TBC24_MOUSE
ID TBC24_MOUSE Reviewed; 561 AA.
AC Q3UUG6; A5D6Q7; Q3TTZ8; Q3UH11; Q6ZPW4; Q8BH92; Q8BNF2; Q8C3C6; Q8C3W8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=TBC1 domain family member 24;
GN Name=Tbc1d24; Synonyms=Kiaa1171;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Brain, Head, Heart, Hypothalamus, Skin, Spinal cord, and
RC Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20727515; DOI=10.1016/j.ajhg.2010.07.020;
RA Falace A., Filipello F., La Padula V., Vanni N., Madia F.,
RA De Pietri Tonelli D., de Falco F.A., Striano P., Dagna Bricarelli F.,
RA Minetti C., Benfenati F., Fassio A., Zara F.;
RT "TBC1D24, an ARF6-interacting protein, is mutated in familial infantile
RT myoclonic epilepsy.";
RL Am. J. Hum. Genet. 87:365-370(2010).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=24387994; DOI=10.1016/j.ajhg.2013.12.004;
RG University of Washington Center for Mendelian Genomics;
RA Rehman A.U., Santos-Cortez R.L., Morell R.J., Drummond M.C., Ito T.,
RA Lee K., Khan A.A., Basra M.A., Wasif N., Ayub M., Ali R.A., Raza S.I.,
RA Nickerson D.A., Shendure J., Bamshad M., Riazuddin S., Billington N.,
RA Khan S.N., Friedman P.L., Griffith A.J., Ahmad W., Riazuddin S., Leal S.M.,
RA Friedman T.B.;
RT "Mutations in TBC1D24, a gene associated with epilepsy, also cause
RT nonsyndromic deafness DFNB86.";
RL Am. J. Hum. Genet. 94:144-152(2014).
CC -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC protein(s) (PubMed:20727515). Involved in neuronal projections
CC development, probably through a negative modulation of ARF6 function
CC (PubMed:20727515). Involved in the regulation of synaptic vesicle
CC trafficking (By similarity). {ECO:0000250|UniProtKB:Q9ULP9,
CC ECO:0000269|PubMed:20727515}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UUG6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UUG6-2; Sequence=VSP_025702;
CC -!- TISSUE SPECIFICITY: Expressed in brain, particularly at the level of
CC the cortex and the hippocampus. Expressed in the inner ear in spiral
CC ganglion cells, a collection of neurons critical for hearing and
CC balance. {ECO:0000269|PubMed:20727515, ECO:0000269|PubMed:24387994}.
CC -!- DOMAIN: The Rab-GAP TBC domain is essential for phosphatidylinositol
CC binding. {ECO:0000250|UniProtKB:Q9VIH7}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39035.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC98114.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129304; BAC98114.1; ALT_INIT; mRNA.
DR EMBL; AK049306; BAC33671.1; -; mRNA.
DR EMBL; AK049754; BAC33904.1; -; mRNA.
DR EMBL; AK083833; BAC39035.1; ALT_FRAME; mRNA.
DR EMBL; AK084693; BAC39255.1; -; mRNA.
DR EMBL; AK086293; BAC39644.1; -; mRNA.
DR EMBL; AK138431; BAE23659.1; -; mRNA.
DR EMBL; AK147647; BAE28046.1; -; mRNA.
DR EMBL; AK161054; BAE36174.1; -; mRNA.
DR EMBL; BC080845; AAH80845.1; -; mRNA.
DR EMBL; BC094417; AAH94417.1; -; mRNA.
DR CCDS; CCDS28477.1; -. [Q3UUG6-2]
DR CCDS; CCDS50012.1; -. [Q3UUG6-1]
DR RefSeq; NP_001157319.1; NM_001163847.1. [Q3UUG6-1]
DR RefSeq; NP_001157320.1; NM_001163848.1. [Q3UUG6-1]
DR RefSeq; NP_001157321.1; NM_001163849.1. [Q3UUG6-1]
DR RefSeq; NP_001157322.1; NM_001163850.1. [Q3UUG6-2]
DR RefSeq; NP_001157323.1; NM_001163851.1. [Q3UUG6-2]
DR RefSeq; NP_001157324.1; NM_001163852.1. [Q3UUG6-2]
DR RefSeq; NP_001157325.1; NM_001163853.1. [Q3UUG6-2]
DR RefSeq; NP_775278.3; NM_173186.4. [Q3UUG6-2]
DR AlphaFoldDB; Q3UUG6; -.
DR SMR; Q3UUG6; -.
DR STRING; 10090.ENSMUSP00000127005; -.
DR iPTMnet; Q3UUG6; -.
DR PhosphoSitePlus; Q3UUG6; -.
DR SwissPalm; Q3UUG6; -.
DR EPD; Q3UUG6; -.
DR MaxQB; Q3UUG6; -.
DR PaxDb; Q3UUG6; -.
DR PeptideAtlas; Q3UUG6; -.
DR PRIDE; Q3UUG6; -.
DR ProteomicsDB; 254825; -. [Q3UUG6-1]
DR ProteomicsDB; 254826; -. [Q3UUG6-2]
DR DNASU; 224617; -.
DR Ensembl; ENSMUST00000040474; ENSMUSP00000036458; ENSMUSG00000036473. [Q3UUG6-2]
DR Ensembl; ENSMUST00000097376; ENSMUSP00000094989; ENSMUSG00000036473. [Q3UUG6-1]
DR Ensembl; ENSMUST00000167791; ENSMUSP00000127005; ENSMUSG00000036473. [Q3UUG6-1]
DR Ensembl; ENSMUST00000168378; ENSMUSP00000126107; ENSMUSG00000036473. [Q3UUG6-2]
DR Ensembl; ENSMUST00000168410; ENSMUSP00000128868; ENSMUSG00000036473. [Q3UUG6-2]
DR Ensembl; ENSMUST00000171189; ENSMUSP00000128001; ENSMUSG00000036473. [Q3UUG6-2]
DR Ensembl; ENSMUST00000201089; ENSMUSP00000144250; ENSMUSG00000036473. [Q3UUG6-2]
DR Ensembl; ENSMUST00000201301; ENSMUSP00000143949; ENSMUSG00000036473. [Q3UUG6-1]
DR Ensembl; ENSMUST00000201805; ENSMUSP00000143883; ENSMUSG00000036473. [Q3UUG6-1]
DR Ensembl; ENSMUST00000201960; ENSMUSP00000144208; ENSMUSG00000036473. [Q3UUG6-2]
DR Ensembl; ENSMUST00000202925; ENSMUSP00000144575; ENSMUSG00000036473. [Q3UUG6-2]
DR GeneID; 224617; -.
DR KEGG; mmu:224617; -.
DR UCSC; uc008auq.2; mouse. [Q3UUG6-1]
DR UCSC; uc008aus.2; mouse. [Q3UUG6-2]
DR CTD; 57465; -.
DR MGI; MGI:2443456; Tbc1d24.
DR VEuPathDB; HostDB:ENSMUSG00000036473; -.
DR eggNOG; KOG2801; Eukaryota.
DR GeneTree; ENSGT00410000025739; -.
DR HOGENOM; CLU_018035_1_1_1; -.
DR InParanoid; Q3UUG6; -.
DR OMA; SFVDWNQ; -.
DR OrthoDB; 1047825at2759; -.
DR PhylomeDB; Q3UUG6; -.
DR TreeFam; TF315420; -.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR BioGRID-ORCS; 224617; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Tbc1d24; mouse.
DR PRO; PR:Q3UUG6; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q3UUG6; protein.
DR Bgee; ENSMUSG00000036473; Expressed in pigmented layer of retina and 261 other tissues.
DR ExpressionAtlas; Q3UUG6; baseline and differential.
DR Genevisible; Q3UUG6; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031594; C:neuromuscular junction; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0061564; P:axon development; IMP:MGI.
DR GO; GO:0016358; P:dendrite development; IMP:MGI.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IDA:MGI.
DR GO; GO:1902083; P:negative regulation of peptidyl-cysteine S-nitrosylation; IDA:MGI.
DR GO; GO:0036475; P:neuron death in response to oxidative stress; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:2001224; P:positive regulation of neuron migration; ISO:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Cytoplasmic vesicle; GTPase activation; Membrane; Phosphoprotein;
KW Reference proteome; Synapse.
FT CHAIN 1..561
FT /note="TBC1 domain family member 24"
FT /id="PRO_0000288505"
FT DOMAIN 45..236
FT /note="Rab-GAP TBC"
FT DOMAIN 343..556
FT /note="TLDc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01234"
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 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULP9"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 322..327
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_025702"
FT CONFLICT 3
FT /note="P -> H (in Ref. 2; BAE23659)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="K -> R (in Ref. 2; BAE36174)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="K -> E (in Ref. 2; BAC39644)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="E -> G (in Ref. 2; BAC39255)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="S -> G (in Ref. 1; BAC98114)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="N -> I (in Ref. 2; BAE28046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 63236 MW; 1C35837B82FF093E CRC64;
MDPPGYNCFV DKDKMDASIQ DLGPKELNCT ELQELKQLAR QGYWAQSHTL RGKVYQRLIR
DIPCRTVTPD ASVYSDIVGK IVGKHSSSSL PLPEFVDNTQ VPTYCLNTRG EGAVRKILLC
IANQFPDISF CPALPAVVAL LLHYSIDEAE CFEKACRILS CNDPTKKLID QSFLAFESSC
MTFGDLVNKY CQAAHKLMVA VSEDVLQVYS DWQRWLFGEL PLNYFARVFD VFLVEGYKVL
YRVALAILKF FHKVRAGQPL ESDNVKQDIR MFVKDIAKTV SPEKLLEKAF AIRLFSRKEI
QLLQMANEKA LRQKGITVKQ KSVSLSKRQF VHLAVHAENF HSEIVSVKEM RDIWSWIPER
FALCQPLLLF SSLQHGYSLS RFYFQCEGHE PTLLLIKTTQ KEVCGAYLST DWSERTKFGG
KLGFFGTGEC FVFRLQPEVQ RYEWVVIKHP ELTKATSLKS SEAAGSSSLI SHCSSDPADR
LSPFLAARHF NLPSKTESMF MAGGNDCLII GGGGGQALYV DGDLNRGRTG HCDTFNNQPL
CSENFLIAAV EAWGFQDPDT E
