ID W5N019_LEPOC Unreviewed; 1269 AA.
AC W5N019;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=TBC1 domain family member 4 {ECO:0000313|Ensembl:ENSLOCP00000013978.1};
GN Name=TBC1D4 {ECO:0000313|Ensembl:ENSLOCP00000013978.1};
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:ENSLOCP00000013978.1, 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:ENSLOCP00000013978.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01034998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01034999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01035000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01035001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015220026.1; XM_015364540.1.
DR AlphaFoldDB; W5N019; -.
DR STRING; 7918.ENSLOCP00000013978; -.
DR Ensembl; ENSLOCT00000014007.1; ENSLOCP00000013978.1; ENSLOCG00000011360.1.
DR GeneID; 102691902; -.
DR CTD; 9882; -.
DR eggNOG; KOG4436; Eukaryota.
DR GeneTree; ENSGT00940000158486; -.
DR HOGENOM; CLU_005350_13_2_1; -.
DR InParanoid; W5N019; -.
DR OMA; QQMRDPA; -.
DR OrthoDB; 2908929at2759; -.
DR Proteomes; UP000018468; Linkage group LG17.
DR Bgee; ENSLOCG00000011360; Expressed in intestine and 13 other cell types or tissues.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR CDD; cd00934; PTB; 1.
DR CDD; cd01269; PTB_TBC1D1_like; 1.
DR Gene3D; 1.10.10.2750; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 1.10.8.270; putative rabgap domain of human tbc1 domain family member 14 like domains; 1.
DR Gene3D; 1.10.472.80; Ypt/Rab-GAP domain of gyp1p, domain 3; 1.
DR InterPro; IPR021785; DUF3350.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000195; Rab-GAP-TBC_dom.
DR InterPro; IPR035969; Rab-GAP_TBC_sf.
DR PANTHER; PTHR47219; RAB GTPASE-ACTIVATING PROTEIN 1-LIKE; 1.
DR PANTHER; PTHR47219:SF13; TBC1 DOMAIN FAMILY MEMBER 4 ISOFORM X1; 1.
DR Pfam; PF11830; DUF3350; 1.
DR Pfam; PF00640; PID; 2.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00462; PTB; 2.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF47923; Ypt/Rab-GAP domain of gyp1p; 2.
DR PROSITE; PS01179; PID; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 21..164
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT DOMAIN 344..416
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT DOMAIN 890..1084
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000259|PROSITE:PS50086"
FT REGION 228..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1171..1240
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 569..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1269 AA; 142936 MW; 0D43F08A82FD59F5 CRC64;
MEATDSQDDK TNNPSKSEKR FALWYMGWSP LDRRTTLPML PWLVAEIRRR RERSEAGSAQ
AREVQIILIP PLIRCVPASN SSSSVFIFEH KAQHISRFIH NSHDITYFAY LIRTQPDNPE
SEMACHVFKA SDPNQVPDVI SSIRQVSKAA LKEDAKTKQE GEEAFYNSQR FEVLYCGKVT
VLHKKAPSTL IDDCVEKFKQ HELESKRIKL LNDQRGSTDS VSFIVGEGDP LTPLLSSPPD
RGEGGGAADS VNGNSVLSAS ASQASLHGSR SAFPECILED SGFDDQQEFR TRCNSLAAGL
QKKVSDSNLT GPLRRRHASA PSHVQPSDAE KNRTMLFQVG RFEVNLISPD SKSVVLEKNF
KDISSCSQGI KQTDHFGFIC REAIESGPSQ YVCYVFQCAS ESLVDEVMLT LKQAFSTAAA
LQNAKTQIKL CEACPMHDLH KLCERIEGLY PPRAKLIIQR HLSLLNDNEQ ADIFERVQKM
KPSSDQEENE LVILHLRQLC EAKQKTHLHI GETPQPNSSN SGLSESVSTS GRFKLDVLKN
KARKSLTNSL ENIFSRGASR MRGRLGSMDS YERSSSLASD KDCSPGDSPP TTPPASPVSS
LGQAFPEEDP DSPQFRRRAH TFSHPPSSKK RISFPDSRSQ SSRSPIQRQQ SVAPELLQSS
PIAISRRTRS VSESDSSSSS IPASFSAPTF LKNLYQASSR PLPLADSGNF KSNGEGRKRT
FSGCSSDSLS AGVPPVTPRR ISWRQKIFLR VASPMSKSPA AMQRKDRLDG TELLPLSPLA
PALEKDPLAA LLQPEEAFVE KRPRHTAEDL RALWKKAIHQ QILLLRMEKE NQRLEASRDE
LHTRKIKLDY QEVGQCPKDV SAAWDKRLSV PGRAKARCDM EEIHSALSQG VPKNRRGEIW
QFLAHQYRLR HRLPCKQQPP DTSYKELLKQ LTAQQHAILV DLGRTFPTHQ YFSTQLGAGQ
LSLFNLLKAY SLLDVEVGYC QGISFLAGVL LLHMSEEQAF EMLKFIMYDL SFRKQYKPDM
VSLQIQMYQL SRLLHDYHRD LYDHLEENEI SPSLYAAPWF LTLFASQFPL GFVASIYDLI
FLQGTEVIFK VALYLLSSHE SRIMECDSFE TIVDFLKSTI PNLTLAQMEK TISQVLEMDI
SKQLHAYEVE YHVLQDEMLE ASSPTEDGDR LEKLEKANSQ LKKQNMDLLE KLQAARLKIQ
SLELTMENFL TRESKMKHLI RSLEQEKAAY QKTIERMRSS LPQDMLSDVE LTEIKCGSNS
KAKPGNKKP
//
