ID A0A2K5EP10_AOTNA Unreviewed; 517 AA.
AC A0A2K5EP10;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:ENSANAP00000034936.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000034936.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000034936.1}
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}.
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DR AlphaFoldDB; A0A2K5EP10; -.
DR Ensembl; ENSANAT00000053003.1; ENSANAP00000034936.1; ENSANAG00000034979.1.
DR GeneTree; ENSGT00940000158930; -.
DR Proteomes; UP000233020; 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; cd00108; KR; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR000742; EGF-like_dom.
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; PF00051; Kringle; 2.
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; SM00130; KR; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57440; Kringle-like; 2.
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; PS00021; KRINGLE_1; 2.
DR PROSITE; PS50070; KRINGLE_2; 2.
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};
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:UP000233020};
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..517
FT /note="Plasminogen activator"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014373697"
FT DOMAIN 36..74
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 80..162
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 169..251
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 266..516
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 312
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT ACT_SITE 361
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT ACT_SITE 468
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT DISULFID 40..51
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 45..62
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3,
FT ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 64..73
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3,
FT ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 81..162
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 102..144
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 133..157
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 170..251
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 191..233
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 222..246
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 254..385
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 297..313
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 305..374
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 399..474
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 431..447
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT DISULFID 464..492
FT /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
SQ SEQUENCE 517 AA; 57642 MW; 0BB4D26A608E9F99 CRC64;
MSTVKAGLCC VLLLCGAVFA SPSQEIHARF RRGARSYRGC SEPRCFNGGT CRQALYFSDF
VCQCPEGFTG KRCEIDTKAT CYEDKGISYR GTWSTAESGA ECTNWNSSVL AQKPYSGRRP
DAVRLGLGNH NYCRNPDRDS KPWCYVFKAG RYSSEFCSIP PCSKGENGDC YFGKGLAYRG
THSLTTSGAS CLPWNSMILI DKVYTAHNPN AQALGLGKHN FCRNPDGDAK PWCHVLKNRR
LTWEYCDMPS CSTCGLRQYN RPQFRIKGGL FADIATHPWQ AAIFAKHRRS PGERFLCGGI
LIGSCWILSA AHCFQERFPP HHLTVILGRT YRVVPGEEEQ KFEVEKYIVH KEFDDDTYDN
DIALLQLKSD SSHCAQESDV VRTVCLPAAD LQLPDWTECE LSGYGKHEAT SPFYSERLKE
AHVRLYPSSR CTSQHLFNRT VTNNMLCAGD TRSGGPQANL HDACQGDSGG PLVCSKDGRM
TLVGIISWGL GCGQKDVPGV YTKVTNYLDW IQDNMRP
//
