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Plasminogen (EC 3.4.21.7)

 A0A096NZY9_PAPAN        Unreviewed;       810 AA.
A0A096NZY9;
26-NOV-2014, integrated into UniProtKB/TrEMBL.
28-FEB-2018, sequence version 2.
05-DEC-2018, entry version 35.
RecName: Full=Plasminogen {ECO:0000256|PIRNR:PIRNR001150};
EC=3.4.21.7 {ECO:0000256|PIRNR:PIRNR001150};
Papio anubis (Olive baboon).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Papio.
NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000018664, ECO:0000313|Proteomes:UP000028761};
[1] {ECO:0000313|Ensembl:ENSPANP00000018664, ECO:0000313|Proteomes:UP000028761}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A.,
Aqrawi P.A., Arias F.A., Attaway T.A., Awwad R.A., Babu C.B.,
Bandaranaike D.B., Battles P.B., Bell A.B., Beltran B.B.,
Berhane-Mersha D.B., Bess C.B., Bickham C.B., Bolden T.B.,
Carter K.C., Chau D.C., Chavez A.C., Clerc-Blankenburg K.C.,
Coyle M.C., Dao M.D., Davila M.L.D., Davy-Carroll L.D., Denson S.D.,
Dinh H.D., Fernandez S.F., Fernando P.F., Forbes L.F., Francis C.F.,
Francisco L.F., Fu Q.F., Garcia-Iii R.G., Garrett T.G., Gross S.G.,
Gubbala S.G., Hirani K.H., Hogues M.H., Hollins B.H., Jackson L.J.,
Javaid M.J., Jhangiani S.J., Johnson A.J., Johnson B.J., Jones J.J.,
Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K., Kovar C.K.,
Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P.,
Perez Y.P., Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q.,
Rouhana J.R., Ruiz M.R., Ruiz S.-J.R., Saada N.S., Santibanez J.S.,
Scheel M.S., Schneider B.S., Simmons D.S., Sisson I.S., Tang L.-Y.T.,
Thornton R.T., Tisius J.T., Toledanes G.T., Trejos Z.T., Usmani K.U.,
Varghese R.V., Vattathil S.V., Vee V.V., Walker D.W.,
Weissenberger G.W., White C.W., Williams A.W., Woodworth J.W.,
Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N., Nazareth L.N.,
Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
"Whole Genome Assembly of Papio anubis.";
Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|Ensembl:ENSPANP00000018664}
IDENTIFICATION.
Ensembl;
Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
-!- 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:
Reaction=Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher
selectivity than trypsin. Converts fibrin into soluble
products.; EC=3.4.21.7;
Evidence={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; AHZZ02026022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; XP_009204619.2; XM_009206355.2.
Ensembl; ENSPANT00000021927; ENSPANP00000018664; ENSPANG00000007072.
GeneID; 101008370; -.
CTD; 5340; -.
GeneTree; ENSGT00940000155208; -.
OrthoDB; EOG091G0AH5; -.
Proteomes; UP000028761; Chromosome 4.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-UniRule.
GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-UniRule.
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:UP000028761};
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:UP000028761};
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 20 810 Plasminogen. {ECO:0000256|SAM:SignalP}.
/FTId=PRO_5014123103.
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 581 808 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}.
SEQUENCE 810 AA; 90754 MW; F6CD6E5644ACBB1F CRC64;
MEHKEVVLLL LLFLKSGQGE PLDDYVNTKG ASLFSITKKQ LRAGSIEECA AKCEEEEEFT
CRSFQYHSKE QQCVIMAENR KSSIVFRMRD VILFEKKVYL SECKTGNGKN YRGTMSKTKT
GITCQKWSST SPHRPRFSPA THPSEGLEEN YCRNPDNDEQ GPWCYTTDPE HRFDYCDIPE
CEDECMHCSG ENYYGKISKT MSGLECQAWD SQSPHAHGYI PSKFPNKNLK KNYCRNPDGE
PRPWCFTTDP NKRWELCDIP RCTTPPPSSG PTYQCLKGTG ENYRGDVAVT VSGHTCQRWS
AQTPHIHNRT PENFPCKNLD ENYCRNPDGE KAPWCYTTDS QVRWEYCKIP SCESSPVSTE
PLDPTAPPEL TPVVQECYYG DGQSYRGTSS ITVTGKKCQS WSSMTPHWHQ RTPENYPNAG
LTMNYCRNPD ADKGPWCFTT DPSVRWEYCN LKKCSGTEGS VAAPPPVAQL PDAETPSEED
CMFGNGKRYR GKKATTVTGT PCQEWAAKEP HSHLIFTPET YPRAGLEKNY CRNPDGDVGG
PWCYTTNPRK LYDYCDVPQC ASSSFDCGKP QVEPKKCPGR VVGGCVAHAH SWPWQVSLRT
RFGMHFCGGT LISPEWVLTA AHCLEKSPRP SFYKVILGAH QEVRLEPHVQ EIEVSKMFSE
PAGADIALLK LSSPAIITDK VIPACLPSPN YVVADRTECF ITGWGETQGT YGAGLLKEAR
LPVIENKVCN RYEFLNGRVK STELCAGHLA GGTDSCQGDS GGPLVCFEKD KYILQGVTSW
GLGCARPNKP GVYVRVSRFV TWIEGVMRNN


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