CTL4_HUMAN
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 03-AUG-2022, entry version 148.
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,
GN TPPT1 {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.
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, AND ALTERNATIVE SPLICING.
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, AND CHARACTERIZATION
RP OF VARIANTS LEU-6; VAL-123 AND SER-397.
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, AND
RP CHARACTERIZATION OF VARIANT DFNA72 VAL-156.
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).
CC {ECO:0000250|UniProtKB:Q7T2B0, ECO:0000269|PubMed:23651124,
CC ECO:0000269|PubMed:24379411, ECO:0000269|PubMed:28013291}.
CC -!- FUNCTION: [Isoform 3]: Has also thiamine pyrophosphate transporter
CC activity. {ECO:0000269|PubMed:24379411}.
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 -!- 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.
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 GlyGen; Q53GD3; 7 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q53GD3; -.
DR PhosphoSitePlus; Q53GD3; -.
DR BioMuta; SLC44A4; -.
DR DMDM; 311033368; -.
DR jPOST; Q53GD3; -.
DR MassIVE; Q53GD3; -.
DR MaxQB; Q53GD3; -.
DR PaxDb; Q53GD3; -.
DR PeptideAtlas; Q53GD3; -.
DR PRIDE; Q53GD3; -.
DR ProteomicsDB; 19913; -.
DR ProteomicsDB; 5163; -.
DR ProteomicsDB; 5359; -.
DR ProteomicsDB; 62477; -. [Q53GD3-1]
DR ProteomicsDB; 62478; -. [Q53GD3-2]
DR Antibodypedia; 71079; 61 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 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; 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 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; 15 hits in 1069 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 91 other tissues.
DR ExpressionAtlas; Q53GD3; baseline and differential.
DR Genevisible; Q53GD3; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0015220; F:choline transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0090422; F:thiamine pyrophosphate transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
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; IMP: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; IBA:GO_Central.
DR InterPro; IPR007603; Choline_transptr-like.
DR PANTHER; PTHR12385; PTHR12385; 1.
DR Pfam; PF04515; Choline_transpo; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Deafness; Disease variant;
KW Glycoprotein; Membrane; Non-syndromic deafness; Reference proteome;
KW Transmembrane; Transmembrane helix.
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
