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Database: UniProt
Entry: A0A3B3DRJ1_ORYME
LinkDB: A0A3B3DRJ1_ORYME
Original site: A0A3B3DRJ1_ORYME 
ID   A0A3B3DRJ1_ORYME        Unreviewed;       605 AA.
AC   A0A3B3DRJ1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=t-plasminogen activator {ECO:0000256|ARBA:ARBA00013193};
DE            EC=3.4.21.68 {ECO:0000256|ARBA:ARBA00013193};
GN   Name=PLAT {ECO:0000313|Ensembl:ENSOMEP00000032049.1};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000032049.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000032049.1}
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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   AlphaFoldDB; A0A3B3DRJ1; -.
DR   Ensembl; ENSOMET00000023883.1; ENSOMEP00000032049.1; ENSOMEG00000017298.1.
DR   GeneTree; ENSGT00940000158930; -.
DR   OMA; WCYIFKA; -.
DR   Proteomes; UP000261560; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
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; 2.10.70.10; Complement Module, domain 1; 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; 3.
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   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; 2.
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; SSF57603; FnI-like domain; 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.
PE   4: Predicted;
KW   Digestion {ECO:0000256|ARBA:ARBA00022757};
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   Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW   ProRule:PRU00121}; Plasminogen activation {ECO:0000256|ARBA:ARBA00023202};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..605
FT                   /note="t-plasminogen activator"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017238717"
FT   DOMAIN          78..116
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          122..204
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          211..293
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          331..601
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   ACT_SITE        377
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT   ACT_SITE        426
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT   ACT_SITE        553
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-1"
FT   DISULFID        38..66
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT   DISULFID        64..74
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT   DISULFID        82..93
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT   DISULFID        87..104
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-3,
FT                   ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        106..115
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-3,
FT                   ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        123..204
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT   DISULFID        144..186
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT   DISULFID        175..199
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT   DISULFID        212..293
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT   DISULFID        233..275
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT   DISULFID        264..288
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT   DISULFID        316..450
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT   DISULFID        362..378
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT   DISULFID        370..439
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT   DISULFID        464..559
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
FT   DISULFID        496..512
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001145-3"
SQ   SEQUENCE   605 AA;  67945 MW;  1C78B33691BCF1CB CRC64;
     MLRSLHLFLL LSALYCSLAE NVELLRSKRG VRFYRVLCVD SETSAVRSYG DTWLRWKGQR
     VEYCHCALRG QERCHSVPVI NCYVSQCYNG GTCKESVYTS DYICQCPQGF KGTQCEINSN
     EKCIVGKGEG YRGTLSVTRS GEECINWNST SLRGKKFTAR KNDASSLGLG NHNFCRNPDQ
     DSSPWCYIYK GNQIIWELCS LPKCSGDRNR ECMQGLGKSY RGTTAVTKTG SACLPWDSPA
     VRRKRNNAWK SNALDLGLSN HNFCRNPDGD SGPWCHTYKN MQLTWELCDI PKCSRAPSTI
     TTLGPRAPTT NNQATCGQRL DNTLNRPTFR IFGGRGSDIT EQPWQAAINF YVPRVKRHFH
     LCGGVLIDSC WVLSAAHCFQ EKDTPEILQV ILGRTFRTQN SNSEQIFKVE KLWIHEKFDS
     ETYDNDIAIL KLKTDMGLCA VNSEEVLPAC LPDRGLQLPD WTECEISGYG KSSEFSPEFS
     EQVKRGHVRL WPKERCTPEV LSGRPVTPNM LCAGDTRGKD DACKVSVSTL IKPQSLMSLP
     IIIPSSFYSQ GDSGGPLVCR NQNRMTLMGL VSWGDGCGEK DKPGVYTRVT NYIDWIKRKI
     QASPV
//
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