ID A0A2I3NIJ7_PAPAN Unreviewed; 499 AA.
AC A0A2I3NIJ7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Plasminogen activator {ECO:0000256|PIRNR:PIRNR001145};
DE EC=3.4.21.68 {ECO:0000256|PIRNR:PIRNR001145};
GN Name=PLAT {ECO:0000313|Ensembl:ENSPANP00000047696.2};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000047696.2, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000047696.2, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000047696.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form
CC plasmin.; EC=3.4.21.68; Evidence={ECO:0000256|ARBA:ARBA00001538,
CC ECO:0000256|PIRNR:PIRNR001145};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|PIRNR:PIRNR001145}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|PIRNR:PIRNR001145}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A2I3NIJ7; -.
DR Ensembl; ENSPANT00000054673.2; ENSPANP00000047696.2; ENSPANG00000006697.3.
DR GeneTree; ENSGT00940000158930; -.
DR Proteomes; UP000028761; Chromosome 8.
DR Bgee; ENSPANG00000006697; Expressed in pigmented layer of retina and 65 other cell types or tissues.
DR ExpressionAtlas; A0A2I3NIJ7; baseline.
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:0031639; P:plasminogen activation; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00061; FN1; 1.
DR CDD; cd00108; KR; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000083; Fibronectin_type1.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR026280; Tissue_plasm_act.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24264:SF42; TISSUE-TYPE PLASMINOGEN ACTIVATOR; 1.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00039; fn1; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001145; Tissue_plasm_act; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00058; FN1; 1.
DR SMART; SM00130; KR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01253; FN1_1; 1.
DR PROSITE; PS51091; FN1_2; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR001145-3};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001145};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Plasminogen activation {ECO:0000256|ARBA:ARBA00023202,
KW ECO:0000256|PIRNR:PIRNR001145};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR001145};
KW Reference proteome {ECO:0000313|Proteomes:UP000028761};
KW Secreted {ECO:0000256|PIRNR:PIRNR001145};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR001145}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..499
FT /note="Plasminogen activator"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035190697"
FT DOMAIN 39..81
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 82..120
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 151..233
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 248..498
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 42..52
FT /note="Important for binding to annexin A2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-2"
FT ACT_SITE 294
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT ACT_SITE 343
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT ACT_SITE 450
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT SITE 102
FT /note="Important for binding to LRP1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-2"
FT SITE 401
FT /note="Important for single-chain activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-2"
FT SITE 449
FT /note="Important for single-chain activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-2"
FT DISULFID 41..71
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 69..78
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 86..97
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 91..108
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3,
FT ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 110..119
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3,
FT ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 152..233
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 173..215
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 204..228
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 236..367
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 279..295
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 287..356
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 381..456
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 413..429
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 446..474
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
SQ SEQUENCE 499 AA; 55844 MW; C23710DA358346AB CRC64;
MNAMKRGLCC VLLLCGAVFA SPSQEIHARF RRGARSYQVI CRDEKTQMIY QQHQSWLRPV
LRSNRVEYCW CNSGRAQCHS VPVKSCSEPR CFNGGTCQQA LYFSDFVCQC PEGFAGKHCE
IDSKPWCYVF KAGKYSSEFC STPACSEGNS DCYFGNGLAY RGTHSLTASG ASCLPWNSMI
LIGKVYTAQN PNAQALGLGK HNYCRNPDGD AKPWCHVLKN RRLTWEYCDV PSCSTCGLRQ
YSQPQFRIKG GLFADIASHP WQAAIFAKHR RSPGERFLCG GILISSCWIL SAAHCFQERF
PPHHLTVYLG RTYRVVPGEE EQKFEVEKYI VHKEFDDDTY DNDIALLQLK SDSSHCAQES
SVVRTVCLPP ADLQLPDWTE CELSGYGKHE ASSPFYSERL KEAHVRLYPS SRCTSQHLLN
RTVTDNMLCA GDTRSGGPQA NLHDACQGDS GGPLVCLNDG RMTLVGIISW GLGCGQKDVP
GVYTKVTNYL DWIQDNMQP
//
