TBC24_XENLA
ID TBC24_XENLA Reviewed; 562 AA.
AC A1A5K6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=TBC1 domain family member 24;
GN Name=tbc1d24;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-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; BC128694; AAI28695.1; -; mRNA.
DR RefSeq; NP_001090574.1; NM_001097105.1.
DR AlphaFoldDB; A1A5K6; -.
DR SMR; A1A5K6; -.
DR PRIDE; A1A5K6; -.
DR DNASU; 100036814; -.
DR GeneID; 100036814; -.
DR KEGG; xla:100036814; -.
DR CTD; 100036814; -.
DR Xenbase; XB-GENE-981686; tbc1d24.1.L.
DR OMA; SFVDWNQ; -.
DR OrthoDB; 1047825at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 100036814; Expressed in ovary and 19 other tissues.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
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; 1.
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_0000288506"
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 450..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..469
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; 63807 MW; FCD3AC4E8043CC16 CRC64;
MDEAEYGRFV DWDKMEAGGQ EQSPKVLSCT DFQELKQMAR QGHWAKSHTL RAKVYQKLIK
EIPCRTVTPD ASVYRDIVGK IVGKRSASSL PLPEFVDDRQ IPSYSLNSEG TGAVRKIISC
ISNQFPDISF CPALPSLVAL LLHYSQDEAE CFENVSRILA CNDPNRRLVD QTFLAFESSC
MTFGDLAGKY CQGPHKLMVA VSEDVLELYS DWQRWIFGEL PFAYITRVFD VFLVEGYKVL
FRVALALLKF FHKVRGGQPM ESNNVKRDLQ MFVRDLNKCV TPEKLLEKAF AIRLFSRKEI
QLLQMANEKA LQQKGITVKQ KRQNVHLAVH AENFTSEIVS VKEMRDIWSW IPERFALSQP
LLLFTNREHG NSLSRFYLHC EGHEPTLLLI KTTNQEVCGA FLSTDWSERK RSGNKLSFFG
TGECFVFRLQ PEVERYEWVV IKHPELGKVN SSSADKEANS SQSDKDGIDP SSRLSPFLAT
RHFNLPSKTA SMFMAGSIDC IIIGGGDGQA LYLDPDLNYG RTSHCNTFNN QPLCSETFQI
SIIEVWGFKD NMNNDGAHSA LH
