SC5A7_RAT
ID SC5A7_RAT Reviewed; 580 AA.
AC Q9JMD7;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Spinal cord;
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 INTERACTION WITH SEC14L1, AND REGION.
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).
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:10649566}.
CC -!- SUBUNIT: Homooligomerizes at cell surface (By similarity). Interacts
CC with SEC14L1; may regulate SLC5A7 (PubMed:17092608).
CC {ECO:0000250|UniProtKB:Q9GZV3, ECO:0000269|PubMed:17092608}.
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: Expressed in basal forebrain, brain stem, spinal
CC chord, and striatum. Specific for cholinergic neurons.
CC {ECO:0000269|PubMed:10649566}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB030947; BAA90484.1; -; mRNA.
DR RefSeq; NP_445973.1; NM_053521.1.
DR AlphaFoldDB; Q9JMD7; -.
DR SMR; Q9JMD7; -.
DR STRING; 10116.ENSRNOP00000014548; -.
DR BindingDB; Q9JMD7; -.
DR ChEMBL; CHEMBL5797; -.
DR TCDB; 2.A.21.8.1; the solute:sodium symporter (sss) family.
DR GlyGen; Q9JMD7; 1 site.
DR iPTMnet; Q9JMD7; -.
DR PhosphoSitePlus; Q9JMD7; -.
DR PaxDb; Q9JMD7; -.
DR GeneID; 85426; -.
DR KEGG; rno:85426; -.
DR UCSC; RGD:69270; rat.
DR CTD; 60482; -.
DR RGD; 69270; Slc5a7.
DR eggNOG; KOG3761; Eukaryota.
DR InParanoid; Q9JMD7; -.
DR PhylomeDB; Q9JMD7; -.
DR Reactome; R-RNO-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR PRO; PR:Q9JMD7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005769; C:early endosome; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0044853; C:plasma membrane raft; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0033265; F:choline binding; ISO:RGD.
DR GO; GO:0015220; F:choline transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0005307; F:choline:sodium symporter activity; ISO:RGD.
DR GO; GO:0008292; P:acetylcholine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0015871; P:choline transport; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; ISO:RGD.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; ISO:RGD.
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_0000105393"
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:0000269|PubMed:17092608"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 580 AA; 63407 MW; B7CB73323DAD17A7 CRC64;
MPFHVEGLVA IILFYLLIFL VGIWAAWKTK NSGNAEERSE 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
NQTAYGFPDP KTKEEADMIL PIVLQYLCPV YISFFGLGAV SAAVMSSADS SILSASSMFA
RNIYQLSFRQ NASDKEIVWV MRITVFVFGA SATAMALLTK TVYGLWYLSS DLVYIIIFPQ
LLCVLFIKGT NTYGAVAGYI FGLFLRITGG EPYLYLQPLI FYPGYYPDKN GIYNQRFPFK
TLSMVTSFFT NICVSYLAKY LFESGTLPPK LDIFDAVVSR HSEENMDKTI LVRNENIKLN
ELAPVKPRQS LTLSSTFTNK EALLDVDSSP EGSGTEDNLQ
