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Database: UniProt
Entry: A0A2Y9L069_ENHLU
LinkDB: A0A2Y9L069_ENHLU
Original site: A0A2Y9L069_ENHLU 
ID   A0A2Y9L069_ENHLU        Unreviewed;      1153 AA.
AC   A0A2Y9L069;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Proto-oncogene DBL isoform X5 {ECO:0000313|RefSeq:XP_022376994.1};
GN   Name=LOC111158943 {ECO:0000313|RefSeq:XP_022376994.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022376994.1};
RN   [1] {ECO:0000313|RefSeq:XP_022376994.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022376994.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_022376994.1; XM_022521286.1.
DR   AlphaFoldDB; A0A2Y9L069; -.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd00160; RhoGEF; 1.
DR   CDD; cd00170; SEC14; 1.
DR   CDD; cd11857; SH3_DBS; 1.
DR   CDD; cd00176; SPEC; 1.
DR   Gene3D; 1.20.58.60; -; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR035532; DBS_SH3.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   PANTHER; PTHR22826:SF146; PROTO-ONCOGENE DBL; 1.
DR   PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR   Pfam; PF13716; CRAL_TRIO_2; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00150; SPEC; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          27..227
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|PROSITE:PS50191"
FT   DOMAIN          648..828
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          846..962
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1069..1130
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          973..1011
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          383..413
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        973..1002
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1153 AA;  131937 MW;  D4F7079C2EA204FA CRC64;
     MAAAGSGPHL GSPTLAAPDA RPASAPPAPV RCGGTPGLLV GRDRYASVPA AQAAPLQVDV
     AVALPRGRSS EKYGRSYLCL LQAVFVAGGR GKENDWIITF PENCNFRCIP EEVIAKVLTY
     LTSIARQNGS DSRFTIILDR RLDTWSSLKI SLQKISVSFP GNLHLVLVLR PTSFLQRTFT
     DIGFRFSQED FMLKLPVVML SSVSDLLTYI DDKQLTPELG GTLQYCHSEW IIFRNAIENF
     ALTVKEMAQM LQSFGTELAE TELPDDIPSI EEILAVRAER YHMLKNDITA VTKEGKILLT
     SLEVPGAEDP VGSRLEHRHH VNGDWQTVNK LLTQVHDMEI AFDGFWEKHQ LKMQQYLQLW
     KFEQDFQELV SEVELMLNQQ AELADVTGNI GQVKQKIKKL ENLDENSQDL LAKARFVILH
     GHRLAANHHY ALDLICQRCN ELRYLSDVLV KEIKAKRIQL SKIFKMHKLL QQARQCCDEG
     ECLLANQEID KFQSKEDAQK ALRDIENFLE MALPFINYDP DTLQYEFDVI LSPELKVQMQ
     TVQLKLEHIR SAFENQQAGF RNLTDKNMKP VEFVVPASDN LMRSRATFSP KHVGVGYSFF
     QACKLFSKGK KTWRQNQSDL KIEVVHDGRE KSSDQSSSLD NDNTLDVLQN HVLNELIQTE
     RVYVRELFTV LLGYRAEMDN PEMFDLMPPL LRNKKDVLFG NMAEIYEFHN NIFLNSLENC
     VDAPERVGPC FLERKDDFQM YAKYCQNKPR SEAIWKKYSE CAFFQECQRK LKHRLGLDSY
     LLKPVQRITK YQLLLKELLK YSKGCRGFEQ LKEALDTMLD LLKSVNDSMH QIAINGYIGN
     LNELGKMIMQ GAFSVWTGHK KGATKMKDFA RFKPMQRHLF LYEKAIVFCK RRVESGEGSE
     RYPSYSFKHC LKMDEVGITE YVKGDNRKFE IWYAGKEEVY IVQAPNVDVK MTWLKEIRNI
     LLKQQELMTV KKRKQHNPLT DLDHLSSQRN DENPKRRQHG SFLGAEEPVP EPSGALAEVQ
     EAVPLVRAEA NTGWTQMSAP AEISEDPEEW PSNYVYASYD DNEEIRPLMS PGKYKALADC
     RKRGPEDLLI RNGDVIQFLH EDVEGQWLVK NLNRRKEGLI PGNTAQVLIG DYRFRNAKVP
     DAALSNTRKL SSP
//
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