CTL1_TORMA
ID CTL1_TORMA Reviewed; 646 AA.
AC Q9I9B9;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Choline transporter-like protein 1;
DE AltName: Full=Solute carrier family 44 member 1;
GN Name=slc44a1; Synonyms=ctl1;
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], AND FUNCTION.
RX PubMed=10677542; DOI=10.1073/pnas.030339697;
RA O'Regan S., Traiffort E., Ruat M., Cha N., Compaore D., Meunier F.-M.;
RT "An electric lobe suppressor for a yeast choline transport mutation belongs
RT to a new family of transporter-like proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:1835-1840(2000).
RN [2]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12352613; DOI=10.1097/00001756-200209160-00009;
RA Meunier F.-M., O'Regan S.;
RT "Expression of CTL1 in myelinating structures of Torpedo marmorata.";
RL NeuroReport 13:1617-1620(2002).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12675144; DOI=10.1023/a:1022877524469;
RA O'Regan S., Meunier F.-M.;
RT "Selection and characterization of the choline transport mutation
RT suppressor from Torpedo electric lobe, CTL1.";
RL Neurochem. Res. 28:551-555(2003).
CC -!- FUNCTION: Probable choline transporter. May be involved in membrane
CC synthesis and myelin production. {ECO:0000269|PubMed:10677542,
CC ECO:0000269|PubMed:12675144}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12352613}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:12352613}.
CC -!- TISSUE SPECIFICITY: Present in myelinated structures from brain and
CC spinal cord (at protein level). {ECO:0000269|PubMed:12352613,
CC ECO:0000269|PubMed:12675144}.
CC -!- SIMILARITY: Belongs to the CTL (choline transporter-like) family.
CC {ECO:0000305}.
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DR EMBL; AJ245618; CAB75556.1; -; mRNA.
DR AlphaFoldDB; Q9I9B9; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR007603; Choline_transptr-like.
DR PANTHER; PTHR12385; PTHR12385; 1.
DR Pfam; PF04515; Choline_transpo; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..646
FT /note="Choline transporter-like protein 1"
FT /id="PRO_0000191715"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..331
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..435
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..559
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 581..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 646 AA; 72254 MW; A19A0E1D81453F6F CRC64;
MGCCGCGSEE GSVRQWKPLE QRSCTDVLWL LIFVLFCIGM AIICGFAIAS GAAQRLVFGY
DSYGNICGHK NTEIKDVTMS GLDHTDKKYV FFFEPCNWDM VHLKILSVAL CVTKCPDMDL
KTLEDVRNFA KYNGSRLCLY NLDPTQYTSK NSKSCPILPV KSSKPIPFFH RCVPMDSGCK
INFKALTTFV SYNSVLQRVI TGVMTSKEII VGLCLMSLVL SILLMVIIRY ISKVLVWILA
ILTIIGSIGG TAVLWWLYAD HKKTLKLDPS QGDVAADNVT ALLVCAIIAT VITVILLLLM
LIMRKRVALT IALFHVAGKV FIHIPFLIFQ SLWTFLALAF FWIYWIAVLL LLATAGYPQK
KDQGYVEFKV SGPLQYTWIY HLVGLIWISE FILACQQMTI AGAVVTYYFT RDKHNLPATP
ILASMCRLIK YHLGTVAKGS FIITLIKIPQ MILVYIHSQL KGKENACAKC MLKACMCCLW
CLEKCLLYLN RNAYIATSIN GTSFCTSAKD AIVILVENAM RVAAINTVGD FVLFLGKLLI
VLVTGFVGII LLNYQRDYTV WVLPLIIICL FAFFVSHCFL SIYEMVVDVL FLCFAVDCKH
NDGSPGREYY MDKSLMEFMD ESRKAMRSVT GSGAEMKSMA SGSDNA
