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SC5A7_TORMA
ID   SC5A7_TORMA             Reviewed;         584 AA.
AC   Q8UWF0;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=High-affinity choline transporter 1;
GN   Name=CHT1;
OS   Torpedo marmorata (Marbled electric ray).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Torpedo.
OX   NCBI_TaxID=7788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Electric lobe;
RX   PubMed=12358793; DOI=10.1046/j.1471-4159.2002.01044.x;
RA   Lane-Guermonprez L., O'Regan S., Meunier F.-M., Morot-Gaudry-Talarmain Y.;
RT   "The neuronal choline transporter CHT1 is regulated by immunosuppressor-
RT   sensitive pathways.";
RL   J. Neurochem. 82:874-884(2002).
CC   -!- FUNCTION: Imports choline from the extracellular space to the neuron
CC       with high affinity. Rate-limiting step in acetylcholine synthesis.
CC       Sodium ion and chloride ion dependent. {ECO:0000269|PubMed:12358793}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Specific for cholinergic neurons.
CC       {ECO:0000269|PubMed:12358793}.
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}.
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DR   EMBL; AJ420808; CAD12727.1; -; mRNA.
DR   AlphaFoldDB; Q8UWF0; -.
DR   SMR; Q8UWF0; -.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   GO; GO:0015220; F:choline transmembrane transporter activity; IMP:UniProtKB.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0008292; P:acetylcholine biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Glycoprotein; Ion transport; Membrane; Neurotransmitter biosynthesis;
KW   Phosphoprotein; Sodium; Sodium transport; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..584
FT                   /note="High-affinity choline transporter 1"
FT                   /id="PRO_0000105394"
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..50
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..83
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..127
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        149..166
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..193
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        215..239
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..276
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        298..319
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        341..378
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        400..408
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        430..437
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        459..487
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        488..508
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        509..584
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   584 AA;  63660 MW;  995F937B01195A3D CRC64;
     MTVHIDGIVA IVLFYLLILF VGLWAAWKSK NTSMEGAMDR SEAIMIGGRD IGLLVGGFTM
     TATWVGGGYI NGTAEAVYVP GYGLAWAQAP FGYALSLVIG GLFFAKPMRS RGYVTMLDPF
     QQMYGKRMGG LLFIPALLGE IFWSAAILSA LGATLSVIVD ININVSVVVS AVIAVLYTLV
     GGLYSVAYTD VVQLFCIFLG LWISIPFALL NPAVTDIIVT ANQEVYQEPW VGNIQSKDSL
     IWIDNFLLLM LGGIPWQVYF QRVLSASSAT YAQVLSFLAA FGCVLMAIPS VLIGAIGTST
     DWNQTSYGLP GPIGKNETDM ILPIVLQHLC PPYISFFGLG AVSAAVMSSA DSSILSASSM
     FARNIYHLAF RQEASDKEIV WVMRITIFLF GGAATSMALL AQSIYGLWYL SSDLVYVIIF
     PQLISVLFVK GTNTYGSIAG YIIGFLLRIS GGEPYLHMQP FIYYPGCYLD HSFGDDPVYV
     QRFPFKTMAM LFSFLGNTGV SYLVKYLFVS GILPPKLDFL DSVVSKHSKE IMDKTFLMNQ
     DNITLSELVH VNPIHSASVS AALTNKEAFE DIEPNPELSK SGND
 
 
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