CTL4_PIG
ID CTL4_PIG Reviewed; 707 AA.
AC A5PF08;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Choline transporter-like protein 4 {ECO:0000250|UniProtKB:Q53GD3};
DE AltName: Full=Solute carrier family 44 member 4 {ECO:0000250|UniProtKB:Q53GD3};
DE AltName: Full=Thiamine pyrophosphate transporter 1 {ECO:0000250|UniProtKB:Q53GD3};
GN Name=SLC44A4 {ECO:0000250|UniProtKB:Q53GD3};
GN Synonyms=CTL4 {ECO:0000250|UniProtKB:Q53GD3},
GN TPPT1 {ECO:0000250|UniProtKB:Q53GD3};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- PTM: N-glycosylated; N-glycosylation of Asn-677 and Asn-390 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; AL773527; CAN87705.1; -; Genomic_DNA.
DR RefSeq; NP_001095288.1; NM_001101818.1.
DR RefSeq; XP_005665856.1; XM_005665799.2.
DR AlphaFoldDB; A5PF08; -.
DR STRING; 9823.ENSSSCP00000001514; -.
DR PaxDb; A5PF08; -.
DR PeptideAtlas; A5PF08; -.
DR Ensembl; ENSSSCT00000033364; ENSSSCP00000028905; ENSSSCG00000001419.
DR Ensembl; ENSSSCT00025102862; ENSSSCP00025045556; ENSSSCG00025074458.
DR Ensembl; ENSSSCT00030077922; ENSSSCP00030035599; ENSSSCG00030055836.
DR Ensembl; ENSSSCT00040059607; ENSSSCP00040024992; ENSSSCG00040043733.
DR Ensembl; ENSSSCT00045068724; ENSSSCP00045048929; ENSSSCG00045039450.
DR Ensembl; ENSSSCT00060092064; ENSSSCP00060039781; ENSSSCG00060066461.
DR Ensembl; ENSSSCT00065020489; ENSSSCP00065008309; ENSSSCG00065015210.
DR Ensembl; ENSSSCT00070046745; ENSSSCP00070039431; ENSSSCG00070023449.
DR GeneID; 100124377; -.
DR KEGG; ssc:100124377; -.
DR CTD; 80736; -.
DR VGNC; VGNC:93120; SLC44A4.
DR eggNOG; KOG1362; Eukaryota.
DR GeneTree; ENSGT00940000160576; -.
DR HOGENOM; CLU_017181_3_1_1; -.
DR InParanoid; A5PF08; -.
DR OMA; GAYCGFG; -.
DR OrthoDB; 329225at2759; -.
DR TreeFam; TF313325; -.
DR Reactome; R-SSC-1483191; Synthesis of PC.
DR Reactome; R-SSC-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR Proteomes; UP000008227; Chromosome 7.
DR Proteomes; UP000314985; Chromosome 7.
DR Bgee; ENSSSCG00000001419; Expressed in caecum and 25 other tissues.
DR ExpressionAtlas; A5PF08; baseline.
DR Genevisible; A5PF08; SS.
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; IBA:GO_Central.
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 3: Inferred from homology;
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_0000359721"
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..226
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..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 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q53GD3"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q53GD3"
FT CARBOHYD 402
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; 78480 MW; 592738F0031DA64B CRC64;
MGEKQDPDKA YGKPAKYDPS FRGPIRNRSC TDIICCVLFF VFILGYIAVG LVAWVYGDPQ
QVLYPRNSSG AYCGIGENKD KPYLLYFNIF SCVLTTNIIA VAQNGLDCPT PQVCVSSCPA
VSWTVATNQL SQTVGQVFYA ANRSFCLPGV PGDMPVHQSL SQELCPSFLL PSSPALGRCF
PWPNSTVPEV PEISNTSISQ GISGLLDSLN ARDISVKIFE DFAQSWYWIL AALGVALVLS
LLFVLLLRLV AGPLVFVLII GVLGVLAYGI YHCWNEYRLL RDKGASISQL GFTTNLSAYS
SVQETWLAAL ILLAVLEGIL LLMLIFLRQR IRIAIALLEE ASRAVGQMMS TLFYPLVTFV
LLLVCIAYWA MTALYLATSG QPQYVLWAPN VSLAGCEKVM MNTSCDPMNQ PVNSTCPGLM
CVFQGYLSTG LVQRSLFNLQ IYGVLGLFWT INWVLALGQC VLAGAFASFY WAFHKPRDIP
TFPLSSAFIR TLRYHTGSLA FGALILTLVQ IARAILEYID HKLRGAQNPV ARCIMCCFKC
CLWCLEKFIK FLNRNAYIMI AIYGKNFCVS AKNAFMLLMR NIVRVVVLDK VTDLLLFFGK
LLVVGGVGVL SFFFFTGRIQ GLGKDFESPQ LNYYWLPIMT SIMGAYVIAS GFFSVFGMCV
DTLFLCFLED LERNDGSLDR PYYMSKALLK ILGKKNEVPS GDKKRKK
