ID W5M767_LEPOC Unreviewed; 338 AA.
AC W5M767;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Docking protein 6 {ECO:0000313|Ensembl:ENSLOCP00000004225.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000004225.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000004225.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the DOK family. Type B subfamily.
CC {ECO:0000256|ARBA:ARBA00006520}.
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DR EMBL; AHAT01004319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01004320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01004321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01004322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01004323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015209286.1; XM_015353800.1.
DR AlphaFoldDB; W5M767; -.
DR STRING; 7918.ENSLOCP00000004225; -.
DR Ensembl; ENSLOCT00000004233.1; ENSLOCP00000004225.1; ENSLOCG00000003566.1.
DR GeneID; 102686350; -.
DR KEGG; loc:102686350; -.
DR CTD; 220164; -.
DR eggNOG; KOG4047; Eukaryota.
DR GeneTree; ENSGT00940000158760; -.
DR HOGENOM; CLU_057256_1_0_1; -.
DR InParanoid; W5M767; -.
DR OMA; NIFRRCW; -.
DR OrthoDB; 2996885at2759; -.
DR Proteomes; UP000018468; Linkage group LG9.
DR Bgee; ENSLOCG00000003566; Expressed in camera-type eye and 3 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd14678; PH_DOK4_DOK5_DOK6; 1.
DR CDD; cd13164; PTB_DOK4_DOK5_DOK6; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR InterPro; IPR037816; DOK4/5/6_PH.
DR InterPro; IPR002404; IRS_PTB.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR21258:SF43; DOCKING PROTEIN 6; 1.
DR PANTHER; PTHR21258; DOCKING PROTEIN RELATED; 1.
DR Pfam; PF02174; IRS; 1.
DR SMART; SM01244; IRS; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00310; PTBI; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR PROSITE; PS51064; IRS_PTB; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 132..237
FT /note="IRS-type PTB"
FT /evidence="ECO:0000259|PROSITE:PS51064"
FT REGION 318..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 338 AA; 38768 MW; 0C7C466DE8F2A356 CRC64;
MASNFNDIVK QGYVKFRSRK LGIFRRCWLV LKKASSKGPR RLEKFPDEKA AYFRNFHKIT
ELHNIKNITR LPRETKKHAV TIIFYDETSK TFACESELEA EEWCKLLCVE CLGSRLNDIS
LGEPDLLAAG VQREQNERFN VYLMPTPNLD IYGECTMQIT HENIYLWDIH NARVKLVMWP
LSSLRRYGRD STWFTFESGR MCDTGEGLFT FQTREGEMIY QRVHSATLSI AQQHERLMIE
MEKNAQIQSG SNEGALSKSV SLPRSAYWHH ITRQDSVGEI FSLQGASLGM TLVPRAQTFP
SHLLEQGADE ELARIRHQEQ ALSPSSGYGS SYSSGPVQ
//
