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Q8BGY9 (SC5A7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
High affinity choline transporter 1
Alternative name(s):
Hemicholinium-3-sensitive choline transporter
Short name=CHT
Solute carrier family 5 member 7
Gene names
Name:Slc5a7
Synonyms:Cht1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length580 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Imports choline from the extracellular space to the neuron with high affinity. Rate-limiting step in acetylcholine synthesis. Sodium ion and chloride ion dependent. Ref.6

Subcellular location

Membrane; Multi-pass membrane protein By similarity.

Tissue specificity

Found in spinal cord, brain-stem, mid-brain and striatum. Specific for cholinergic neurons.

Post-translational modification

Phosphorylated by PKC and dephosphorylated by PP1/PP2A. Ref.5

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. Ref.6

Miscellaneous

Specifically inhibited by nanomolar concentrations of hemicholinium 3.

Sequence similarities

Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family. [View classification]

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APPP050672EBI-2010752,EBI-77613From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 580580High affinity choline transporter 1
PRO_0000105392

Regions

Topological domain1 – 66Extracellular Potential
Transmembrane7 – 2721Helical; Potential
Topological domain28 – 4821Cytoplasmic Potential
Transmembrane49 – 6921Helical; Potential
Topological domain70 – 8112Extracellular Potential
Transmembrane82 – 10221Helical; Potential
Topological domain103 – 12523Cytoplasmic Potential
Transmembrane126 – 14621Helical; Potential
Topological domain147 – 16418Extracellular Potential
Transmembrane165 – 18521Helical; Potential
Topological domain186 – 1916Cytoplasmic Potential
Transmembrane192 – 21221Helical; Potential
Topological domain213 – 23725Extracellular Potential
Transmembrane238 – 25821Helical; Potential
Topological domain259 – 27416Cytoplasmic Potential
Transmembrane275 – 29521Helical; Potential
Topological domain296 – 31722Extracellular Potential
Transmembrane318 – 33821Helical; Potential
Topological domain339 – 37638Cytoplasmic Potential
Transmembrane377 – 39721Helical; Potential
Topological domain398 – 4069Extracellular Potential
Transmembrane407 – 42721Helical; Potential
Topological domain428 – 4358Cytoplasmic Potential
Transmembrane436 – 45621Helical; Potential
Topological domain457 – 48125Extracellular Potential
Transmembrane482 – 50221Helical; Potential
Topological domain503 – 58078Cytoplasmic Potential

Amino acid modifications

Glycosylation3011N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict21S → P in AAG36945. Ref.1
Sequence conflict381R → H in CAC03719. Ref.2
Sequence conflict731E → V in CAC03719. Ref.2
Sequence conflict861Q → H in AAG36945. Ref.1
Sequence conflict1191Q → K in AAG36945. Ref.1
Sequence conflict2751F → Y in CAC03719. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8BGY9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 6154CE6622772A41

FASTA58063,365
        10         20         30         40         50         60 
MSFHVEGLVA IILFYLLIFL VGIWAAWKTK NSGNPEERSE AIIVGGRDIG LLVGGFTMTA 

        70         80         90        100        110        120 
TWVGGGYING TAEAVYGPGC GLAWAQAPIG YSLSLILGGL FFAKPMRSKG YVTMLDPFQQ 

       130        140        150        160        170        180 
IYGKRMGGLL FIPALMGEMF WAAAIFSALG ATISVIIDVD VNISVIVSAL IAILYTLVGG 

       190        200        210        220        230        240 
LYSVAYTDVV QLFCIFIGLW ISVPFALSHP AVTDIGFTAV HAKYQSPWLG TIESVEVYTW 

       250        260        270        280        290        300 
LDNFLLLMLG GIPWQAYFQR VLSSSSATYA QVLSFLAAFG CLVMALPAIC IGAIGASTDW 

       310        320        330        340        350        360 
NQTAYGYPDP KTKEEADMIL PIVLQYLCPV YISFFGLGAV SAAVMSSADS SILSASSMFA 

       370        380        390        400        410        420 
RNIYQLSFRQ NASDKEIVWV MRITVLVFGA SATAMALLTK TVYGLWYLSS DLVYIIIFPQ 

       430        440        450        460        470        480 
LLCVLFIKGT NTYGAVAGYI FGLFLRITGG EPYLYLQPLI FYPGYYSDKN GIYNQRFPFK 

       490        500        510        520        530        540 
TLSMVTSFFT NICVSYLAKY LFESGTLPPK LDVFDAVVAR HSEENMDKTI LVRNENIKLN 

       550        560        570        580 
ELAPVKPRQS LTLSSTFTNK EALLDVDSSP EGSGTEDNLQ 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a murine hemicholinium-3-sensitive choline transporter."
Apparsundaram S., Ferguson S.M., Blakely R.D.
Biochem. Soc. Trans. 29:711-716(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Spinal cord.
[2]"Molecular cloning of the human and murine high affinity choline transporters and characterization of the human gene structure."
Wieland A., Bonisch H., Bruess M.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/cJ.
Tissue: Brain stem.
[3]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Diencephalon and Embryonic head.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Embryonic brain.
[5]"Regulation of choline transporter surface expression and phosphorylation by protein kinase C and protein phosphatase 1/2A."
Gates J. Jr., Ferguson S.M., Blakely R.D., Apparsundaram S.
J. Pharmacol. Exp. Ther. 310:536-545(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY PKC.
Tissue: Corpus striatum and Hippocampus.
[6]"Lethal impairment of cholinergic neurotransmission in hemicholinium-3-sensitive choline transporter knockout mice."
Ferguson S.M., Bazalakova M., Savchenko V., Tapia J.C., Wright J., Blakely R.D.
Proc. Natl. Acad. Sci. U.S.A. 101:8762-8767(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF276872 mRNA. Translation: AAG36945.2.
AJ401467 mRNA. Translation: CAC03719.1.
AK034415 mRNA. Translation: BAC28702.1.
AK053063 mRNA. Translation: BAC35253.1.
BC065089 mRNA. Translation: AAH65089.1.
CCDSCCDS28885.1.
RefSeqNP_071308.2. NM_022025.4.
XP_006524837.1. XM_006524774.1.
XP_006524838.1. XM_006524775.1.
UniGeneMm.155241.

3D structure databases

ProteinModelPortalQ8BGY9.
SMRQ8BGY9. Positions 77-446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-46467N.
IntActQ8BGY9. 3 interactions.

Chemistry

BindingDBQ8BGY9.
ChEMBLCHEMBL3013.

PTM databases

PhosphoSiteQ8BGY9.

Proteomic databases

PaxDbQ8BGY9.
PRIDEQ8BGY9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000095712; ENSMUSP00000093379; ENSMUSG00000023945.
GeneID63993.
KEGGmmu:63993.
UCSCuc008czy.1. mouse.

Organism-specific databases

CTD60482.
MGIMGI:1927126. Slc5a7.

Phylogenomic databases

eggNOGCOG0591.
GeneTreeENSGT00690000101915.
HOGENOMHOG000016386.
HOVERGENHBG054160.
InParanoidQ8BGY9.
KOK14387.
OMAHAKYQKP.
OrthoDBEOG7P8P7C.
PhylomeDBQ8BGY9.
TreeFamTF314588.

Gene expression databases

BgeeQ8BGY9.
GenevestigatorQ8BGY9.

Family and domain databases

InterProIPR001734. Na/solute_symporter.
[Graphical view]
PANTHERPTHR11819. PTHR11819. 1 hit.
PfamPF00474. SSF. 1 hit.
[Graphical view]
PROSITEPS50283. NA_SOLUT_SYMP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio319843.
PROQ8BGY9.
SOURCESearch...

Entry information

Entry nameSC5A7_MOUSE
AccessionPrimary (citable) accession number: Q8BGY9
Secondary accession number(s): Q99PK3, Q9ESW5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot