CTL4_MOUSE
ID CTL4_MOUSE Reviewed; 707 AA.
AC Q91VA1; Q7TQ02; Q9CVA7;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Choline transporter-like protein 4 {ECO:0000305};
DE AltName: Full=Solute carrier family 44 member 4 {ECO:0000312|MGI:MGI:1917379};
DE AltName: Full=Thiamine pyrophosphate transporter 1 {ECO:0000303|PubMed:24379411};
DE Short=mTPPT1 {ECO:0000303|PubMed:24379411};
GN Name=Slc44a4 {ECO:0000312|MGI:MGI:1917379};
GN Synonyms=Ctl4 {ECO:0000305}, Ng22, TPPT1 {ECO:0000303|PubMed:24379411};
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 GENOMIC DNA].
RC STRAIN=129;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Blastocyst, and Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 340-707.
RC STRAIN=C57BL/6J; TISSUE=Stomach;
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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
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).
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). Also described as a
CC thiamine pyrophosphate transporter in colon, may mediate the absorption
CC of microbiota-generated thiamine pyrophosphate and contribute to host
CC thiamine (vitamin B1) homeostasis (PubMed:24379411).
CC {ECO:0000250|UniProtKB:Q53GD3, ECO:0000250|UniProtKB:Q7T2B0,
CC ECO:0000269|PubMed:24379411}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q53GD3}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q53GD3}. Apical cell
CC membrane {ECO:0000250|UniProtKB:Q53GD3}.
CC -!- TISSUE SPECIFICITY: Expressed in colon and cecum.
CC {ECO:0000269|PubMed:24379411}.
CC -!- PTM: N-glycosylated; N-glycosylation of Asn-67 and Asn-391 is required
CC for a proper thiamine pyrophosphate uptake.
CC {ECO:0000250|UniProtKB:Q53GD3}.
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; AF109906; AAC84166.1; -; Genomic_DNA.
DR EMBL; BC010808; AAH10808.1; -; mRNA.
DR EMBL; BC052652; AAH52652.1; -; mRNA.
DR EMBL; AK008864; BAB25938.1; -; mRNA.
DR CCDS; CCDS37591.1; -.
DR RefSeq; NP_076046.1; NM_023557.3.
DR AlphaFoldDB; Q91VA1; -.
DR STRING; 10090.ENSMUSP00000007249; -.
DR GlyGen; Q91VA1; 8 sites.
DR iPTMnet; Q91VA1; -.
DR PhosphoSitePlus; Q91VA1; -.
DR jPOST; Q91VA1; -.
DR PaxDb; Q91VA1; -.
DR PRIDE; Q91VA1; -.
DR ProteomicsDB; 284055; -.
DR Antibodypedia; 71079; 61 antibodies from 12 providers.
DR DNASU; 70129; -.
DR Ensembl; ENSMUST00000007249; ENSMUSP00000007249; ENSMUSG00000007034.
DR GeneID; 70129; -.
DR KEGG; mmu:70129; -.
DR UCSC; uc008ceh.2; mouse.
DR CTD; 80736; -.
DR MGI; MGI:1917379; Slc44a4.
DR VEuPathDB; HostDB:ENSMUSG00000007034; -.
DR eggNOG; KOG1362; Eukaryota.
DR GeneTree; ENSGT00940000160576; -.
DR HOGENOM; CLU_017181_3_1_1; -.
DR InParanoid; Q91VA1; -.
DR OMA; MNSSCPG; -.
DR OrthoDB; 329225at2759; -.
DR PhylomeDB; Q91VA1; -.
DR TreeFam; TF313325; -.
DR Reactome; R-MMU-1483191; Synthesis of PC.
DR Reactome; R-MMU-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR BioGRID-ORCS; 70129; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Slc44a4; mouse.
DR PRO; PR:Q91VA1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q91VA1; protein.
DR Bgee; ENSMUSG00000007034; Expressed in left colon and 92 other tissues.
DR ExpressionAtlas; Q91VA1; baseline and differential.
DR Genevisible; Q91VA1; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISS: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; ISO:MGI.
DR GO; GO:0015220; F:choline transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0090422; F:thiamine pyrophosphate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008292; P:acetylcholine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0061526; P:acetylcholine secretion; ISS:UniProtKB.
DR GO; GO:0015871; P:choline transport; ISS:UniProtKB.
DR GO; GO:0035675; P:neuromast hair cell development; ISS:UniProtKB.
DR GO; GO:0032475; P:otolith formation; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS: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 Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..707
FT /note="Choline transporter-like protein 4"
FT /id="PRO_0000191724"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..227
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..307
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..452
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 520..557
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 579..594
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 595..615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 616..635
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..707
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q53GD3"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q53GD3"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q53GD3"
FT CONFLICT 461
FT /note="V -> A (in Ref. 2; AAH10808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 78723 MW; 544118B5B030A376 CRC64;
MGRKQNENEA HGNSAKYDPS FRGPIKNRGC TDIICCVLFL IFILGYIIVG LVAWVYGDPR
QVLYPRNSTG AYCGVGDNKD KPYVLYFDIL SCAAAINIIS IAENGLQCPT PQVCVSSCPL
APWAVEVFQF SKTVGEVYGE RRNFCLPAVS PDMIVEESLQ KGLCPRFLLP STPALGRCFP
LPNINFTLPE DLRINNTTVS NGISGLLDSI NARDVSVKIF EDFAQSWYWI LVALGVALAL
SLLFILLLRL VAAPLVLLLI VGVLAVLAYG IYHCWQQYQV FRDKGASITQ LGFTTNFSAY
QSVKETWLAA LIVLAVLEGI LLLMLIFLRQ RIRIAIALLK EASRAVGQMM STMFYPLVTF
VLLVICIGYW AVTALYLATS GQPQYIYWAS NTSTPGCENV PVNMTCDPMA PLNSSCPNLK
CVFKGYSTTG LAQRSLFNLQ IYGVLGLFWT VNWVLALGQC VLAGAFASFY WAFHKPRDIP
TFPLSSAFIR TLRYHTGSLA FGALILSLVQ IARVILEYID HKLRGSQNPV ARCIICCFKC
CLWCLEKFIK FLNRNAYIMI AIYGKNFCVS AKNAFMLLMR NVLRVVVLDK VTDLLLFFGK
LLVVGGVGVL SFFFFSGRIK GLGKDFENPN LNYYWLPIMT SIMGAYVIAS GFFSVFGMCV
DTLFLCFLED LERNDGSQER PYYMPKALLK ILGKKNEAPT GGKTRKK
