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Plasminogen (EC 3.4.21.7)

 H2QU06_PANTR            Unreviewed;       813 AA.
H2QU06;
21-MAR-2012, integrated into UniProtKB/TrEMBL.
28-FEB-2018, sequence version 2.
12-SEP-2018, entry version 55.
RecName: Full=Plasminogen {ECO:0000256|PIRNR:PIRNR001150};
EC=3.4.21.7 {ECO:0000256|PIRNR:PIRNR001150};
Name=PLG {ECO:0000313|Ensembl:ENSPTRP00000032051,
ECO:0000313|VGNC:VGNC:11165};
Pan troglodytes (Chimpanzee).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pan.
NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000032051, ECO:0000313|Proteomes:UP000002277};
[1] {ECO:0000313|Ensembl:ENSPTRP00000032051, ECO:0000313|Proteomes:UP000002277}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16136131; DOI=10.1038/nature04072;
Chimpanzee sequencing and analysis consortium;
"Initial sequence of the chimpanzee genome and comparison with the
human genome.";
Nature 437:69-87(2005).
[2] {ECO:0000313|Ensembl:ENSPTRP00000032051}
IDENTIFICATION.
Ensembl;
Submitted (FEB-2012) to UniProtKB.
-!- FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as
a proteolytic factor in a variety of other processes including
embryonic development, tissue remodeling, tumor invasion, and
inflammation. In ovulation, weakens the walls of the Graafian
follicle. It activates the urokinase-type plasminogen activator,
collagenases and several complement zymogens, such as C1 and C5.
Cleavage of fibronectin and laminin leads to cell detachment and
apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand
factor. Its role in tissue remodeling and tumor invasion may be
modulated by CSPG4. Binds to cells.
{ECO:0000256|PIRNR:PIRNR001150}.
-!- CATALYTIC ACTIVITY: Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa;
higher selectivity than trypsin. Converts fibrin into soluble
products. {ECO:0000256|PIRNR:PIRNR001150}.
-!- ACTIVITY REGULATION: Converted into plasmin by plasminogen
activators, both plasminogen and its activator being bound to
fibrin. {ECO:0000256|PIRNR:PIRNR001150}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|PIRNR:PIRNR001150}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen
subfamily. {ECO:0000256|PIRNR:PIRNR001150}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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EMBL; AACZ04028780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
ProteinModelPortal; H2QU06; -.
STRING; 9598.ENSPTRP00000032051; -.
MEROPS; S01.233; -.
PaxDb; H2QU06; -.
PRIDE; H2QU06; -.
Ensembl; ENSPTRT00000034673; ENSPTRP00000032051; ENSPTRG00000018774.
VGNC; VGNC:11165; PLG.
eggNOG; ENOG410IDXR; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000119133; -.
InParanoid; H2QU06; -.
OMA; CEDECMH; -.
OrthoDB; EOG091G0AH5; -.
TreeFam; TF329901; -.
Proteomes; UP000002277; Chromosome 6.
Bgee; ENSPTRG00000018774; Expressed in 4 organ(s), highest expression level in liver.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0031232; C:extrinsic component of external side of plasma membrane; IEA:Ensembl.
GO; GO:0044218; C:other organism cell membrane; IEA:Ensembl.
GO; GO:0034185; F:apolipoprotein binding; IEA:Ensembl.
GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
GO; GO:0019900; F:kinase binding; IEA:Ensembl.
GO; GO:1904854; F:proteasome core complex binding; IEA:Ensembl.
GO; GO:1990405; F:protein antigen binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-UniRule.
GO; GO:0022617; P:extracellular matrix disassembly; IEA:Ensembl.
GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-UniRule.
GO; GO:0052182; P:modification by host of symbiont morphology or physiology via secreted substance; IEA:Ensembl.
GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
GO; GO:0051918; P:negative regulation of fibrinolysis; IEA:Ensembl.
GO; GO:0051919; P:positive regulation of fibrinolysis; IEA:Ensembl.
GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-UniRule.
CDD; cd00108; KR; 5.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.20.10; -; 4.
InterPro; IPR000001; Kringle.
InterPro; IPR013806; Kringle-like.
InterPro; IPR018056; Kringle_CS.
InterPro; IPR038178; Kringle_sf.
InterPro; IPR003609; Pan_app.
InterPro; IPR023317; Pept_S1A_plasmin.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00051; Kringle; 5.
Pfam; PF00024; PAN_1; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001150; Plasmin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00130; KR; 5.
SMART; SM00473; PAN_AP; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57440; SSF57440; 5.
PROSITE; PS00021; KRINGLE_1; 5.
PROSITE; PS50070; KRINGLE_2; 5.
PROSITE; PS50948; PAN; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
3: Inferred from homology;
Blood coagulation {ECO:0000256|PIRNR:PIRNR001150};
Complete proteome {ECO:0000313|Proteomes:UP000002277};
Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00121,
ECO:0000256|SAAS:SAAS00037407};
Fibrinolysis {ECO:0000256|PIRNR:PIRNR001150};
Hemostasis {ECO:0000256|PIRNR:PIRNR001150};
Hydrolase {ECO:0000256|PIRNR:PIRNR001150,
ECO:0000256|RuleBase:RU363034, ECO:0000256|SAAS:SAAS00745848};
Kringle {ECO:0000256|PROSITE-ProRule:PRU00121,
ECO:0000256|SAAS:SAAS00045973};
Protease {ECO:0000256|PIRNR:PIRNR001150,
ECO:0000256|RuleBase:RU363034, ECO:0000256|SAAS:SAAS00745848};
Reference proteome {ECO:0000313|Proteomes:UP000002277};
Secreted {ECO:0000256|PIRNR:PIRNR001150};
Serine protease {ECO:0000256|PIRNR:PIRNR001150,
ECO:0000256|RuleBase:RU363034, ECO:0000256|SAAS:SAAS00745848};
Tissue remodeling {ECO:0000256|PIRNR:PIRNR001150}.
DOMAIN 20 101 Apple. {ECO:0000259|PROSITE:PS50948}.
DOMAIN 105 184 Kringle. {ECO:0000259|PROSITE:PS50070}.
DOMAIN 187 265 Kringle. {ECO:0000259|PROSITE:PS50070}.
DOMAIN 277 355 Kringle. {ECO:0000259|PROSITE:PS50070}.
DOMAIN 379 457 Kringle. {ECO:0000259|PROSITE:PS50070}.
DOMAIN 483 563 Kringle. {ECO:0000259|PROSITE:PS50070}.
DOMAIN 584 811 Peptidase S1.
{ECO:0000259|PROSITE:PS50240}.
ACT_SITE 625 625 Charge relay system.
{ECO:0000256|PIRSR:PIRSR001150-1}.
ACT_SITE 668 668 Charge relay system.
{ECO:0000256|PIRSR:PIRSR001150-1}.
ACT_SITE 763 763 Charge relay system.
{ECO:0000256|PIRSR:PIRSR001150-1}.
BINDING 137 137 Fibrin. {ECO:0000256|PIRSR:PIRSR001150-
2}.
BINDING 139 139 Fibrin. {ECO:0000256|PIRSR:PIRSR001150-
2}.
BINDING 139 139 Omega-aminocarboxylic acids.
{ECO:0000256|PIRSR:PIRSR001150-2}.
BINDING 161 161 Omega-aminocarboxylic acids.
{ECO:0000256|PIRSR:PIRSR001150-2}.
BINDING 175 175 Omega-aminocarboxylic acids.
{ECO:0000256|PIRSR:PIRSR001150-2}.
BINDING 435 435 Omega-aminocarboxylic acids.
{ECO:0000256|PIRSR:PIRSR001150-2}.
BINDING 448 448 Omega-aminocarboxylic acids.
{ECO:0000256|PIRSR:PIRSR001150-2}.
DISULFID 188 265 {ECO:0000256|PROSITE-ProRule:PRU00121}.
DISULFID 209 248 {ECO:0000256|PROSITE-ProRule:PRU00121}.
DISULFID 237 260 {ECO:0000256|PROSITE-ProRule:PRU00121}.
DISULFID 278 355 {ECO:0000256|PROSITE-ProRule:PRU00121}.
DISULFID 299 338 {ECO:0000256|PROSITE-ProRule:PRU00121}.
DISULFID 327 350 {ECO:0000256|PROSITE-ProRule:PRU00121}.
DISULFID 380 457 {ECO:0000256|PROSITE-ProRule:PRU00121}.
DISULFID 401 440 {ECO:0000256|PROSITE-ProRule:PRU00121}.
DISULFID 429 452 {ECO:0000256|PROSITE-ProRule:PRU00121}.
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


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