ID A0A2K5XL37_MANLE Unreviewed; 499 AA.
AC A0A2K5XL37;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:ENSMLEP00000004019.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000004019.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000004019.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A2K5XL37; -.
DR Ensembl; ENSMLET00000019616.1; ENSMLEP00000004019.1; ENSMLEG00000017692.1.
DR GeneTree; ENSGT00940000158930; -.
DR Proteomes; UP000233140; Unplaced.
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:UP000233140};
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_5014331072"
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 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 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; 55723 MW; 312CC77CA8ECF32C CRC64;
MNAMKRGLCC VLLLCGAVFA SPSQEIHARF RRGARSYQVI CTDEKTQMIY 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
PLHHLTVILG RTYRVVPGEE EQKFEVEKYI VHKEFDDDTY DNDIALLQLK SDSSHCAQES
SVVRTVCLPP ADLQLPDWTE CELSGYGKHE ALSPFYSERL KEAHVRLYPS SRCTSQHLLN
RTVTDNMLCA GDTRSGGPQA NLHDACQGDS GGPLVCLNGG RMTLVGIISW GLGCGQKDVP
GVYTKVTNYL DWIQDNMQP
//
