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Plasminogen (EC 3.4.21.7)

 K7EVW6_PONAB            Unreviewed;       816 AA.
K7EVW6;
09-JAN-2013, integrated into UniProtKB/TrEMBL.
09-JAN-2013, sequence version 1.
27-SEP-2017, entry version 45.
RecName: Full=Plasminogen {ECO:0000256|PIRNR:PIRNR001150};
EC=3.4.21.7 {ECO:0000256|PIRNR:PIRNR001150};
Name=PLG {ECO:0000313|Ensembl:ENSPPYP00000024703};
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pongo.
NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000024703, ECO:0000313|Proteomes:UP000001595};
[1] {ECO:0000313|Ensembl:ENSPPYP00000024703, ECO:0000313|Proteomes:UP000001595}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Wilson R.K., Mardis E.;
"A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|Ensembl:ENSPPYP00000024703}
IDENTIFICATION.
Ensembl;
Submitted (NOV-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}.
-!- ENZYME 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}.
-!- CAUTION: The sequence shown here is derived from an Ensembl
automatic analysis pipeline and should be considered as
preliminary data. {ECO:0000313|Ensembl:ENSPPYP00000024703}.
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EMBL; ABGA01021407; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; ABGA01021408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; ABGA01021409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; ABGA01065989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; ABGA01065990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; ABGA01065991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; ABGA01065992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
ProteinModelPortal; K7EVW6; -.
Ensembl; ENSPPYT00000033968; ENSPPYP00000024703; ENSPPYG00000017153.
eggNOG; ENOG410IDXR; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000119133; -.
OMA; PTYQCLK; -.
OrthoDB; EOG091G0AH5; -.
TreeFam; TF329901; -.
Proteomes; UP000001595; Chromosome 6.
GO; GO:0072562; C:blood microparticle; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; 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:0005102; F:receptor binding; IEA:Ensembl.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl.
GO; GO:0052182; P:modification by host of symbiont morphology or physiology via secreted substance; IEA:Ensembl.
GO; GO:0071674; P:mononuclear cell migration; IEA:Ensembl.
GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
GO; GO:0045445; P:myoblast differentiation; 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:0042246; P:tissue regeneration; IEA:Ensembl.
GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-UniRule.
GO; GO:0060707; P:trophoblast giant cell differentiation; IEA:Ensembl.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR000001; Kringle.
InterPro; IPR013806; Kringle-like.
InterPro; IPR018056; Kringle_CS.
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:UP000001595};
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:UP000001595};
Secreted {ECO:0000256|PIRNR:PIRNR001150};
Serine protease {ECO:0000256|PIRNR:PIRNR001150,
ECO:0000256|RuleBase:RU363034, ECO:0000256|SAAS:SAAS00745848};
Signal {ECO:0000256|SAM:SignalP};
Tissue remodeling {ECO:0000256|PIRNR:PIRNR001150}.
SIGNAL 1 19 {ECO:0000256|SAM:SignalP}.
CHAIN 20 816 Plasminogen. {ECO:0000256|SAM:SignalP}.
/FTId=PRO_5003900982.
DOMAIN 16 98 Apple. {ECO:0000259|PROSITE:PS50948}.
DOMAIN 102 181 Kringle. {ECO:0000259|PROSITE:PS50070}.
DOMAIN 184 262 Kringle. {ECO:0000259|PROSITE:PS50070}.
DOMAIN 274 352 Kringle. {ECO:0000259|PROSITE:PS50070}.
DOMAIN 376 454 Kringle. {ECO:0000259|PROSITE:PS50070}.
DOMAIN 480 560 Kringle. {ECO:0000259|PROSITE:PS50070}.
DOMAIN 581 816 Peptidase S1.
{ECO:0000259|PROSITE:PS50240}.
ACT_SITE 622 622 Charge relay system.
{ECO:0000256|PIRSR:PIRSR001150-1}.
ACT_SITE 665 665 Charge relay system.
{ECO:0000256|PIRSR:PIRSR001150-1}.
ACT_SITE 760 760 Charge relay system.
{ECO:0000256|PIRSR:PIRSR001150-1}.
BINDING 134 134 Fibrin. {ECO:0000256|PIRSR:PIRSR001150-
2}.
BINDING 136 136 Fibrin. {ECO:0000256|PIRSR:PIRSR001150-
2}.
BINDING 136 136 Omega-aminocarboxylic acids.
{ECO:0000256|PIRSR:PIRSR001150-2}.
BINDING 158 158 Omega-aminocarboxylic acids.
{ECO:0000256|PIRSR:PIRSR001150-2}.
BINDING 172 172 Omega-aminocarboxylic acids.
{ECO:0000256|PIRSR:PIRSR001150-2}.
BINDING 432 432 Omega-aminocarboxylic acids.
{ECO:0000256|PIRSR:PIRSR001150-2}.
BINDING 445 445 Omega-aminocarboxylic acids.
{ECO:0000256|PIRSR:PIRSR001150-2}.
DISULFID 185 262 {ECO:0000256|PROSITE-ProRule:PRU00121}.
DISULFID 206 245 {ECO:0000256|PROSITE-ProRule:PRU00121}.
DISULFID 234 257 {ECO:0000256|PROSITE-ProRule:PRU00121}.
DISULFID 275 352 {ECO:0000256|PROSITE-ProRule:PRU00121}.
DISULFID 296 335 {ECO:0000256|PROSITE-ProRule:PRU00121}.
DISULFID 324 347 {ECO:0000256|PROSITE-ProRule:PRU00121}.
DISULFID 377 454 {ECO:0000256|PROSITE-ProRule:PRU00121}.
DISULFID 398 437 {ECO:0000256|PROSITE-ProRule:PRU00121}.
DISULFID 426 449 {ECO:0000256|PROSITE-ProRule:PRU00121}.
SEQUENCE 816 AA; 91040 MW; CF687F1985BBA2BB CRC64;
MEHKEVVLLL LLFLKSGQGE PLDDYVNTQG ASLFSVTKKQ LRAGSIEECA AKCEEEKEFT
CRAFQYHSKE QQCVIMAENR KSSIIIRMRD VVLFEKKVYL SECKTGNGKN YRGTMSKTKN
GITCQKWSST SPHRPRFSPA THPSEGLEEN YCRNPDNDAQ GPWCYTTDPE HRYDYCDIPE
CEEACMHCSG ENYDGKISKT MSGLECQAWD SQSPHAHGYI PSKFPNKNLK KNYCRNPDGE
PRPWCFTTDP NKRWELCDIP RCTTPPPSSG PTYQCLKGTG ENYRGNVAVT VSGHTCQRWS
AQTPQTHNRT PENFPCKNLD ENYCRNPDGE KAPWCYTTNS QVRWEYCKIP SCDSSPVSTE
QLDPTAPPEL TPVVQDCYHG DGQSYRGTSS TTTTGKKCQS WSSMTPHWHQ KTPENYPDAG
LTMNYCRNPD ADKGPWCFTT DPSVRWEYCN LKKCSGTEGS VVAPPPVAQL PNVETPSEED
CMFGNGKGYR GKRATTVTGT PCQEWAAQEP HRHSIFTPQT NPRAGLEKNY CRNPDGDEGG
PWCYTTNPRK HYDYCDVPQC ASSSFDCGKP QVEPKKCPGR VVGGCVANAH SWPWQVSLRT
RFGTHFCGGT LISPEWVLTA AHCLEKSPRP SSYKVILGAH QEVNLEPHVQ EIEVSRLFLE
PTRADIALLK LSSPAVITDK VIPACLPSPN YVVAGRTECF ITGWGETQGT FGAGLLKEAQ
LPVIENKVCN RYEFLNGRVK STELCAGHLA GGTDSCQGDS GGPLVCFEKD KYILQGVTSW
GLGCARPNKP GVYVRVSRKD NSDNLKAVIY SKEQFP


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