; the interaction inhibits most of
CC the angiogenic effects of angiostatin. {ECO:0000256|ARBA:ARBA00038571}.
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 AlphaFoldDB; A0A287A481; -.
DR Ensembl; ENSSSCT00000055744.3; ENSSSCP00000038571.2; ENSSSCG00000004038.5.
DR VGNC; VGNC:111814; PLG.
DR GeneTree; ENSGT00940000155208; -.
DR Proteomes; UP000008227; Chromosome 1.
DR Bgee; ENSSSCG00000004038; Expressed in liver and 17 other cell types or tissues.
DR ExpressionAtlas; A0A287A481; baseline and differential.
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:0007596; P:blood coagulation; IEA:UniProtKB-UniRule.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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; 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:A0A287A481};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
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 DOMAIN 23..103
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 107..186
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 189..267
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 279..357
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 381..459
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 484..564
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 585..812
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 626
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT ACT_SITE 669
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT ACT_SITE 764
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT BINDING 163
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 177
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 437
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 450
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT DISULFID 190..267
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 211..250
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 239..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 280..357
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 301..340
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 329..352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 382..459
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 403..442
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 431..454
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 814 AA; 91003 MW; 5468819ADAF1DECB CRC64;
MGSHPYILLV GLQTGIHSQE RGLGDSLDDY VNTQGAFLFS LSRKQVAARS VEECAAKCEA
ETNFICRAFQ YHSKDQQCVV MAENSKTSPI ARMRDVVLFE KRIYLSECKT GNGKNYRGTT
SKTKSGVICQ KWSVSSPHIP KYSPEKFPLA GLEENYCRNP DNDEKGPWCY TTDPETRFDY
CDIPECEDEC MHCSGEHYEG KISKTMSGIE CQSWGSQSPH AHGYLPSKFP NKNLKMNYCR
NPDGEPRPWC FTTDPNKRWE FCDIPRCTTP PPTSGPTYQC LKGRGENYRG TVSVTASGHT
CQRWSAQSPH KHNRTPENFP CKNLEENYCR NPDGETAPWC YTTDSEVRWD YCKIPSCGSS
TTSTEYLDAP VPPEQTPVAQ DCYRGNGESY RGTSSTTITG RKCQSWVSMT PHRHEKTPGN
FPNAGLTMNY CRNPDADKSP WCYTTDPRVR WEYCNLKKCS ETEQQVTNFP AIAQVPSVED
LSEDCMFGNG KRYRGKRATT VAGVPCQEWA AQEPHRHSIF TPETNPRAGL EKNYCRNPDG
DDNGPWCYTT NPQKLFDYCD VPQCVTSSFD CGKPKVEPKK CPARVVGGCV SIPHSWPWQI
SLRHRYGGHF CGGTLISPEW VLTAKHCLEK SSSPSSYKVI LGAHEEHHLG EGVQEIDVSK
LFKEPSGADI ALLKLSSPAI ITDKVIPACL PTPNYVVADR TACYITGWGE TKGTYGAGLL
KEARLPVIEN KVCNRYEYLD GKVSSNELCA GHLAGGIDSC QGDSGGPLVC FEKDKYILQG
VTSWGLGCAL PNKPGVYVRV SRFVTWIEEI MRRN
//
