ID H2QU06_PANTR Unreviewed; 813 AA.
AC H2QU06;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 82.
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:ENSPTRP00000032051.4,
GN ECO:0000313|VGNC:VGNC:11165};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000032051.4, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000032051.4, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000032051.4}
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 -!- 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 EMBL; AACZ04028780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2QU06; -.
DR MEROPS; S01.233; -.
DR PaxDb; 9598-ENSPTRP00000032051; -.
DR Ensembl; ENSPTRT00000034673.4; ENSPTRP00000032051.4; ENSPTRG00000018774.6.
DR VGNC; VGNC:11165; PLG.
DR eggNOG; ENOG502QVNP; Eukaryota.
DR GeneTree; ENSGT00940000155208; -.
DR HOGENOM; CLU_017565_0_0_1; -.
DR InParanoid; H2QU06; -.
DR TreeFam; TF329901; -.
DR Proteomes; UP000002277; Chromosome 6.
DR Bgee; ENSPTRG00000018774; Expressed in liver and 6 other cell types or tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0034185; F:apolipoprotein binding; IEA:Ensembl.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:1990405; F:protein antigen binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl.
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:0051702; P:biological process involved in interaction with symbiont; IEA:Ensembl.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-UniRule.
DR GO; GO:0022617; P:extracellular matrix disassembly; IEA:Ensembl.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-UniRule.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0051918; P:negative regulation of fibrinolysis; IEA:Ensembl.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IEA:Ensembl.
DR GO; GO:0051919; P:positive regulation of fibrinolysis; IEA:Ensembl.
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 3: Inferred from homology;
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, ECO:0000256|RuleBase:RU363034};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|PIRNR:PIRNR001150, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|PIRNR:PIRNR001150};
KW Serine protease {ECO:0000256|PIRNR:PIRNR001150,
KW ECO:0000256|RuleBase:RU363034};
KW Tissue remodeling {ECO:0000256|ARBA:ARBA00023148,
KW ECO:0000256|PIRNR:PIRNR001150}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 20..101
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 105..184
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 187..265
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 277..355
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 379..457
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 483..563
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 584..811
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 129..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 625
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT ACT_SITE 668
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT ACT_SITE 763
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-1"
FT BINDING 139
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 161
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 175
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 435
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT BINDING 448
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT /evidence="ECO:0000256|PIRSR:PIRSR001150-2"
FT DISULFID 188..265
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 209..248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 237..260
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 278..355
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 299..338
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 327..350
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 380..457
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 401..440
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 429..452
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 813 AA; 90913 MW; B97F1F782A301F90 CRC64;
DQYLSQVLLF YNFLRNPDTC QGEPLDDYVN TQGASLFSVT KKQLGAGSIE ECAAKCEEDK
EFTCRAFQYH SKEQQCVIMA ENRKSSIIIR MRDVVLFEKK VYLSECKTGN GKNYRGTMSK
TKNGITCQKW SSTSPHRPRF SPATHPSEGL EENYCRNPDN DPQGPWCYTT DPEKRYDYCD
ILECEEECMH CSGENYDGKI SKTMSGLECQ AWDSQSPHAH GYIPSKFPNK NLKKNYCRNP
DGELRPWCFT TDPNKRWELC DIPRCTTPPP SSGPTYQCLK GTGENYRGNV AVTVSGHTCQ
HWSAQTPHTH NRTPENFPCK NLDENYCRNP DGKRAPWCHT TNSQVRWEYC KIPSCDSSLV
STEQLAPTAP PELTPVVQDC YHGDGQSYRG TSSTTTTGKK CQSWSSMTPH RHQKTPENYP
NAGLTMNYCR NPDADKGPWC FTTDPSVRWE YCNLKKCSGT EASVVAPPPV VQLPNVETPS
EEDCMFGNGK GYRGKRATTV TGTPCQDWAA QEPHRHSIFT PETNPRAGLE KNYCRNPDGD
VGGPWCYTTN PRKLYDYCDV PQCASPSFDC GKPQVEPKKC PGRVVGGCVA HPHSWPWQVS
LRTRLGMHFC GGTLISPEWV LTAAHCLEKS PRPSSYKVIL GAHQEVKLEP HVQEIEVSRL
FLEPTRTDIA LLKLSSPAII TDKVIPACLP SPNYVVADRT ECFITGWGET QGTFGAGLLK
EAQLPVIENK VCNRNEFLNG RVKSTELCAG HLAGGTDSCQ GDSGGPLVCF EKDKYILQGV
TSWGLGCARP NKPGVYVRVS RFVTWIEGVM RNN
//
