SC5A7_HUMAN
ID SC5A7_HUMAN Reviewed; 580 AA.
AC Q9GZV3; Q53TF2;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=High affinity choline transporter 1;
DE AltName: Full=Hemicholinium-3-sensitive choline transporter;
DE Short=CHT;
DE AltName: Full=Solute carrier family 5 member 7;
GN Name=SLC5A7; Synonyms=CHT1;
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 [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Spinal cord;
RX PubMed=11027560; DOI=10.1006/bbrc.2000.3561;
RA Apparsundaram S., Ferguson S.M., George A.L. Jr., Blakely R.D.;
RT "Molecular cloning of a human, hemicholinium-3-sensitive choline
RT transporter.";
RL Biochem. Biophys. Res. Commun. 276:862-867(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spinal cord;
RX PubMed=11068039; DOI=10.1016/s0014-5793(00)02134-7;
RA Okuda T., Haga T.;
RT "Functional characterization of the human high-affinity choline
RT transporter.";
RL FEBS Lett. 484:92-97(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Hypothalamus;
RA Wieland A., Bonisch H., Bruess M.;
RT "Molecular cloning of the human and murine high affinity choline
RT transporters and characterization of the human gene structure.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP INTERACTION WITH SEC14L1.
RX PubMed=17092608; DOI=10.1016/j.neuint.2006.09.010;
RA Ribeiro F.M., Ferreira L.T., Marion S., Fontes S., Gomez M., Ferguson S.S.,
RA Prado M.A., Prado V.F.;
RT "SEC14-like protein 1 interacts with cholinergic transporters.";
RL Neurochem. Int. 50:356-364(2007).
RN [7]
RP INVOLVEMENT IN HMN7A.
RX PubMed=23141292; DOI=10.1016/j.ajhg.2012.09.019;
RA Barwick K.E., Wright J., Al-Turki S., McEntagart M.M., Nair A., Chioza B.,
RA Al-Memar A., Modarres H., Reilly M.M., Dick K.J., Ruggiero A.M.,
RA Blakely R.D., Hurles M.E., Crosby A.H.;
RT "Defective presynaptic choline transport underlies hereditary motor
RT neuropathy.";
RL Am. J. Hum. Genet. 91:1103-1107(2012).
RN [8]
RP TOPOLOGY, SUBUNIT, AND MUTAGENESIS OF ILE-89 AND GLU-451.
RX PubMed=23132865; DOI=10.1074/jbc.m112.405027;
RA Okuda T., Osawa C., Yamada H., Hayashi K., Nishikawa S., Ushio T., Kubo Y.,
RA Satou M., Ogawa H., Haga T.;
RT "Transmembrane topology and oligomeric structure of the high-affinity
RT choline transporter.";
RL J. Biol. Chem. 287:42826-42834(2012).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN CMS20, VARIANTS CMS20
RP GLY-48; GLU-65; SER-105; HIS-111; CYS-175; THR-291; LEU-344; GLN-361;
RP VAL-418 AND GLY-446, AND CHARACTERIZATION OF VARIANTS CMS20 GLY-48; GLU-65;
RP SER-105; GLN-361 AND GLY-446.
RX PubMed=27569547; DOI=10.1016/j.ajhg.2016.06.033;
RA Bauche S., O'Regan S., Azuma Y., Laffargue F., McMacken G., Sternberg D.,
RA Brochier G., Buon C., Bouzidi N., Topf A., Lacene E., Remerand G.,
RA Beaufrere A.M., Pebrel-Richard C., Thevenon J., El Chehadeh-Djebbar S.,
RA Faivre L., Duffourd Y., Ricci F., Mongini T., Fiorillo C., Astrea G.,
RA Burloiu C.M., Butoianu N., Sandu C., Servais L., Bonne G., Nelson I.,
RA Desguerre I., Nougues M.C., Boeuf B., Romero N., Laporte J., Boland A.,
RA Lechner D., Deleuze J.F., Fontaine B., Strochlic L., Lochmuller H.,
RA Eymard B., Mayer M., Nicole S.;
RT "Impaired presynaptic high-affinity choline transporter causes a congenital
RT myasthenic syndrome with episodic apnea.";
RL Am. J. Hum. Genet. 99:753-761(2016).
RN [10]
RP VARIANT VAL-89.
RX PubMed=12237312; DOI=10.1074/jbc.m207742200;
RA Okuda T., Okamura M., Kaitsuka C., Haga T., Gurwitz D.;
RT "Single nucleotide polymorphism of the human high affinity choline
RT transporter alters transport rate.";
RL J. Biol. Chem. 277:45315-45322(2002).
CC -!- FUNCTION: Transmembrane transporter that imports choline from the
CC extracellular space into the neuron with high affinity. Choline uptake
CC is the rate-limiting step in acetylcholine synthesis. Sodium ion- and
CC chloride ion-dependent. {ECO:0000269|PubMed:11027560,
CC ECO:0000269|PubMed:27569547}.
CC -!- SUBUNIT: Homooligomerizes at cell surface (PubMed:23132865). Interacts
CC with SEC14L1; may regulate SLC5A7 (PubMed:17092608).
CC {ECO:0000269|PubMed:17092608, ECO:0000269|PubMed:23132865}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11027560}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:11027560}. Cell membrane
CC {ECO:0000269|PubMed:27569547}. Synapse {ECO:0000269|PubMed:27569547}.
CC Note=Localized at the neuromuscular junction.
CC {ECO:0000269|PubMed:27569547}.
CC -!- TISSUE SPECIFICITY: Expressed in putamen, spinal cord and medulla.
CC Specific for cholinergic neurons.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- DISEASE: Neuronopathy, distal hereditary motor, 7A (HMN7A)
CC [MIM:158580]: A neuromuscular disorder. Distal hereditary motor
CC neuronopathies constitute a heterogeneous group of neuromuscular
CC disorders caused by selective degeneration of motor neurons in the
CC anterior horn of the spinal cord, without sensory deficit in the
CC posterior horn. The overall clinical picture consists of a classical
CC distal muscular atrophy syndrome in the legs without clinical sensory
CC loss. The disease starts with weakness and wasting of distal muscles of
CC the anterior tibial and peroneal compartments of the legs. Later on,
CC weakness and atrophy may expand to the proximal muscles of the lower
CC limbs and/or to the distal upper limbs. HMN7A is characterized by onset
CC in the second decade of progressive distal muscle wasting and weakness
CC affecting the upper and lower limbs and resulting in walking
CC difficulties and hand grip. There is significant muscle atrophy of the
CC hands and lower limbs. The disorder is associated with vocal cord
CC paresis due to involvement of the tenth cranial nerve.
CC {ECO:0000269|PubMed:23141292}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Myasthenic syndrome, congenital, 20, presynaptic (CMS20)
CC [MIM:617143]: A form of congenital myasthenic syndrome, a group of
CC disorders characterized by failure of neuromuscular transmission,
CC including pre-synaptic, synaptic, and post-synaptic disorders that are
CC not of autoimmune origin. Clinical features are easy fatigability and
CC muscle weakness. CMS20 is an autosomal recessive, pre-synaptic form
CC characterized by severe hypotonia and episodic apnea soon after birth,
CC generalized limb fatigability and weakness, delayed walking, ptosis,
CC poor sucking and swallowing. {ECO:0000269|PubMed:27569547}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Specifically inhibited by nanomolar concentrations of
CC hemicholinium 3.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000305}.
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DR EMBL; AF276871; AAG25940.1; -; mRNA.
DR EMBL; AB043997; BAB18161.1; -; mRNA.
DR EMBL; AJ401466; CAC03717.1; -; mRNA.
DR EMBL; AJ308378; CAC88115.1; -; Genomic_DNA.
DR EMBL; AJ308379; CAC88115.1; JOINED; Genomic_DNA.
DR EMBL; AJ308380; CAC88115.1; JOINED; Genomic_DNA.
DR EMBL; AJ308381; CAC88115.1; JOINED; Genomic_DNA.
DR EMBL; AJ308382; CAC88115.1; JOINED; Genomic_DNA.
DR EMBL; AJ308383; CAC88115.1; JOINED; Genomic_DNA.
DR EMBL; AJ308384; CAC88115.1; JOINED; Genomic_DNA.
DR EMBL; AC009963; AAY14927.1; -; Genomic_DNA.
DR EMBL; BC111525; AAI11526.1; -; mRNA.
DR CCDS; CCDS2074.1; -.
DR PIR; JC7502; JC7502.
DR RefSeq; NP_001291934.1; NM_001305005.2.
DR RefSeq; NP_068587.1; NM_021815.4.
DR AlphaFoldDB; Q9GZV3; -.
DR SMR; Q9GZV3; -.
DR BioGRID; 121915; 7.
DR IntAct; Q9GZV3; 1.
DR STRING; 9606.ENSP00000264047; -.
DR BindingDB; Q9GZV3; -.
DR ChEMBL; CHEMBL4507; -.
DR DrugBank; DB00122; Choline.
DR DrugBank; DB14006; Choline salicylate.
DR DrugCentral; Q9GZV3; -.
DR GuidetoPHARMACOLOGY; 914; -.
DR TCDB; 2.A.21.8.2; the solute:sodium symporter (sss) family.
DR GlyGen; Q9GZV3; 1 site.
DR iPTMnet; Q9GZV3; -.
DR PhosphoSitePlus; Q9GZV3; -.
DR BioMuta; SLC5A7; -.
DR DMDM; 56404957; -.
DR PaxDb; Q9GZV3; -.
DR PeptideAtlas; Q9GZV3; -.
DR PRIDE; Q9GZV3; -.
DR Antibodypedia; 33052; 85 antibodies from 21 providers.
DR DNASU; 60482; -.
DR Ensembl; ENST00000264047.3; ENSP00000264047.2; ENSG00000115665.9.
DR Ensembl; ENST00000409059.5; ENSP00000387346.1; ENSG00000115665.9.
DR GeneID; 60482; -.
DR KEGG; hsa:60482; -.
DR MANE-Select; ENST00000264047.3; ENSP00000264047.2; NM_021815.5; NP_068587.1.
DR UCSC; uc002tdv.4; human.
DR CTD; 60482; -.
DR DisGeNET; 60482; -.
DR GeneCards; SLC5A7; -.
DR GeneReviews; SLC5A7; -.
DR HGNC; HGNC:14025; SLC5A7.
DR HPA; ENSG00000115665; Tissue enriched (brain).
DR MalaCards; SLC5A7; -.
DR MIM; 158580; phenotype.
DR MIM; 608761; gene.
DR MIM; 617143; phenotype.
DR neXtProt; NX_Q9GZV3; -.
DR OpenTargets; ENSG00000115665; -.
DR Orphanet; 139589; Distal hereditary motor neuropathy type 7.
DR Orphanet; 98914; Presynaptic congenital myasthenic syndromes.
DR PharmGKB; PA37838; -.
DR VEuPathDB; HostDB:ENSG00000115665; -.
DR eggNOG; KOG3761; Eukaryota.
DR GeneTree; ENSGT00690000101915; -.
DR HOGENOM; CLU_018808_10_0_1; -.
DR InParanoid; Q9GZV3; -.
DR OMA; AWKTKNT; -.
DR OrthoDB; 799628at2759; -.
DR PhylomeDB; Q9GZV3; -.
DR TreeFam; TF314588; -.
DR PathwayCommons; Q9GZV3; -.
DR Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR Reactome; R-HSA-5619114; Defective SLC5A7 causes distal hereditary motor neuronopathy 7A (HMN7A).
DR Reactome; R-HSA-5658471; Defective SLC5A7 causes distal hereditary motor neuronopathy 7A (HMN7A).
DR SignaLink; Q9GZV3; -.
DR BioGRID-ORCS; 60482; 13 hits in 1063 CRISPR screens.
DR GeneWiki; Choline_transporter; -.
DR GenomeRNAi; 60482; -.
DR Pharos; Q9GZV3; Tchem.
DR PRO; PR:Q9GZV3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9GZV3; protein.
DR Bgee; ENSG00000115665; Expressed in muscle layer of sigmoid colon and 76 other tissues.
DR Genevisible; Q9GZV3; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0033265; F:choline binding; IEA:Ensembl.
DR GO; GO:0015220; F:choline transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0005307; F:choline:sodium symporter activity; IMP:MGI.
DR GO; GO:0008292; P:acetylcholine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0015871; P:choline transport; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IBA:GO_Central.
DR GO; GO:0006836; P:neurotransmitter transport; TAS:Reactome.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
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 1: Evidence at protein level;
KW Cell membrane; Congenital myasthenic syndrome; Disease variant;
KW Glycoprotein; Ion transport; Membrane; Neurodegeneration; Neuropathy;
KW Neurotransmitter biosynthesis; Phosphoprotein; Reference proteome; Sodium;
KW Sodium transport; Symport; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..580
FT /note="High affinity choline transporter 1"
FT /id="PRO_0000105391"
FT TOPO_DOM 1..6
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..164
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..317
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..481
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..580
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 502..580
FT /note="Mediates interaction with SEC14L1"
FT /evidence="ECO:0000250|UniProtKB:Q9JMD7"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 48
FT /note="D -> G (in CMS20; decreased choline transmembrane
FT transporter activity; no effect on localization at plasma
FT membrane; dbSNP:rs886039768)"
FT /evidence="ECO:0000269|PubMed:27569547"
FT /id="VAR_077854"
FT VARIANT 65
FT /note="G -> E (in CMS20; loss of choline transmembrane
FT transporter activity; no effect on localization at plasma
FT membrane; dbSNP:rs886039765)"
FT /evidence="ECO:0000269|PubMed:27569547"
FT /id="VAR_077855"
FT VARIANT 89
FT /note="I -> V (40% reduction in choline uptake rate; found
FT in 0.06 of Ashkenazi Jews; dbSNP:rs1013940)"
FT /evidence="ECO:0000269|PubMed:12237312"
FT /id="VAR_020524"
FT VARIANT 105
FT /note="P -> S (in CMS20; decreased choline transmembrane
FT transporter activity; no effect on localization at plasma
FT membrane; dbSNP:rs886039766)"
FT /evidence="ECO:0000269|PubMed:27569547"
FT /id="VAR_077856"
FT VARIANT 111
FT /note="Y -> H (in CMS20; no effect on localization at
FT plasma membrane)"
FT /evidence="ECO:0000269|PubMed:27569547"
FT /id="VAR_077857"
FT VARIANT 175
FT /note="Y -> C (in CMS20; unknown pathological significance;
FT dbSNP:rs1331713195)"
FT /evidence="ECO:0000269|PubMed:27569547"
FT /id="VAR_077858"
FT VARIANT 291
FT /note="I -> T (in CMS20; unknown pathological significance;
FT dbSNP:rs375397889)"
FT /evidence="ECO:0000269|PubMed:27569547"
FT /id="VAR_077859"
FT VARIANT 344
FT /note="V -> L (in CMS20; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27569547"
FT /id="VAR_077860"
FT VARIANT 361
FT /note="R -> Q (in CMS20; decreased choline transmembrane
FT transporter activity; no effect on localization at plasma
FT membrane; dbSNP:rs147656110)"
FT /evidence="ECO:0000269|PubMed:27569547"
FT /id="VAR_077861"
FT VARIANT 418
FT /note="F -> V (in CMS20; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27569547"
FT /id="VAR_077862"
FT VARIANT 446
FT /note="R -> G (in CMS20; decreased choline transmembrane
FT transporter activity; no effect on localization at plasma
FT membrane)"
FT /evidence="ECO:0000269|PubMed:27569547"
FT /id="VAR_077863"
FT MUTAGEN 89
FT /note="I->A: Only 20% of wild-type choline uptake
FT activity."
FT /evidence="ECO:0000269|PubMed:23132865"
FT MUTAGEN 451
FT /note="E->Q: Only 5% of wild-type choline uptake activity."
FT /evidence="ECO:0000269|PubMed:23132865"
SQ SEQUENCE 580 AA; 63204 MW; 66CB35496CB6E2D6 CRC64;
MAFHVEGLIA IIVFYLLILL VGIWAAWRTK NSGSAEERSE AIIVGGRDIG LLVGGFTMTA
TWVGGGYING TAEAVYVPGY GLAWAQAPIG YSLSLILGGL FFAKPMRSKG YVTMLDPFQQ
IYGKRMGGLL FIPALMGEMF WAAAIFSALG ATISVIIDVD MHISVIISAL IATLYTLVGG
LYSVAYTDVV QLFCIFVGLW ISVPFALSHP AVADIGFTAV HAKYQKPWLG TVDSSEVYSW
LDSFLLLMLG GIPWQAYFQR VLSSSSATYA QVLSFLAAFG CLVMAIPAIL IGAIGASTDW
NQTAYGLPDP KTTEEADMIL PIVLQYLCPV YISFFGLGAV SAAVMSSADS SILSASSMFA
RNIYQLSFRQ NASDKEIVWV MRITVFVFGA SATAMALLTK TVYGLWYLSS DLVYIVIFPQ
LLCVLFVKGT NTYGAVAGYV SGLFLRITGG EPYLYLQPLI FYPGYYPDDN GIYNQKFPFK
TLAMVTSFLT NICISYLAKY LFESGTLPPK LDVFDAVVAR HSEENMDKTI LVKNENIKLD
ELALVKPRQS MTLSSTFTNK EAFLDVDSSP EGSGTEDNLQ
