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High affinity choline transporter 1 (Hemicholinium-3-sensitive choline transporter) (CHT) (Solute carrier family 5 member 7)

 SC5A7_MOUSE             Reviewed;         580 AA.
Q8BGY9; Q99PK3; Q9ESW5;
07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
27-SEP-2017, entry version 113.
RecName: Full=High affinity choline transporter 1;
AltName: Full=Hemicholinium-3-sensitive choline transporter;
Short=CHT;
AltName: Full=Solute carrier family 5 member 7;
Name=Slc5a7; Synonyms=Cht1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spinal cord;
PubMed=11709061; DOI=10.1042/0300-5127:0290711;
Apparsundaram S., Ferguson S.M., Blakely R.D.;
"Molecular cloning and characterization of a murine hemicholinium-3-
sensitive choline transporter.";
Biochem. Soc. Trans. 29:711-716(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Brain stem;
Wieland A., Bonisch H., Bruess M.;
"Molecular cloning of the human and murine high affinity choline
transporters and characterization of the human gene structure.";
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Diencephalon, and Embryonic head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryonic brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION BY PKC.
TISSUE=Corpus striatum, and Hippocampus;
PubMed=15064333; DOI=10.1124/jpet.104.066795;
Gates J. Jr., Ferguson S.M., Blakely R.D., Apparsundaram S.;
"Regulation of choline transporter surface expression and
phosphorylation by protein kinase C and protein phosphatase 1/2A.";
J. Pharmacol. Exp. Ther. 310:536-545(2004).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15173594; DOI=10.1073/pnas.0401667101;
Ferguson S.M., Bazalakova M., Savchenko V., Tapia J.C., Wright J.,
Blakely R.D.;
"Lethal impairment of cholinergic neurotransmission in hemicholinium-
3-sensitive choline transporter knockout mice.";
Proc. Natl. Acad. Sci. U.S.A. 101:8762-8767(2004).
-!- FUNCTION: Transmembrane transporter that imports choline from the
extracellular space to the neuron with high affinity. Choline
uptake is the rate-limiting step in acetylcholine synthesis.
Sodium ion- and chloride ion-dependent.
{ECO:0000269|PubMed:15173594}.
-!- SUBUNIT: Homooligomerizes at cell surface. Interacts with SEC14L1;
may regulate SLC5A7. {ECO:0000250|UniProtKB:Q9GZV3}.
-!- INTERACTION:
P05067:APP (xeno); NbExp=2; IntAct=EBI-2010752, EBI-77613;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9GZV3};
Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9GZV3}. Cell
membrane {ECO:0000250|UniProtKB:Q9GZV3}. Cell junction, synapse
{ECO:0000250|UniProtKB:Q9GZV3}. Note=Localized at the
neuromuscular junction. {ECO:0000250|UniProtKB:Q9GZV3}.
-!- TISSUE SPECIFICITY: Found in spinal cord, brain-stem, mid-brain
and striatum. Specific for cholinergic neurons.
-!- PTM: Phosphorylated by PKC and dephosphorylated by PP1/PP2A.
{ECO:0000269|PubMed:15064333}.
-!- DISRUPTION PHENOTYPE: Although morphologically normal at birth,
knockout mice become immobile, breathe irregularly, appear
cyanotic, and die within a hour. Mice had developmental changes in
neuromuscular junction morphology reminiscent of changes in mutant
mice lacking ACh synthesis. {ECO:0000269|PubMed:15173594}.
-!- MISCELLANEOUS: Specifically inhibited by nanomolar concentrations
of hemicholinium 3.
-!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC
2.A.21) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF276872; AAG36945.2; -; mRNA.
EMBL; AJ401467; CAC03719.1; -; mRNA.
EMBL; AK034415; BAC28702.1; -; mRNA.
EMBL; AK053063; BAC35253.1; -; mRNA.
EMBL; BC065089; AAH65089.1; -; mRNA.
CCDS; CCDS28885.1; -.
RefSeq; NP_071308.2; NM_022025.4.
RefSeq; XP_006524837.1; XM_006524774.3.
RefSeq; XP_006524838.1; XM_006524775.2.
UniGene; Mm.155241; -.
ProteinModelPortal; Q8BGY9; -.
DIP; DIP-46467N; -.
IntAct; Q8BGY9; 3.
STRING; 10090.ENSMUSP00000093379; -.
BindingDB; Q8BGY9; -.
ChEMBL; CHEMBL3013; -.
iPTMnet; Q8BGY9; -.
PhosphoSitePlus; Q8BGY9; -.
PaxDb; Q8BGY9; -.
PRIDE; Q8BGY9; -.
Ensembl; ENSMUST00000095712; ENSMUSP00000093379; ENSMUSG00000023945.
GeneID; 63993; -.
KEGG; mmu:63993; -.
UCSC; uc008czy.1; mouse.
CTD; 60482; -.
MGI; MGI:1927126; Slc5a7.
eggNOG; KOG3761; Eukaryota.
eggNOG; COG0591; LUCA.
GeneTree; ENSGT00690000101915; -.
HOGENOM; HOG000016386; -.
HOVERGEN; HBG054160; -.
InParanoid; Q8BGY9; -.
KO; K14387; -.
OMA; YTWLDSF; -.
OrthoDB; EOG091G050W; -.
PhylomeDB; Q8BGY9; -.
TreeFam; TF314588; -.
Reactome; R-MMU-264642; Acetylcholine Neurotransmitter Release Cycle.
Reactome; R-MMU-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
PRO; PR:Q8BGY9; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000023945; -.
Genevisible; Q8BGY9; MM.
GO; GO:0030424; C:axon; IBA:GO_Central.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0043204; C:perikaryon; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0045202; C:synapse; IBA:GO_Central.
GO; GO:0033265; F:choline binding; IDA:MGI.
GO; GO:0015220; F:choline transmembrane transporter activity; IDA:MGI.
GO; GO:0005307; F:choline:sodium symporter activity; ISO:MGI.
GO; GO:0008292; P:acetylcholine biosynthetic process; IMP:UniProtKB.
GO; GO:0015871; P:choline transport; IDA:MGI.
GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:MGI.
InterPro; IPR001734; Na/solute_symporter.
Pfam; PF00474; SSF; 1.
PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
1: Evidence at protein level;
Cell junction; Cell membrane; Complete proteome; Glycoprotein;
Ion transport; Membrane; Neurotransmitter biosynthesis;
Phosphoprotein; Reference proteome; Sodium; Sodium transport; Symport;
Synapse; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 580 High affinity choline transporter 1.
/FTId=PRO_0000105392.
TOPO_DOM 1 6 Extracellular. {ECO:0000255}.
TRANSMEM 7 27 Helical. {ECO:0000255}.
TOPO_DOM 28 48 Cytoplasmic. {ECO:0000255}.
TRANSMEM 49 69 Helical. {ECO:0000255}.
TOPO_DOM 70 81 Extracellular. {ECO:0000255}.
TRANSMEM 82 102 Helical. {ECO:0000255}.
TOPO_DOM 103 125 Cytoplasmic. {ECO:0000255}.
TRANSMEM 126 146 Helical. {ECO:0000255}.
TOPO_DOM 147 164 Extracellular. {ECO:0000255}.
TRANSMEM 165 185 Helical. {ECO:0000255}.
TOPO_DOM 186 191 Cytoplasmic. {ECO:0000255}.
TRANSMEM 192 212 Helical. {ECO:0000255}.
TOPO_DOM 213 237 Extracellular. {ECO:0000255}.
TRANSMEM 238 258 Helical. {ECO:0000255}.
TOPO_DOM 259 274 Cytoplasmic. {ECO:0000255}.
TRANSMEM 275 295 Helical. {ECO:0000255}.
TOPO_DOM 296 317 Extracellular. {ECO:0000255}.
TRANSMEM 318 338 Helical. {ECO:0000255}.
TOPO_DOM 339 376 Cytoplasmic. {ECO:0000255}.
TRANSMEM 377 397 Helical. {ECO:0000255}.
TOPO_DOM 398 406 Extracellular. {ECO:0000255}.
TRANSMEM 407 427 Helical. {ECO:0000255}.
TOPO_DOM 428 435 Cytoplasmic. {ECO:0000255}.
TRANSMEM 436 456 Helical. {ECO:0000255}.
TOPO_DOM 457 481 Extracellular. {ECO:0000255}.
TRANSMEM 482 502 Helical. {ECO:0000255}.
TOPO_DOM 503 580 Cytoplasmic. {ECO:0000255}.
REGION 502 580 Mediates interaction with SEC14L1.
{ECO:0000250|UniProtKB:Q9JMD7}.
CARBOHYD 301 301 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 2 2 S -> P (in Ref. 1; AAG36945).
{ECO:0000305}.
CONFLICT 38 38 R -> H (in Ref. 2; CAC03719).
{ECO:0000305}.
CONFLICT 73 73 E -> V (in Ref. 2; CAC03719).
{ECO:0000305}.
CONFLICT 86 86 Q -> H (in Ref. 1; AAG36945).
{ECO:0000305}.
CONFLICT 119 119 Q -> K (in Ref. 1; AAG36945).
{ECO:0000305}.
CONFLICT 275 275 F -> Y (in Ref. 2; CAC03719).
{ECO:0000305}.
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


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