SC5A7_MOUSE
ID SC5A7_MOUSE Reviewed; 580 AA.
AC Q8BGY9; Q99PK3; Q9ESW5;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
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 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 [MRNA].
RC TISSUE=Spinal cord;
RX PubMed=11709061; DOI=10.1042/0300-5127:0290711;
RA Apparsundaram S., Ferguson S.M., Blakely R.D.;
RT "Molecular cloning and characterization of a murine hemicholinium-3-
RT sensitive choline transporter.";
RL Biochem. Soc. Trans. 29:711-716(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain stem;
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 (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Embryonic head;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain;
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 [5]
RP PHOSPHORYLATION BY PKC.
RC TISSUE=Corpus striatum, and Hippocampus;
RX PubMed=15064333; DOI=10.1124/jpet.104.066795;
RA Gates J. Jr., Ferguson S.M., Blakely R.D., Apparsundaram S.;
RT "Regulation of choline transporter surface expression and phosphorylation
RT by protein kinase C and protein phosphatase 1/2A.";
RL J. Pharmacol. Exp. Ther. 310:536-545(2004).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15173594; DOI=10.1073/pnas.0401667101;
RA Ferguson S.M., Bazalakova M., Savchenko V., Tapia J.C., Wright J.,
RA Blakely R.D.;
RT "Lethal impairment of cholinergic neurotransmission in hemicholinium-3-
RT sensitive choline transporter knockout mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8762-8767(2004).
CC -!- FUNCTION: Transmembrane transporter that imports choline from the
CC extracellular space to the neuron with high affinity. Choline uptake is
CC the rate-limiting step in acetylcholine synthesis. Sodium ion- and
CC chloride ion-dependent. {ECO:0000269|PubMed:15173594}.
CC -!- SUBUNIT: Homooligomerizes at cell surface. Interacts with SEC14L1; may
CC regulate SLC5A7. {ECO:0000250|UniProtKB:Q9GZV3}.
CC -!- INTERACTION:
CC Q8BGY9; P05067: APP; Xeno; NbExp=2; IntAct=EBI-2010752, EBI-77613;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9GZV3}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q9GZV3}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9GZV3}. Synapse {ECO:0000250|UniProtKB:Q9GZV3}.
CC Note=Localized at the neuromuscular junction.
CC {ECO:0000250|UniProtKB:Q9GZV3}.
CC -!- TISSUE SPECIFICITY: Found in spinal cord, brain-stem, mid-brain and
CC striatum. Specific for cholinergic neurons.
CC -!- PTM: Phosphorylated by PKC and dephosphorylated by PP1/PP2A.
CC {ECO:0000269|PubMed:15064333}.
CC -!- DISRUPTION PHENOTYPE: Although morphologically normal at birth,
CC knockout mice become immobile, breathe irregularly, appear cyanotic,
CC and die within an hour. Mice had developmental changes in neuromuscular
CC junction morphology reminiscent of changes in mutant mice lacking ACh
CC synthesis. {ECO:0000269|PubMed:15173594}.
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; AF276872; AAG36945.2; -; mRNA.
DR EMBL; AJ401467; CAC03719.1; -; mRNA.
DR EMBL; AK034415; BAC28702.1; -; mRNA.
DR EMBL; AK053063; BAC35253.1; -; mRNA.
DR EMBL; BC065089; AAH65089.1; -; mRNA.
DR CCDS; CCDS28885.1; -.
DR RefSeq; NP_071308.2; NM_022025.4.
DR RefSeq; XP_006524837.1; XM_006524774.3.
DR RefSeq; XP_006524838.1; XM_006524775.2.
DR AlphaFoldDB; Q8BGY9; -.
DR SMR; Q8BGY9; -.
DR DIP; DIP-46467N; -.
DR IntAct; Q8BGY9; 3.
DR STRING; 10090.ENSMUSP00000093379; -.
DR BindingDB; Q8BGY9; -.
DR ChEMBL; CHEMBL3013; -.
DR DrugCentral; Q8BGY9; -.
DR GlyGen; Q8BGY9; 1 site.
DR iPTMnet; Q8BGY9; -.
DR PhosphoSitePlus; Q8BGY9; -.
DR PaxDb; Q8BGY9; -.
DR PRIDE; Q8BGY9; -.
DR ProteomicsDB; 255468; -.
DR Antibodypedia; 33052; 85 antibodies from 21 providers.
DR DNASU; 63993; -.
DR Ensembl; ENSMUST00000095712; ENSMUSP00000093379; ENSMUSG00000023945.
DR GeneID; 63993; -.
DR KEGG; mmu:63993; -.
DR UCSC; uc008czy.1; mouse.
DR CTD; 60482; -.
DR MGI; MGI:1927126; Slc5a7.
DR VEuPathDB; HostDB:ENSMUSG00000023945; -.
DR eggNOG; KOG3761; Eukaryota.
DR GeneTree; ENSGT00690000101915; -.
DR HOGENOM; CLU_018808_10_0_1; -.
DR InParanoid; Q8BGY9; -.
DR OMA; AWKTKNT; -.
DR OrthoDB; 799628at2759; -.
DR PhylomeDB; Q8BGY9; -.
DR TreeFam; TF314588; -.
DR Reactome; R-MMU-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR BioGRID-ORCS; 63993; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Slc5a7; mouse.
DR PRO; PR:Q8BGY9; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8BGY9; protein.
DR Bgee; ENSMUSG00000023945; Expressed in lumbar subsegment of spinal cord and 40 other tissues.
DR ExpressionAtlas; Q8BGY9; baseline and differential.
DR Genevisible; Q8BGY9; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0044853; C:plasma membrane raft; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0033265; F:choline binding; IDA:MGI.
DR GO; GO:0015220; F:choline transmembrane transporter activity; IDA:MGI.
DR GO; GO:0005307; F:choline:sodium symporter activity; ISO:MGI.
DR GO; GO:0008292; P:acetylcholine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0015871; P:choline transport; IDA:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:MGI.
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; Glycoprotein; Ion transport; Membrane;
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_0000105392"
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 CONFLICT 2
FT /note="S -> P (in Ref. 1; AAG36945)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="R -> H (in Ref. 2; CAC03719)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="E -> V (in Ref. 2; CAC03719)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="Q -> H (in Ref. 1; AAG36945)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="Q -> K (in Ref. 1; AAG36945)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="F -> Y (in Ref. 2; CAC03719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 580 AA; 63365 MW; 6154CE6622772A41 CRC64;
MSFHVEGLVA IILFYLLIFL VGIWAAWKTK NSGNPEERSE AIIVGGRDIG LLVGGFTMTA
TWVGGGYING TAEAVYGPGC GLAWAQAPIG YSLSLILGGL FFAKPMRSKG YVTMLDPFQQ
IYGKRMGGLL FIPALMGEMF WAAAIFSALG ATISVIIDVD VNISVIVSAL IAILYTLVGG
LYSVAYTDVV QLFCIFIGLW ISVPFALSHP AVTDIGFTAV HAKYQSPWLG TIESVEVYTW
LDNFLLLMLG GIPWQAYFQR VLSSSSATYA QVLSFLAAFG CLVMALPAIC IGAIGASTDW
NQTAYGYPDP KTKEEADMIL PIVLQYLCPV YISFFGLGAV SAAVMSSADS SILSASSMFA
RNIYQLSFRQ NASDKEIVWV MRITVLVFGA SATAMALLTK TVYGLWYLSS DLVYIIIFPQ
LLCVLFIKGT NTYGAVAGYI FGLFLRITGG EPYLYLQPLI FYPGYYSDKN GIYNQRFPFK
TLSMVTSFFT NICVSYLAKY LFESGTLPPK LDVFDAVVAR HSEENMDKTI LVRNENIKLN
ELAPVKPRQS LTLSSTFTNK EALLDVDSSP EGSGTEDNLQ
