SC5A7_CAEEL
ID SC5A7_CAEEL Reviewed; 576 AA.
AC O02228; Q9NL58;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=High-affinity choline transporter 1;
GN Name=cho-1; ORFNames=C48D1.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Bristol N2;
RX PubMed=10649566; DOI=10.1038/72059;
RA Okuda T., Haga T., Kanai Y., Endou H., Ishihara T., Katsura I.;
RT "Identification and characterization of the high-affinity choline
RT transporter.";
RL Nat. Neurosci. 3:120-125(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Imports choline from the extracellular space to the neuron
CC with high affinity. Choline uptake is the rate-limiting step in
CC acetylcholine synthesis. Sodium ion and chloride ion dependent.
CC {ECO:0000269|PubMed:10649566}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in the nervous system, including the nerve
CC ring and cholinergic motor neurons of the ventral nerve cord.
CC {ECO:0000269|PubMed:10649566}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000305}.
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DR EMBL; AB030946; BAA90483.1; -; mRNA.
DR EMBL; Z81049; CAB02847.2; -; Genomic_DNA.
DR PIR; T20037; T20037.
DR RefSeq; NP_502539.1; NM_070138.7.
DR AlphaFoldDB; O02228; -.
DR SMR; O02228; -.
DR STRING; 6239.C48D1.3; -.
DR PaxDb; O02228; -.
DR PeptideAtlas; O02228; -.
DR EnsemblMetazoa; C48D1.3.1; C48D1.3.1; WBGene00000501.
DR GeneID; 178274; -.
DR KEGG; cel:CELE_C48D1.3; -.
DR UCSC; C48D1.3; c. elegans.
DR CTD; 178274; -.
DR WormBase; C48D1.3; CE27109; WBGene00000501; cho-1.
DR eggNOG; KOG3761; Eukaryota.
DR GeneTree; ENSGT00940000168351; -.
DR HOGENOM; CLU_018808_10_0_1; -.
DR InParanoid; O02228; -.
DR OMA; AWKTKNT; -.
DR OrthoDB; 799628at2759; -.
DR PhylomeDB; O02228; -.
DR Reactome; R-CEL-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR PRO; PR:O02228; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000501; Expressed in larva and 3 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0008021; C:synaptic vesicle; IDA:WormBase.
DR GO; GO:0015220; F:choline transmembrane transporter activity; IDA:WormBase.
DR GO; GO:0005307; F:choline:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0008292; P:acetylcholine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0015871; P:choline transport; IDA:WormBase.
DR Gene3D; 1.20.1730.10; -; 1.
DR InterPro; IPR038377; Na/Glc_symporter_sf.
DR InterPro; IPR001734; Na/solute_symporter.
DR Pfam; PF00474; SSF; 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Ion transport; Membrane; Neurotransmitter biosynthesis;
KW Reference proteome; Sodium; Sodium transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..576
FT /note="High-affinity choline transporter 1"
FT /id="PRO_0000105395"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..82
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..165
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..233
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..319
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..408
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..478
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 500..576
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 541..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 576 AA; 62427 MW; FAB09778358288D9 CRC64;
MADLLGIVAI VFFYVLILVV GIWAGRKSKS SKELESEAGA ATEEVMLAGR NIGTLVGIFT
MTATWVGGAY INGTAEALYN GGLLGCQAPV GYAISLVMGG LLFAKKMREE GYITMLDPFQ
HKYGQRIGGL MYVPALLGET FWTAAILSAL GATLSVILGI DMNASVTLSA CIAVFYTFTG
GYYAVAYTDV VQLFCIFVGL WVCVPAAMVH DGAKDISRNA GDWIGEIGGF KETSLWIDCM
LLLVFGGIPW QVYFQRVLSS KTAHGAQTLS FVAGVGCILM AIPPALIGAI ARNTDWRMTD
YSPWNNGTKV ESIPPDKRNM VVPLVFQYLT PRWVAFIGLG AVSAAVMSSA DSSVLSAASM
FAHNIWKLTI RPHASEKEVI IVMRIAIICV GIMATIMALT IQSIYGLWYL CADLVYVILF
PQLLCVVYMP RSNTYGSLAG YAVGLVLRLI GGEPLVSLPA FFHYPMYTDG VQYFPFRTTA
MLSSMATIYI VSIQSEKLFK SGRLSPEWDV MGCVVNIPID HVPLPSDVSF AVSSETLNMK
APNGTPAPVH PNQQPSDENT LLHPYSDQSY YSTNSN
