ID A0A2K5L0D6_CERAT Unreviewed; 499 AA.
AC A0A2K5L0D6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JAN-2026, entry version 35.
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:ENSCATP00000006388.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000006388.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000006388.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCATP00000006388.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Converts the abundant, but inactive, zymogen plasminogen to
CC plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By
CC controlling plasmin-mediated proteolysis, it plays an important role in
CC tissue remodeling and degradation, in cell migration and many other
CC physiopathological events. During oocyte activation, plays a role in
CC cortical granule reaction in the zona reaction, which contributes to
CC the block to polyspermy. {ECO:0000256|ARBA:ARBA00058178}.
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, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
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; A0A2K5L0D6; -.
DR Ensembl; ENSCATT00000023058.1; ENSCATP00000006388.1; ENSCATG00000019615.1.
DR GeneTree; ENSGT00940000158930; -.
DR Proteomes; UP000233060; Unassembled WGS sequence.
DR Bgee; ENSCATG00000019615; Expressed in adult mammalian kidney and 11 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031639; P:plasminogen activation; IEA:InterPro.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:TreeGrafter.
DR GO; GO:0014909; P:smooth muscle cell migration; IEA:TreeGrafter.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00061; FN1; 1.
DR CDD; cd00108; KR; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR FunFam; 2.40.10.10:FF:000054; Complement C1r subcomponent; 1.
DR FunFam; 2.10.70.10:FF:000043; Plasminogen activator; 1.
DR FunFam; 2.10.25.10:FF:000483; Tissue-type plasminogen activator; 1.
DR FunFam; 2.40.10.10:FF:000058; Tissue-type plasminogen activator; 1.
DR FunFam; 2.40.20.10:FF:000001; Urokinase-type plasminogen activator; 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.
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; IPR050127; Serine_Proteases_S1.
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; 1.
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:UP000233060};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR001145};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR001145};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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_5014363691"
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; 55778 MW; 2549DC5F546E4949 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
PLHHLTVILG RTYRVVPGEE EQKFEVEKYI VHKEFDDDTY DNDIALLQLK SDSSHCAQES
SVVRTVCLPP ADLQLPDWTE CELSGYGKHE ALSPFYSERL KEAHVRLYPS SRCTSQHLLN
RTVTDNMLCA GDTRSGGPQA NLHDACQGDS GGPLVCLNGG RMTLVGIISW GLGCGQKDVP
GVYTKVTNYL DWIQDNMQP
//
