TBC24_BOVIN
ID TBC24_BOVIN Reviewed; 516 AA.
AC Q29RJ2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=TBC1 domain family member 24;
GN Name=TBC1D24;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-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; BC114148; AAI14149.1; -; mRNA.
DR RefSeq; NP_001039761.1; NM_001046296.2.
DR AlphaFoldDB; Q29RJ2; -.
DR SMR; Q29RJ2; -.
DR STRING; 9913.ENSBTAP00000007182; -.
DR PaxDb; Q29RJ2; -.
DR PRIDE; Q29RJ2; -.
DR GeneID; 529002; -.
DR KEGG; bta:529002; -.
DR CTD; 57465; -.
DR eggNOG; KOG2801; Eukaryota.
DR InParanoid; Q29RJ2; -.
DR OrthoDB; 1047825at2759; -.
DR Proteomes; UP000009136; Unplaced.
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; 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; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..516
FT /note="TBC1 domain family member 24"
FT /id="PRO_0000288503"
FT DOMAIN 34..236
FT /note="Rab-GAP TBC"
FT DOMAIN 343..516
FT /note="TLDc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01234"
FT REGION 456..476
FT /note="Disordered"
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"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULP9"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULP9"
SQ SEQUENCE 516 AA; 58426 MW; A2094BF11F70FB91 CRC64;
MHPPAYNCFV DRDKMDSAIP DLGPKELSCT ELQELKQLAR QGYWARSYAL RGQVYQRLIR
DIPCRTVTPD ASVYRDIVGK IVGKHSSASL PLPEFVDNTQ VPSYCLNSKG EGAVRKILLC
ISNQFPDVSF CPALPAVVAL LLHYSADEAE CFEKACRILA CNDSSRKLVD QSFLAFESSC
MTFGDLVNKY CQAAHKLMVA VSEDVLQVYA DWQRWLFGEL PLSYFARVFD VFLVEGYKVL
YRVALAILKF FHKVRAGQPL ESDNVKQDIR AFVRDIAKTV SPEKLLEKAF AIRLFSRKEI
QLLQMANEKA LKQKGITVKQ KSVSLSKRQF VHLAVHADNF HSEIVGVKEM RDIWSWVPER
FALCQPLLLF SSLQHGYSLT RFYFQCEGRE PTVLLIKTTQ KEVCGAYLST DWSERNKFGG
KLGFFGTGEC FVFRLQPEVQ RYEWVVIKHP ELTKPAPLEP TTVPPSPSHS VSSEPADRLS
PFLATRHFNL PSKTESLFMA GGSDCLIIGH VAGDWR
