TBC24_XENTR
ID TBC24_XENTR Reviewed; 562 AA.
AC Q08CX5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=TBC1 domain family member 24;
GN Name=tbc1d24;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Oviduct;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC protein(s). Involved in neuronal projections development, probably
CC through a negative modulation of ARF6 function. Involved in the
CC regulation of synaptic vesicle trafficking.
CC {ECO:0000250|UniProtKB:Q9ULP9}.
CC -!- SUBUNIT: Interacts with ARF6. {ECO:0000250|UniProtKB:Q9ULP9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ULP9};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9ULP9}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9ULP9}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9VIH7}. Presynapse
CC {ECO:0000250|UniProtKB:Q9ULP9}. Note=Mainly cytoplasmatic with partial
CC expression at the plasma membrane (By similarity). Associates with
CC certain types of membrane phosphoinositides, preferentially those
CC phosphorylated at the D5 position of the inositol ring such as
CC phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidylinositol
CC 3,4,5-trisphosphate (PIP3) (By similarity).
CC {ECO:0000250|UniProtKB:Q9ULP9, ECO:0000250|UniProtKB:Q9VIH7}.
CC -!- DOMAIN: The Rab-GAP TBC domain is essential for phosphatidylinositol
CC binding. {ECO:0000250|UniProtKB:Q9VIH7}.
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DR EMBL; BC124045; AAI24046.1; -; mRNA.
DR RefSeq; NP_001072701.1; NM_001079233.1.
DR AlphaFoldDB; Q08CX5; -.
DR SMR; Q08CX5; -.
DR STRING; 8364.ENSXETP00000038986; -.
DR PaxDb; Q08CX5; -.
DR Ensembl; ENSXETT00000043751; ENSXETP00000043751; ENSXETG00000020284.
DR GeneID; 780158; -.
DR KEGG; xtr:780158; -.
DR CTD; 780158; -.
DR Xenbase; XB-GENE-981681; tbc1d24.1.
DR eggNOG; KOG2801; Eukaryota.
DR HOGENOM; CLU_018035_1_1_1; -.
DR InParanoid; Q08CX5; -.
DR OMA; SFVDWNQ; -.
DR OrthoDB; 1047825at2759; -.
DR TreeFam; TF315420; -.
DR Reactome; R-XTR-8854214; TBC/RABGAPs.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000020284; Expressed in ovary and 16 other tissues.
DR ExpressionAtlas; Q08CX5; differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; IEA:InterPro.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR040149; TBC1D24.
DR InterPro; IPR006571; TLDc_dom.
DR PANTHER; PTHR23353:SF6; PTHR23353:SF6; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR Pfam; PF07534; TLD; 2.
DR SMART; SM00164; TBC; 1.
DR SMART; SM00584; TLDc; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS51886; TLDC; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cytoplasm; Cytoplasmic vesicle;
KW GTPase activation; Membrane; Reference proteome; Synapse.
FT CHAIN 1..562
FT /note="TBC1 domain family member 24"
FT /id="PRO_0000288507"
FT DOMAIN 42..259
FT /note="Rab-GAP TBC"
FT DOMAIN 337..549
FT /note="TLDc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01234"
FT REGION 451..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:Q9VIH7"
FT BINDING 40
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:Q9VIH7"
FT BINDING 238
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:Q9VIH7"
FT BINDING 242
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:Q9VIH7"
FT BINDING 293..297
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol)"
FT /ligand_id="ChEBI:CHEBI:57880"
FT /evidence="ECO:0000250|UniProtKB:Q9VIH7"
SQ SEQUENCE 562 AA; 63716 MW; 090E67145013C18B CRC64;
MDDTEYGRFV DWDKMEGGGQ EQSTKVLSCT DFQDLKQMAR QGHWAKSHSL RAKVYQKLIK
EIPCRTVTPD ASVYRDIVGK IVGKRPASSL PLPEFVDDRQ IPSYCLNSEG IGAVRKIITC
ISNQFPDISF CPALPSLVAL LLHYSQDEAE CFENVSRILA CNDPNRRLVD QTFLAFESSC
MTFGDLAGKY CQGPHKLMVA VSEDVLEVYS DWQRWIFGEL PFAYITRVFD VFLVEGYKVL
FRVALALLKF FHKVRGGQPM ESNNVKRDIQ MFVRDLNQCV APEKLLEKAF AIRLFSRKEI
QLLQMANEKA LQQKGITVKQ KRQNVHLAVH AENFKSEIVS VKEMRDIWSW IPERFALSQP
LLLYTNREHG NSLSRFYLHC EGHEPTLLLI KTTNQEVCGA FLSTDWSERR RSGNKLSFFG
TGECFVFRLQ PEVERYEWVV IKHPELGKVN ASSGDNDANS SQSAKDGIDP SDRLSPFLAT
RHFNLPSKSA SMFMAGSTDC IIIGGGDGQA LYFDSDLNYG RTSHCNTFNN QPLCSETFQI
SIIEVWGFKD NVNNDGAHSA LP
