ID CTL4_HUMAN Reviewed; 710 AA. AC Q53GD3; A2BED3; B0UXX8; B0UZY8; B4DU94; B4DWM2; E9PEK7; Q5JP84; Q5JQ93; AC Q658S8; Q6UX89; Q8TEW4; Q96C58; Q96K59; Q9Y332; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 2. DT 24-JAN-2024, entry version 156. DE RecName: Full=Choline transporter-like protein 4 {ECO:0000303|PubMed:23651124}; DE AltName: Full=Solute carrier family 44 member 4 {ECO:0000312|HGNC:HGNC:13941}; DE AltName: Full=Thiamine pyrophosphate transporter 1 {ECO:0000303|PubMed:24379411}; DE Short=hTPPT1 {ECO:0000303|PubMed:24379411}; GN Name=SLC44A4 {ECO:0000312|HGNC:HGNC:13941}; GN Synonyms=C6orf29, CTL4 {ECO:0000303|PubMed:23651124}, NG22, TPPT1 GN {ECO:0000303|PubMed:24379411}; ORFNames=UNQ441/PRO874; 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] (ISOFORMS 1; 3 AND 4), AND VARIANTS RP ILE-187 AND VAL-326. RC TISSUE=Mammary gland, and Prostate; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ILE-187 RP AND VAL-326. RC TISSUE=Small intestine; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ILE-187 AND RP VAL-326. RX PubMed=14656967; DOI=10.1101/gr.1736803; RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., RA Hood L.; RT "Analysis of the gene-dense major histocompatibility complex class III RT region and its comparison to mouse."; RL Genome Res. 13:2621-2636(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ILE-187 AND RP VAL-326. RA Shiina S., Tamiya G., Oka A., Inoko H.; RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ILE-187 AND RP VAL-326. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ILE-187 AND RP VAL-326. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLU-128; RP ILE-187 AND VAL-326. RC TISSUE=Colon; 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 [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-308 (ISOFORM 1), CHROMOSOMAL REARRANGEMENT RP WITH NEU1, AND VARIANT ILE-187. RX PubMed=12067718; DOI=10.1016/s0014-5793(02)02748-5; RA Uhl J., Penzel R., Sergi C., Kopitz J., Otto H.F., Cantz M.; RT "Identification of a CTL4/Neu1 fusion transcript in a sialidosis patient."; RL FEBS Lett. 521:19-23(2002). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 81-710 (ISOFORMS 1/3). RC TISSUE=Stomach; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [11] RP IDENTIFICATION, AND NOMENCLATURE. RX PubMed=10677542; DOI=10.1073/pnas.030339697; RA O'Regan S., Traiffort E., Ruat M., Cha N., Compaore D., Meunier F.-M.; RT "An electric lobe suppressor for a yeast choline transport mutation belongs RT to a new family of transporter-like proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 97:1835-1840(2000). RN [12] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=23651124; DOI=10.1111/jnc.12298; RA Song P., Rekow S.S., Singleton C.A., Sekhon H.S., Dissen G.A., Zhou M., RA Campling B., Lindstrom J., Spindel E.R.; RT "Choline transporter-like protein 4 (CTL4) links to non-neuronal RT acetylcholine synthesis."; RL J. Neurochem. 126:451-461(2013). RN [13] RP FUNCTION, FUNCTION (ISOFORM 3), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, RP BIOPHYSICOCHEMICAL PROPERTIES, ALTERNATIVE SPLICING, AND TRANSPORTER RP ACTIVITY. RX PubMed=24379411; DOI=10.1074/jbc.m113.528257; RA Nabokina S.M., Inoue K., Subramanian V.S., Valle J.E., Yuasa H., Said H.M.; RT "Molecular identification and functional characterization of the human RT colonic thiamine pyrophosphate transporter."; RL J. Biol. Chem. 289:4405-4416(2014). RN [14] RP FUNCTION, GLYCOSYLATION AT ASN-69; ASN-155; ASN-197 AND ASN-416, RP MUTAGENESIS OF ASN-29; ASN-69; ASN-155; ASN-197; ASN-298; ASN-393; ASN-409 RP AND ASN-416, AND SUBCELLULAR LOCATION. RX PubMed=26828122; DOI=10.1016/j.bbamem.2016.01.028; RA Nabokina S.M., Subramanian V.S., Said H.M.; RT "The human colonic thiamine pyrophosphate transporter (hTPPT) is a RT glycoprotein and N-linked glycosylation is important for its function."; RL Biochim. Biophys. Acta 1858:866-871(2016). RN [15] RP VARIANTS [LARGE SCALE ANALYSIS] THR-347 AND MET-411. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [16] RP VARIANTS LEU-6; VAL-123; ILE-187; VAL-326 AND SER-397, CHARACTERIZATION OF RP VARIANTS LEU-6; VAL-123 AND SER-397, TRANSPORTER ACTIVITY, AND FUNCTION. RX PubMed=26741288; DOI=10.1038/gene.2015.53; RA Gupta A., Thelma B.K.; RT "Identification of critical variants within SLC44A4, an ulcerative colitis RT susceptibility gene identified in a GWAS in north Indians."; RL Genes Immun. 17:105-109(2016). RN [17] RP FUNCTION, INVOLVEMENT IN DFNA72, VARIANT DFNA72 VAL-156, CHARACTERIZATION RP OF VARIANT DFNA72 VAL-156, AND TRANSPORTER ACTIVITY. RX PubMed=28013291; DOI=10.1093/hmg/ddw394; RA Ma Z., Xia W., Liu F., Ma J., Sun S., Zhang J., Jiang N., Wang X., Hu J., RA Ma D.; RT "SLC44A4 mutation causes autosomal dominant hereditary postlingual non- RT syndromic mid-frequency hearing loss."; RL Hum. Mol. Genet. 26:383-394(2017). CC -!- FUNCTION: Choline transporter that plays a role in the choline- CC acetylcholine system and is required to the efferent innervation of CC hair cells in the olivocochlear bundle for the maintenance of CC physiological function of outer hair cells and the protection of hair CC cells from acoustic injury (By similarity) (PubMed:23651124, CC PubMed:28013291). Also described as a thiamine pyrophosphate CC transporter in colon, may mediate the absorption of microbiota- CC generated thiamine pyrophosphate and contribute to host thiamine CC (vitamin B1) homeostasis (PubMed:24379411, PubMed:26741288). CC {ECO:0000250|UniProtKB:Q7T2B0, ECO:0000269|PubMed:23651124, CC ECO:0000269|PubMed:24379411, ECO:0000269|PubMed:26741288, CC ECO:0000269|PubMed:28013291}. CC -!- FUNCTION: [Isoform 3]: Has also thiamine pyrophosphate transporter CC activity. {ECO:0000269|PubMed:24379411}. CC -!- CATALYTIC ACTIVITY: CC Reaction=choline(out) + n H(+)(in) = choline(in) + n H(+)(out); CC Xref=Rhea:RHEA:75463, ChEBI:CHEBI:15354, ChEBI:CHEBI:15378; CC Evidence={ECO:0000269|PubMed:23651124, ECO:0000269|PubMed:28013291}; CC -!- CATALYTIC ACTIVITY: CC Reaction=thiamine diphosphate(out) = thiamine diphosphate(in); CC Xref=Rhea:RHEA:75471, ChEBI:CHEBI:58937; CC Evidence={ECO:0000269|PubMed:24379411, ECO:0000269|PubMed:26741288}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.17 uM for thiamine pyrophosphate {ECO:0000269|PubMed:24379411}; CC Vmax=18.19 pmol/min/mg enzyme {ECO:0000269|PubMed:24379411}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:24379411, CC ECO:0000269|PubMed:26828122}; Multi-pass membrane protein CC {ECO:0000305|PubMed:24379411, ECO:0000305|PubMed:26828122}. Apical cell CC membrane {ECO:0000269|PubMed:24379411}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q53GD3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q53GD3-2; Sequence=VSP_030998; CC Name=3; CC IsoId=Q53GD3-3; Sequence=VSP_046236; CC Name=4; CC IsoId=Q53GD3-4; Sequence=VSP_046821; CC -!- TISSUE SPECIFICITY: Highly expressed in colon, also detected in CC prostate, trachea and lung (PubMed:24379411). Isoform 3 is also CC expressed in colon but a lower levels (PubMed:24379411). CC {ECO:0000269|PubMed:24379411}. CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in colon at low levels. CC {ECO:0000269|PubMed:24379411}. CC -!- PTM: N-glycosylated; N-glycosylation of Asn-69, Asn-155 and Asn-393 is CC required for a proper thiamine pyrophosphate uptake. CC {ECO:0000269|PubMed:26828122}. CC -!- DISEASE: Note=An interstitial deletion causing the fusion of exon 10 of CC CTL4 with the 3'-UTR of NEU has been detected in two patients affected CC by sialidosis. {ECO:0000269|PubMed:12067718}. CC -!- DISEASE: Deafness, autosomal dominant, 72 (DFNA72) [MIM:617606]: 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. DFNA72 primarily affects the middle frequencies. It CC gradually progresses to whole-frequency hearing loss. CC {ECO:0000269|PubMed:28013291}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the CTL (choline transporter-like) family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK027397; BAB55083.1; -; mRNA. DR EMBL; AK300550; BAG62256.1; -; mRNA. DR EMBL; AK301596; BAG63084.1; -; mRNA. DR EMBL; AY358457; AAQ88822.1; -; mRNA. DR EMBL; AK222998; BAD96718.1; -; mRNA. DR EMBL; AF134726; AAD21813.1; -; Genomic_DNA. DR EMBL; BA000025; BAB63296.1; -; Genomic_DNA. DR EMBL; AL662834; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL671762; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL844853; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX005460; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR388202; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759784; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR936237; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03538.1; -; Genomic_DNA. DR EMBL; BC014659; AAH14659.1; -; mRNA. DR EMBL; AF466766; AAL75992.1; -; mRNA. DR EMBL; AL833009; CAH56275.1; -; mRNA. DR CCDS; CCDS4724.2; -. [Q53GD3-1] DR CCDS; CCDS54989.1; -. [Q53GD3-3] DR CCDS; CCDS54990.1; -. [Q53GD3-4] DR RefSeq; NP_001171515.1; NM_001178044.1. [Q53GD3-4] DR RefSeq; NP_001171516.1; NM_001178045.1. [Q53GD3-3] DR RefSeq; NP_079533.2; NM_025257.2. [Q53GD3-1] DR AlphaFoldDB; Q53GD3; -. DR BioGRID; 123281; 3. DR IntAct; Q53GD3; 2. DR STRING; 9606.ENSP00000229729; -. DR ChEMBL; CHEMBL3713014; -. DR DrugBank; DB00122; Choline. DR DrugBank; DB14006; Choline salicylate. DR TCDB; 2.A.92.1.7; the choline transporter-like (ctl) family. DR GlyConnect; 1112; 3 N-Linked glycans (1 site). DR GlyCosmos; Q53GD3; 7 sites, 2 glycans. DR GlyGen; Q53GD3; 7 sites, 2 N-linked glycans (1 site). DR iPTMnet; Q53GD3; -. DR PhosphoSitePlus; Q53GD3; -. DR SwissPalm; Q53GD3; -. DR BioMuta; SLC44A4; -. DR DMDM; 311033368; -. DR jPOST; Q53GD3; -. DR MassIVE; Q53GD3; -. DR MaxQB; Q53GD3; -. DR PaxDb; 9606-ENSP00000229729; -. DR PeptideAtlas; Q53GD3; -. DR ProteomicsDB; 19913; -. DR ProteomicsDB; 5163; -. DR ProteomicsDB; 5359; -. DR ProteomicsDB; 62477; -. [Q53GD3-1] DR ProteomicsDB; 62478; -. [Q53GD3-2] DR Antibodypedia; 71079; 67 antibodies from 12 providers. DR DNASU; 80736; -. DR Ensembl; ENST00000229729.11; ENSP00000229729.6; ENSG00000204385.13. [Q53GD3-1] DR Ensembl; ENST00000375562.8; ENSP00000364712.4; ENSG00000204385.13. [Q53GD3-4] DR Ensembl; ENST00000383379.8; ENSP00000372870.4; ENSG00000206378.10. [Q53GD3-1] DR Ensembl; ENST00000415517.6; ENSP00000414120.2; ENSG00000229077.8. DR Ensembl; ENST00000417894.6; ENSP00000389244.2; ENSG00000235336.8. DR Ensembl; ENST00000425238.6; ENSP00000399161.2; ENSG00000228263.8. [Q53GD3-1] DR Ensembl; ENST00000442152.6; ENSP00000398852.2; ENSG00000232180.8. DR Ensembl; ENST00000453831.6; ENSP00000393939.2; ENSG00000231479.8. [Q53GD3-1] DR Ensembl; ENST00000544672.5; ENSP00000444109.1; ENSG00000204385.13. [Q53GD3-3] DR Ensembl; ENST00000546461.3; ENSP00000449039.1; ENSG00000231479.8. [Q53GD3-3] DR Ensembl; ENST00000547493.1; ENSP00000449232.1; ENSG00000229077.8. DR Ensembl; ENST00000547684.1; ENSP00000449180.1; ENSG00000206378.10. [Q53GD3-3] DR Ensembl; ENST00000548188.1; ENSP00000447560.1; ENSG00000228263.8. [Q53GD3-3] DR Ensembl; ENST00000549663.5; ENSP00000449642.1; ENSG00000228263.8. [Q53GD3-4] DR Ensembl; ENST00000549677.5; ENSP00000449518.1; ENSG00000206378.10. [Q53GD3-4] DR Ensembl; ENST00000550401.2; ENSP00000448474.1; ENSG00000235336.8. DR Ensembl; ENST00000551168.3; ENSP00000448088.1; ENSG00000231479.8. [Q53GD3-4] DR Ensembl; ENST00000553121.5; ENSP00000447704.1; ENSG00000232180.8. DR GeneID; 80736; -. DR KEGG; hsa:80736; -. DR MANE-Select; ENST00000229729.11; ENSP00000229729.6; NM_025257.3; NP_079533.2. DR UCSC; uc010jti.4; human. [Q53GD3-1] DR AGR; HGNC:13941; -. DR CTD; 80736; -. DR DisGeNET; 80736; -. DR GeneCards; SLC44A4; -. DR HGNC; HGNC:13941; SLC44A4. DR HPA; ENSG00000204385; Tissue enhanced (intestine, prostate, stomach). DR MalaCards; SLC44A4; -. DR MIM; 606107; gene. DR MIM; 617606; phenotype. DR neXtProt; NX_Q53GD3; -. DR OpenTargets; ENSG00000204385; -. DR Orphanet; 90635; Rare autosomal dominant non-syndromic sensorineural deafness type DFNA. DR PharmGKB; PA25930; -. DR VEuPathDB; HostDB:ENSG00000204385; -. DR eggNOG; KOG1362; Eukaryota. DR GeneTree; ENSGT00940000160576; -. DR HOGENOM; CLU_017181_3_1_1; -. DR InParanoid; Q53GD3; -. DR OMA; MNSSCPG; -. DR OrthoDB; 551961at2759; -. DR PhylomeDB; Q53GD3; -. DR TreeFam; TF313325; -. DR PathwayCommons; Q53GD3; -. DR Reactome; R-HSA-1483191; Synthesis of PC. DR Reactome; R-HSA-425366; Transport of bile salts and organic acids, metal ions and amine compounds. DR SignaLink; Q53GD3; -. DR BioGRID-ORCS; 80736; 17 hits in 1147 CRISPR screens. DR ChiTaRS; SLC44A4; human. DR GeneWiki; SLC44A4; -. DR GenomeRNAi; 80736; -. DR Pharos; Q53GD3; Tbio. DR PRO; PR:Q53GD3; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q53GD3; Protein. DR Bgee; ENSG00000204385; Expressed in mucosa of transverse colon and 93 other cell types or tissues. DR ExpressionAtlas; Q53GD3; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW. DR GO; GO:0015220; F:choline transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0090422; F:thiamine pyrophosphate transmembrane transporter activity; IMP:UniProtKB. DR GO; GO:0008292; P:acetylcholine biosynthetic process; IMP:UniProtKB. DR GO; GO:0061526; P:acetylcholine secretion; IMP:UniProtKB. DR GO; GO:0015871; P:choline transport; IDA:UniProtKB. DR GO; GO:0035675; P:neuromast hair cell development; ISS:UniProtKB. DR GO; GO:0032475; P:otolith formation; ISS:UniProtKB. DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; TAS:Reactome. DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB. DR GO; GO:0030974; P:thiamine pyrophosphate transmembrane transport; IDA:UniProtKB. DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome. DR InterPro; IPR007603; Choline_transptr-like. DR PANTHER; PTHR12385; CHOLINE TRANSPORTER-LIKE (SLC FAMILY 44); 1. DR PANTHER; PTHR12385:SF37; CHOLINE TRANSPORTER-LIKE PROTEIN 4; 1. DR Pfam; PF04515; Choline_transpo; 1. DR Genevisible; Q53GD3; HS. PE 1: Evidence at protein level; KW Alternative splicing; Antiport; Cell membrane; Deafness; Disease variant; KW Glycoprotein; Membrane; Non-syndromic deafness; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..710 FT /note="Choline transporter-like protein 4" FT /id="PRO_0000191723" FT TOPO_DOM 1..34 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 35..55 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 56..229 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 230..250 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 251..252 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 253..273 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 274..309 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 310..330 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 331..358 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 359..379 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 380..455 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 456..476 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 477..501 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 502..522 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 523..560 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 561..581 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 582..597 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 598..618 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 619..638 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 639..659 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 660..710 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT SITE 308 FT /note="Breakpoint for translocation with NEU1" FT CARBOHYD 69 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:26828122" FT CARBOHYD 155 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:26828122" FT CARBOHYD 197 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:26828122" FT CARBOHYD 298 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 393 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:26828122" FT CARBOHYD 405 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 416 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:26828122" FT VAR_SEQ 1..422 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12975309" FT /id="VSP_030998" FT VAR_SEQ 1..76 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046236" FT VAR_SEQ 115..156 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046821" FT VARIANT 6 FT /note="R -> L (no effect on thiamine pyrophosphate FT transporter activity; dbSNP:rs2075798)" FT /evidence="ECO:0000269|PubMed:26741288" FT /id="VAR_023406" FT VARIANT 123 FT /note="D -> V (no effect on thiamine pyrophosphate FT transporter activity; dbSNP:rs12661281)" FT /evidence="ECO:0000269|PubMed:26741288" FT /id="VAR_047020" FT VARIANT 128 FT /note="G -> E (in dbSNP:rs17856465)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_047021" FT VARIANT 156 FT /note="M -> V (in DFNA72; decreases choline transmembrane FT transporter activity; dbSNP:rs1135402753)" FT /evidence="ECO:0000269|PubMed:28013291" FT /id="VAR_078848" FT VARIANT 187 FT /note="V -> I (in dbSNP:rs2242665)" FT /evidence="ECO:0000269|PubMed:12067718, FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:14656967, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:26741288, ECO:0000269|Ref.3, FT ECO:0000269|Ref.5, ECO:0000269|Ref.7" FT /id="VAR_023407" FT VARIANT 326 FT /note="M -> V (in dbSNP:rs644827)" FT /evidence="ECO:0000269|PubMed:14574404, FT ECO:0000269|PubMed:14656967, ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:26741288, FT ECO:0000269|Ref.3, ECO:0000269|Ref.5, ECO:0000269|Ref.7" FT /id="VAR_023408" FT VARIANT 347 FT /note="A -> T (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036210" FT VARIANT 397 FT /note="P -> S (no effect on thiamine pyrophosphate FT transporter activity; dbSNP:rs116706632)" FT /evidence="ECO:0000269|PubMed:26741288" FT /id="VAR_078849" FT VARIANT 411 FT /note="T -> M (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs563426936)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036211" FT VARIANT 493 FT /note="R -> C (in dbSNP:rs6915800)" FT /id="VAR_023409" FT MUTAGEN 29 FT /note="N->D: No effect on glycosylation." FT /evidence="ECO:0000269|PubMed:26828122" FT MUTAGEN 69 FT /note="N->D: Decreases glycosylation levels. Decreases FT thiamine pyrophosphate uptake." FT /evidence="ECO:0000269|PubMed:26828122" FT MUTAGEN 155 FT /note="N->D: Decreases glycosylation levels. Decreases FT thiamine pyrophosphate uptake." FT /evidence="ECO:0000269|PubMed:26828122" FT MUTAGEN 197 FT /note="N->D: Decreases glycosylation levels. No effect on FT thiamine pyrophosphate uptake." FT /evidence="ECO:0000269|PubMed:26828122" FT MUTAGEN 298 FT /note="N->D: No effect on glycosylation." FT /evidence="ECO:0000269|PubMed:26828122" FT MUTAGEN 393 FT /note="N->D: Decreases glycosylation levels. Decreases FT thiamine pyrophosphate uptake." FT /evidence="ECO:0000269|PubMed:26828122" FT MUTAGEN 409 FT /note="N->D: No effect on glycosylation." FT /evidence="ECO:0000269|PubMed:26828122" FT MUTAGEN 416 FT /note="N->D: Decreases glycosylation levels. No effect on FT thiamine pyrophosphate uptake." FT /evidence="ECO:0000269|PubMed:26828122" FT CONFLICT 117..118 FT /note="Missing (in Ref. 10; CAH56275)" FT /evidence="ECO:0000305" FT CONFLICT 144..145 FT /note="NR -> SS (in Ref. 1; BAB55083)" FT /evidence="ECO:0000305" FT CONFLICT 379..386 FT /note="LATSGQPQ -> PLPTQPATLG (in Ref. 4; AAD21813 and 5; FT BAB63296)" FT /evidence="ECO:0000305" FT CONFLICT 636 FT /note="Missing (in Ref. 8; AAH14659)" FT /evidence="ECO:0000305" SQ SEQUENCE 710 AA; 79254 MW; 4DE5B45574C408AD CRC64; MGGKQRDEDD EAYGKPVKYD PSFRGPIKNR SCTDVICCVL FLLFILGYIV VGIVAWLYGD PRQVLYPRNS TGAYCGMGEN KDKPYLLYFN IFSCILSSNI ISVAENGLQC PTPQVCVSSC PEDPWTVGKN EFSQTVGEVF YTKNRNFCLP GVPWNMTVIT SLQQELCPSF LLPSAPALGR CFPWTNVTPP ALPGITNDTT IQQGISGLID SLNARDISVK IFEDFAQSWY WILVALGVAL VLSLLFILLL RLVAGPLVLV LILGVLGVLA YGIYYCWEEY RVLRDKGASI SQLGFTTNLS AYQSVQETWL AALIVLAVLE AILLLMLIFL RQRIRIAIAL LKEASKAVGQ MMSTMFYPLV TFVLLLICIA YWAMTALYLA TSGQPQYVLW ASNISSPGCE KVPINTSCNP TAHLVNSSCP GLMCVFQGYS SKGLIQRSVF NLQIYGVLGL FWTLNWVLAL GQCVLAGAFA SFYWAFHKPQ DIPTFPLISA FIRTLRYHTG SLAFGALILT LVQIARVILE YIDHKLRGVQ NPVARCIMCC FKCCLWCLEK FIKFLNRNAY IMIAIYGKNF CVSAKNAFML LMRNIVRVVV LDKVTDLLLF FGKLLVVGGV GVLSFFFFSG RIPGLGKDFK SPHLNYYWLP IMTSILGAYV IASGFFSVFG MCVDTLFLCF LEDLERNNGS LDRPYYMSKS LLKILGKKNE APPDNKKRKK //