ID A0A3Q1ILK3_ANATE Unreviewed; 637 AA.
AC A0A3Q1ILK3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Docking protein 2 {ECO:0000313|Ensembl:ENSATEP00000021205.2};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000021205.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000021205.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the DOK family. Type A subfamily.
CC {ECO:0000256|ARBA:ARBA00010955}.
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DR AlphaFoldDB; A0A3Q1ILK3; -.
DR STRING; 64144.ENSATEP00000021205; -.
DR Ensembl; ENSATET00000021563.2; ENSATEP00000021205.2; ENSATEG00000014731.2.
DR GeneTree; ENSGT00940000159868; -.
DR InParanoid; A0A3Q1ILK3; -.
DR Proteomes; UP000265040; Unplaced.
DR CDD; cd14676; PH_DOK1_2_3; 1.
DR CDD; cd01203; PTB_DOK1_DOK2_DOK3; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR InterPro; IPR037751; Dok1/2/3_PTB.
DR InterPro; IPR002404; IRS_PTB.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR21258:SF14; DOCKING PROTEIN 2; 1.
DR PANTHER; PTHR21258; DOCKING PROTEIN RELATED; 1.
DR Pfam; PF02174; IRS; 1.
DR Pfam; PF00169; PH; 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.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000265040}.
FT DOMAIN 4..121
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 158..261
FT /note="IRS-type PTB"
FT /evidence="ECO:0000259|PROSITE:PS51064"
FT REGION 264..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..620
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 72267 MW; B1599134BC018639 CRC64;
MEGDIRKQGM LYLQQQRFGK KWKRVWCMLF RESSCSISRL EFFECKDAGP LEKNDKTLRK
QQEHKKVIRL ADCIRVTEVE ADGCPRDTGP FLVETTEKIY MFAADRNQVE DWTHKLCEIA
FPMSWVEHGP KRGSLHRGNR VDEDEGMEDN SLYSGRETVR DFRVCVRRTE ASDRCRLKGD
GVLRADVESL HLLDKTGEIV YTWPYRYLRR FGRDKSTFSF EAGRRCDSGE GNFEFDTKQG
NILFQTVEGA INLQRITLPH RQTSGGGLVN LEPSQSLNLS SPPHNTVPVQ SRTPPPPQSR
GHMPQTPTAQ AEDSVYSMVN EHAVVHHKEK ESSTSIQQQQ QQQQRPQLSR LEPPVDKVLT
GVKSLTLDTR GLPAPRKNQV KMISSCPLPH VEPGSNLAPG PGSATASNSR LSPNLSSGPS
LGDTYSQITL PAAVDRSTKR EKRGERGGNL AKPCTPPVIN PDPEYSLPFD TIAKNVMVNI
LDSHQSHDSG ADPVYDSIDE MKIRNVFRSN VDTTRKVEHI YDEPEGCAAP AQKLPPSVYD
DPEEMRGDAW RIMGTAADPK GHEYPYNSRV DDYAVPKRPK RAFPVRQNTK EEEEEEAGEE
QQVEQIQEQE EQEQEEEEEE QEHRRDSPYN NVMVKMV
//
