TBC24_HUMAN
ID TBC24_HUMAN Reviewed; 559 AA.
AC Q9ULP9; A0JNW3; B9A6M6; Q2KJ08;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=TBC1 domain family member 24;
GN Name=TBC1D24; Synonyms=KIAA1171;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-295.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-295.
RC TISSUE=Brain;
RX PubMed=19077034; DOI=10.1111/j.1365-2443.2008.01251.x;
RA Ishibashi K., Kanno E., Itoh T., Fukuda M.;
RT "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC)
RT protein that possesses Rab3A-GAP activity.";
RL Genes Cells 14:41-52(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Retinoblastoma;
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH ARF6,
RP VARIANTS FIME HIS-147 AND VAL-515, AND CHARACTERIZATION OF VARIANTS FIME
RP HIS-147 AND VAL-515.
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 [6]
RP FUNCTION, VARIANT FIME LEU-251, AND CHARACTERIZATION OF VARIANT FIME
RP LEU-251.
RX PubMed=20797691; DOI=10.1016/j.ajhg.2010.08.001;
RA Corbett M.A., Bahlo M., Jolly L., Afawi Z., Gardner A.E., Oliver K.L.,
RA Tan S., Coffey A., Mulley J.C., Dibbens L.M., Simri W., Shalata A.,
RA Kivity S., Jackson G.D., Berkovic S.F., Gecz J.;
RT "A focal epilepsy and intellectual disability syndrome is due to a mutation
RT in TBC1D24.";
RL Am. J. Hum. Genet. 87:371-375(2010).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-480, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP VARIANT DEE16 SER-229, AND CHARACTERIZATION OF VARIANT DEE16 SER-229.
RX PubMed=23526554; DOI=10.1002/humu.22318;
RA Milh M., Falace A., Villeneuve N., Vanni N., Cacciagli P., Assereto S.,
RA Nabbout R., Benfenati F., Zara F., Chabrol B., Villard L., Fassio A.;
RT "Novel compound heterozygous mutations in TBC1D24 cause familial malignant
RT migrating partial seizures of infancy.";
RL Hum. Mutat. 34:869-872(2013).
RN [10]
RP VARIANTS DFNB86 TYR-70 AND PRO-293.
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).
RN [11]
RP INVOLVEMENT IN DFNA65, AND VARIANT DFNA65 LEU-178.
RX PubMed=24729547; DOI=10.1002/humu.22558;
RA Zhang L., Hu L., Chai Y., Pang X., Yang T., Wu H.;
RT "A dominant mutation in the stereocilia-expressing gene TBC1D24 is a
RT probable cause for nonsyndromic hearing impairment.";
RL Hum. Mutat. 35:814-818(2014).
RN [12]
RP VARIANT DFNA65 LEU-178.
RX PubMed=24729539; DOI=10.1002/humu.22557;
RA Azaiez H., Booth K.T., Bu F., Huygen P., Shibata S.B., Shearer A.E.,
RA Kolbe D., Meyer N., Black-Ziegelbein E.A., Smith R.J.;
RT "TBC1D24 mutation causes autosomal-dominant nonsyndromic hearing loss.";
RL Hum. Mutat. 35:819-823(2014).
RN [13]
RP VARIANTS DOORS GLU-20; CYS-40; SER-110; CYS-242 AND PHE-333.
RX PubMed=24291220; DOI=10.1016/s1474-4422(13)70265-5;
RA Campeau P.M., Kasperaviciute D., Lu J.T., Burrage L.C., Kim C., Hori M.,
RA Powell B.R., Stewart F., Felix T.M., van den Ende J., Wisniewska M.,
RA Kayserili H., Rump P., Nampoothiri S., Aftimos S., Mey A., Nair L.D.,
RA Begleiter M.L., De Bie I., Meenakshi G., Murray M.L., Repetto G.M.,
RA Golabi M., Blair E., Male A., Giuliano F., Kariminejad A., Newman W.G.,
RA Bhaskar S.S., Dickerson J.E., Kerr B., Banka S., Giltay J.C., Wieczorek D.,
RA Tostevin A., Wiszniewska J., Cheung S.W., Hennekam R.C., Gibbs R.A.,
RA Lee B.H., Sisodiya S.M.;
RT "The genetic basis of DOORS syndrome: an exome-sequencing study.";
RL Lancet Neurol. 13:44-58(2014).
RN [14]
RP VARIANTS DEE16 ASP-113 AND PRO-159.
RX PubMed=27541164; DOI=10.1002/ajmg.a.37933;
RA Lozano R., Herman K., Rothfuss M., Rieger H., Bayrak-Toydemir P.,
RA Aprile D., Fruscione F., Zara F., Fassio A.;
RT "Clinical intrafamilial variability in lethal familial neonatal seizure
RT disorder caused by TBC1D24 mutations.";
RL Am. J. Med. Genet. A 170:3207-3214(2016).
RN [15]
RP VARIANTS EPRPDC 81-ILE--LYS-84 DEL; MET-182; HIS-360; VAL-500; ARG-501 AND
RP ARG-511, INVOLVEMENT IN EPRPDC, FUNCTION, SUBCELLULAR LOCATION, AND
RP CHARACTERIZATION OF VARIANT EPRPDC ARG-501.
RX PubMed=31257402; DOI=10.1093/brain/awz175;
RA Luethy K., Mei D., Fischer B., De Fusco M., Swerts J., Paesmans J.,
RA Parrini E., Lubarr N., Meijer I.A., Mackenzie K.M., Lee W.T., Cittaro D.,
RA Aridon P., Schoovaerts N., Versees W., Verstreken P., Casari G.,
RA Guerrini R.;
RT "TBC1D24-TLDc-related epilepsy exercise-induced dystonia: rescue by
RT antioxidants in a disease model.";
RL Brain 142:2319-2335(2019).
CC -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC protein(s) (PubMed:20727515, PubMed:20797691). Involved in neuronal
CC projections development, probably through a negative modulation of ARF6
CC function (PubMed:20727515). Involved in the regulation of synaptic
CC vesicle trafficking (PubMed:31257402). {ECO:0000269|PubMed:20727515,
CC ECO:0000269|PubMed:20797691, ECO:0000269|PubMed:31257402}.
CC -!- SUBUNIT: Interacts with ARF6. {ECO:0000269|PubMed:20727515}.
CC -!- INTERACTION:
CC Q9ULP9-2; P62330: ARF6; NbExp=2; IntAct=EBI-10968870, EBI-638181;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20727515};
CC Peripheral membrane protein {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:20727515}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9VIH7}. Presynapse
CC {ECO:0000269|PubMed:31257402}. Note=Mainly cytoplasmatic with partial
CC expression at the plasma membrane (PubMed:20727515). 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:Q9VIH7, ECO:0000269|PubMed:20727515}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ULP9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULP9-2; Sequence=VSP_025701;
CC -!- TISSUE SPECIFICITY: Highest expression in brain.
CC {ECO:0000269|PubMed:20727515}.
CC -!- DOMAIN: The Rab-GAP TBC domain is essential for phosphatidylinositol
CC binding. {ECO:0000250|UniProtKB:Q9VIH7}.
CC -!- DISEASE: Familial infantile myoclonic epilepsy (FIME) [MIM:605021]: A
CC subtype of idiopathic epilepsy starting in early infancy and
CC manifesting as myoclonic seizures, febrile convulsions, and tonic-
CC clonic seizures. {ECO:0000269|PubMed:20727515,
CC ECO:0000269|PubMed:20797691}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Developmental and epileptic encephalopathy 16 (DEE16)
CC [MIM:615338]: A severe autosomal recessive neurologic disorder
CC characterized by onset of seizures in the first weeks or months of
CC life. Seizures can be of various types, are unresponsive to medication,
CC last for long periods of time, and occur frequently. Affected infants
CC show psychomotor regression or lack of psychomotor development, as well
CC as other neurologic features such as extrapyramidal signs and
CC hypotonia. Most die in childhood. {ECO:0000269|PubMed:23526554,
CC ECO:0000269|PubMed:27541164}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Deafness, autosomal dominant, 65 (DFNA65) [MIM:616044]: A form
CC of non-syndromic sensorineural hearing loss. Sensorineural deafness
CC results from damage to the neural receptors of the inner ear, the nerve
CC pathways to the brain, or the area of the brain that receives sound
CC information. DFNA65 is characterized by postlingual onset of slowly
CC progressive hearing loss in the third decade. Initially affecting the
CC high frequencies, the hearing loss eventually affects all frequencies
CC and results in severe to profound deafness in the seventh decade.
CC Vestibular function is normal. {ECO:0000269|PubMed:24729539,
CC ECO:0000269|PubMed:24729547}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Deafness, onychodystrophy, osteodystrophy, intellectual
CC disability, and seizures syndrome (DOORS) [MIM:220500]: A syndrome
CC characterized by sensorineural deafness, intellectual disability,
CC hypoplastic or absent nails, small or absent distal phalanges of hands
CC and feet. Additional features include coarse facies, a large nose with
CC wide nasal bridge, bulbous tip and anteverted nares, a long prominent
CC philtrum and downturned corners of the mouth. Progressive neurological
CC manifestations include seizures from infancy, optic atrophy, and
CC peripheral polyneuropathy. {ECO:0000269|PubMed:24291220}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Deafness, autosomal recessive, 86 (DFNB86) [MIM:614617]: A
CC form of non-syndromic deafness characterized by prelingual onset of
CC profound sensorineural hearing loss affecting all frequencies.
CC {ECO:0000269|PubMed:24387994}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Epilepsy, rolandic, with proxysmal exercise-induce dystonia
CC and writer's cramp (EPRPDC) [MIM:608105]: An autosomal recessive
CC neurologic disorder characterized by onset of focal seizures in infancy
CC and exercise-induced dystonia in childhood. Clinical features include
CC involuntary movements and difficulties with fine motor skills of the
CC hand. {ECO:0000269|PubMed:31257402}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86485.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB032997; BAA86485.1; ALT_INIT; mRNA.
DR EMBL; AB449911; BAH16654.1; -; mRNA.
DR EMBL; BC112389; AAI12390.1; -; mRNA.
DR EMBL; BC127014; AAI27015.1; -; mRNA.
DR EMBL; BC127015; AAI27016.1; -; mRNA.
DR CCDS; CCDS42107.1; -. [Q9ULP9-2]
DR CCDS; CCDS55980.1; -. [Q9ULP9-1]
DR RefSeq; NP_001186036.1; NM_001199107.1. [Q9ULP9-1]
DR RefSeq; NP_065756.1; NM_020705.2. [Q9ULP9-2]
DR RefSeq; XP_016878982.1; XM_017023493.1. [Q9ULP9-1]
DR RefSeq; XP_016878983.1; XM_017023494.1. [Q9ULP9-2]
DR RefSeq; XP_016878984.1; XM_017023495.1. [Q9ULP9-2]
DR AlphaFoldDB; Q9ULP9; -.
DR SMR; Q9ULP9; -.
DR BioGRID; 121535; 46.
DR IntAct; Q9ULP9; 17.
DR STRING; 9606.ENSP00000293970; -.
DR iPTMnet; Q9ULP9; -.
DR MetOSite; Q9ULP9; -.
DR PhosphoSitePlus; Q9ULP9; -.
DR BioMuta; TBC1D24; -.
DR DMDM; 148887040; -.
DR EPD; Q9ULP9; -.
DR jPOST; Q9ULP9; -.
DR MassIVE; Q9ULP9; -.
DR MaxQB; Q9ULP9; -.
DR PaxDb; Q9ULP9; -.
DR PeptideAtlas; Q9ULP9; -.
DR PRIDE; Q9ULP9; -.
DR ProteomicsDB; 85090; -. [Q9ULP9-1]
DR ProteomicsDB; 85091; -. [Q9ULP9-2]
DR Antibodypedia; 42567; 65 antibodies from 19 providers.
DR DNASU; 57465; -.
DR Ensembl; ENST00000567020.6; ENSP00000454408.1; ENSG00000162065.14. [Q9ULP9-2]
DR Ensembl; ENST00000569874.2; ENSP00000455005.2; ENSG00000162065.14. [Q9ULP9-2]
DR Ensembl; ENST00000627285.1; ENSP00000486121.1; ENSG00000162065.14. [Q9ULP9-2]
DR Ensembl; ENST00000646147.1; ENSP00000494678.1; ENSG00000162065.14. [Q9ULP9-1]
DR GeneID; 57465; -.
DR KEGG; hsa:57465; -.
DR MANE-Select; ENST00000646147.1; ENSP00000494678.1; NM_001199107.2; NP_001186036.1.
DR UCSC; uc002cqk.4; human. [Q9ULP9-1]
DR CTD; 57465; -.
DR DisGeNET; 57465; -.
DR GeneCards; TBC1D24; -.
DR GeneReviews; TBC1D24; -.
DR HGNC; HGNC:29203; TBC1D24.
DR HPA; ENSG00000162065; Tissue enhanced (salivary).
DR MalaCards; TBC1D24; -.
DR MIM; 220500; phenotype.
DR MIM; 605021; phenotype.
DR MIM; 608105; phenotype.
DR MIM; 613577; gene.
DR MIM; 614617; phenotype.
DR MIM; 615338; phenotype.
DR MIM; 616044; phenotype.
DR neXtProt; NX_Q9ULP9; -.
DR OpenTargets; ENSG00000162065; -.
DR Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR Orphanet; 79500; DOORS syndrome.
DR Orphanet; 352582; Familial infantile myoclonic epilepsy.
DR Orphanet; 352587; Focal epilepsy-intellectual disability-cerebro-cerebellar malformation.
DR Orphanet; 293181; Malignant migrating focal seizures of infancy.
DR Orphanet; 352596; Progressive myoclonic epilepsy with dystonia.
DR Orphanet; 163727; Rolandic epilepsy-paroxysmal exercise-induced dystonia-writer's cramp syndrome.
DR PharmGKB; PA144596267; -.
DR VEuPathDB; HostDB:ENSG00000162065; -.
DR eggNOG; KOG2801; Eukaryota.
DR GeneTree; ENSGT00410000025739; -.
DR HOGENOM; CLU_018035_1_1_1; -.
DR InParanoid; Q9ULP9; -.
DR OMA; MINDTSH; -.
DR OrthoDB; 1047825at2759; -.
DR PhylomeDB; Q9ULP9; -.
DR TreeFam; TF315420; -.
DR PathwayCommons; Q9ULP9; -.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR SignaLink; Q9ULP9; -.
DR BioGRID-ORCS; 57465; 20 hits in 1076 CRISPR screens.
DR GenomeRNAi; 57465; -.
DR Pharos; Q9ULP9; Tbio.
DR PRO; PR:Q9ULP9; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9ULP9; protein.
DR Bgee; ENSG00000162065; Expressed in parotid gland and 166 other tissues.
DR ExpressionAtlas; Q9ULP9; baseline and differential.
DR Genevisible; Q9ULP9; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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; IDA:HPA.
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; IEA:Ensembl.
DR GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IEA:Ensembl.
DR GO; GO:1902083; P:negative regulation of peptidyl-cysteine S-nitrosylation; IEA:Ensembl.
DR GO; GO:0036475; P:neuron death in response to oxidative stress; IDA:MGI.
DR GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:2001224; P:positive regulation of neuron migration; IEA:Ensembl.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Cytoplasmic vesicle; Deafness; Disease variant; Epilepsy;
KW GTPase activation; Intellectual disability; Membrane;
KW Non-syndromic deafness; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..559
FT /note="TBC1 domain family member 24"
FT /id="PRO_0000288504"
FT DOMAIN 47..262
FT /note="Rab-GAP TBC"
FT DOMAIN 343..554
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 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 322..327
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025701"
FT VARIANT 20
FT /note="Q -> E (in DOORS; dbSNP:rs201257588)"
FT /evidence="ECO:0000269|PubMed:24291220"
FT /id="VAR_070912"
FT VARIANT 40
FT /note="R -> C (in DOORS; dbSNP:rs398122966)"
FT /evidence="ECO:0000269|PubMed:24291220"
FT /id="VAR_070913"
FT VARIANT 70
FT /note="D -> Y (in DFNB86; dbSNP:rs587777147)"
FT /evidence="ECO:0000269|PubMed:24387994"
FT /id="VAR_070994"
FT VARIANT 81..84
FT /note="Missing (in EPRPDC)"
FT /evidence="ECO:0000269|PubMed:31257402"
FT /id="VAR_083253"
FT VARIANT 110
FT /note="G -> S (in DOORS; unknown pathological significance;
FT dbSNP:rs747821285)"
FT /evidence="ECO:0000269|PubMed:24291220"
FT /id="VAR_070914"
FT VARIANT 113
FT /note="A -> D (in DEE16; dbSNP:rs770820144)"
FT /evidence="ECO:0000269|PubMed:27541164"
FT /id="VAR_078184"
FT VARIANT 147
FT /note="D -> H (in FIME; significantly impairs the
FT interaction with ARF6; partially induces neurite overgrowth
FT when overexpressed in primary cortical neurons;
FT dbSNP:rs267607103)"
FT /evidence="ECO:0000269|PubMed:20727515"
FT /id="VAR_064365"
FT VARIANT 159
FT /note="L -> P (in DEE16; dbSNP:rs863223337)"
FT /evidence="ECO:0000269|PubMed:27541164"
FT /id="VAR_078185"
FT VARIANT 178
FT /note="S -> L (in DFNA65; dbSNP:rs483352866)"
FT /evidence="ECO:0000269|PubMed:24729539,
FT ECO:0000269|PubMed:24729547"
FT /id="VAR_072107"
FT VARIANT 182
FT /note="T -> M (in EPRPDC; unknown pathological
FT significance; dbSNP:rs763670146)"
FT /evidence="ECO:0000269|PubMed:31257402"
FT /id="VAR_083254"
FT VARIANT 229
FT /note="F -> S (in DEE16; loss of function mutation; impairs
FT the interaction with ARF6; overexpression of the mutant
FT protein in primary cortical neurons abolishes the ability
FT to increase neurite length and arborization;
FT dbSNP:rs397514713)"
FT /evidence="ECO:0000269|PubMed:23526554"
FT /id="VAR_070102"
FT VARIANT 242
FT /note="R -> C (in DOORS; dbSNP:rs398122965)"
FT /evidence="ECO:0000269|PubMed:24291220"
FT /id="VAR_070915"
FT VARIANT 251
FT /note="F -> L (in FIME; fails to induce neurite overgrowth
FT when overexpressed in primary cortical neurons;
FT dbSNP:rs267607104)"
FT /evidence="ECO:0000269|PubMed:20797691"
FT /id="VAR_064366"
FT VARIANT 293
FT /note="R -> P (in DFNB86; dbSNP:rs199700840)"
FT /evidence="ECO:0000269|PubMed:24387994"
FT /id="VAR_070995"
FT VARIANT 295
FT /note="F -> L (in dbSNP:rs72768728)"
FT /evidence="ECO:0000269|PubMed:10574461,
FT ECO:0000269|PubMed:19077034"
FT /id="VAR_070890"
FT VARIANT 333
FT /note="L -> F (in DOORS; dbSNP:rs797044548)"
FT /evidence="ECO:0000269|PubMed:24291220"
FT /id="VAR_070916"
FT VARIANT 360
FT /note="R -> H (in EPRPDC; dbSNP:rs765965968)"
FT /evidence="ECO:0000269|PubMed:31257402"
FT /id="VAR_083255"
FT VARIANT 500
FT /note="A -> V (in EPRPDC; dbSNP:rs564477999)"
FT /evidence="ECO:0000269|PubMed:31257402"
FT /id="VAR_083256"
FT VARIANT 501
FT /note="G -> R (in EPRPDC; results in synaptic vesicle
FT trafficking defects when expressed in a heterologous
FT system; does not affect localization to presynapse when
FT expressed in a heterologous system; dbSNP:rs1596973014)"
FT /evidence="ECO:0000269|PubMed:31257402"
FT /id="VAR_083257"
FT VARIANT 511
FT /note="G -> R (in EPRPDC; unknown pathological
FT significance; dbSNP:rs1251822607)"
FT /evidence="ECO:0000269|PubMed:31257402"
FT /id="VAR_083258"
FT VARIANT 515
FT /note="A -> V (in FIME; does not affect the interaction
FT with ARF6; fails to induce neurite overgrowth when
FT overexpressed in primary cortical neurons;
FT dbSNP:rs267607105)"
FT /evidence="ECO:0000269|PubMed:20727515"
FT /id="VAR_064367"
SQ SEQUENCE 559 AA; 62919 MW; 0F4EA43297ACC7F9 CRC64;
MDSPGYNCFV DKDKMDAAIQ DLGPKELSCT ELQELKQLAR QGYWAQSHAL RGKVYQRLIR
DIPCRTVTPD ASVYSDIVGK IVGKHSSSCL PLPEFVDNTQ VPSYCLNARG EGAVRKILLC
LANQFPDISF CPALPAVVAL LLHYSIDEAE CFEKACRILA CNDPGRRLID QSFLAFESSC
MTFGDLVNKY CQAAHKLMVA VSEDVLQVYA DWQRWLFGEL PLCYFARVFD VFLVEGYKVL
YRVALAILKF FHKVRAGQPL ESDSVKQDIR TFVRDIAKTV SPEKLLEKAF AIRLFSRKEI
QLLQMANEKA LKQKGITVKQ KSVSLSKRQF VHLAVHAENF RSEIVSVREM RDIWSWVPER
FALCQPLLLF SSLQHGYSLA RFYFQCEGHE PTLLLIKTTQ KEVCGAYLST DWSERNKFGG
KLGFFGTGEC FVFRLQPEVQ RYEWVVIKHP ELTKPPPLMA AEPTAPLSHS ASSDPADRLS
PFLAARHFNL PSKTESMFMA GGSDCLIVGG GGGQALYIDG DLNRGRTSHC DTFNNQPLCS
ENFLIAAVEA WGFQDPDTQ
