CTL4_RAT
ID CTL4_RAT Reviewed; 707 AA.
AC Q6MG71;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Choline transporter-like protein 4;
DE AltName: Full=Solute carrier family 44 member 4;
DE AltName: Full=Thiamine pyrophosphate transporter 1 {ECO:0000250|UniProtKB:Q53GD3};
GN Name=Slc44a4 {ECO:0000312|RGD:1303167};
GN Synonyms=Ctl4, Ng22, TPPT1 {ECO:0000250|UniProtKB:Q53GD3};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=15715662; DOI=10.1111/j.1471-4159.2004.02962.x;
RA Traiffort E., Ruat M., O'Regan S., Meunier F.-M.;
RT "Molecular characterization of the family of choline transporter-like
RT proteins and their splice variants.";
RL J. Neurochem. 92:1116-1125(2005).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q53GD3, ECO:0000250|UniProtKB:Q7T2B0}.
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: Highly expressed in intestine, kidney and stomach.
CC Also expressed in testis and lung. {ECO:0000269|PubMed:15715662}.
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}.
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DR EMBL; BX883045; CAE83975.1; -; Genomic_DNA.
DR EMBL; BC079178; AAH79178.1; -; mRNA.
DR RefSeq; NP_997706.1; NM_212541.1.
DR AlphaFoldDB; Q6MG71; -.
DR STRING; 10116.ENSRNOP00000001174; -.
DR GlyGen; Q6MG71; 8 sites.
DR PaxDb; Q6MG71; -.
DR Ensembl; ENSRNOT00000001174; ENSRNOP00000001174; ENSRNOG00000000878.
DR GeneID; 294255; -.
DR KEGG; rno:294255; -.
DR UCSC; RGD:1303167; rat.
DR CTD; 80736; -.
DR RGD; 1303167; Slc44a4.
DR eggNOG; KOG1362; Eukaryota.
DR GeneTree; ENSGT00940000160576; -.
DR HOGENOM; CLU_017181_3_1_1; -.
DR InParanoid; Q6MG71; -.
DR OMA; MNSSCPG; -.
DR OrthoDB; 329225at2759; -.
DR PhylomeDB; Q6MG71; -.
DR Reactome; R-RNO-1483191; Synthesis of PC.
DR Reactome; R-RNO-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR PRO; PR:Q6MG71; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000878; Expressed in jejunum and 13 other tissues.
DR Genevisible; Q6MG71; RN.
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:RGD.
DR GO; GO:0015220; F:choline transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0090422; F:thiamine pyrophosphate transmembrane transporter activity; ISS: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; ISS: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 2: Evidence at transcript 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_0000191725"
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:0000250|UniProtKB:Q53GD3"
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"
SQ SEQUENCE 707 AA; 78737 MW; B37416E597969501 CRC64;
MGKKQKENEA YGNSAKYDPS FRGPIKNRGC TDIICCVLFL VFILGYIVVG LVAWVYGDPR
QVLYPRNSTG AYCGVGDNKD KPYVLYFNIL SCAAAINVIS IAENGLQCPT PQVCVSSCPQ
TPWVVEGFQL SNTVGDVYKE YRNFCVPAVS PDMVVMDSLQ KGLCPSFLLP STPALGRCFP
LPNINFTLPE QLQINNTTVS KGISGLLDSI NARDVSVKIF EDFAQSWYWI LVALGVALVL
SLLFILLLRL VAAPLVLLLI VGVLAVLAYG IYHCWQQYRE LRDQGVSITQ LGFTANLSAY
QNVKETWLAA LIILAVLEGV LLLMLIFLRQ RIRIAIALLK EASRAVGQMM STMFYPLVTF
VLLVICIGYW AVTALYLATS GQPQYVYWVH NTSTPGCEKV LVNVSCDPMA PLNSSCPELK
CTFTGYSSSG LAQRSLFNLQ IYGILGLFWT VNWVLALGQC VLAGAFASFY WAFHKPRDIP
TFPLSSAFIR TLRYHTGSLA FGALILTLVQ IARVILEYID HKLRGSQNPV ARCIICCFKC
CLWCLEKFIK FLNRNAYIMI AIYGKNFCVS AKNAFMLLMR NVVRVVVLDK VTDLLLFFGK
LLVVGGVGVL SFFFFSGRIK GLGKDFKNPD LNYYWLPIMT SIMGAYVIAS GFFSVFGMCV
DTLFLCFLED LERNDGSQER PYYMPKALLK ILGKKNEVPT GGKNRKK
