CTL1_RAT
ID CTL1_RAT Reviewed; 656 AA.
AC Q8VII6; Q9JJZ7;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Choline transporter-like protein 1;
DE AltName: Full=Solute carrier family 44 member 1;
DE AltName: CD_antigen=CD92;
GN Name=Slc44a1; Synonyms=Cd92, Cdw92, Ctl1;
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] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=15715662; DOI=10.1111/j.1471-4159.2004.02962.x;
RA Traiffort E., Ruat M., O'Regan S., Meunier F.-M.;
RT "Molecular characterization of the family of choline transporter-like
RT proteins and their splice variants.";
RL J. Neurochem. 92:1116-1125(2005).
RN [3]
RP PROTEIN SEQUENCE OF 2-14; 57-71; 75-88; 90-104; 108-118; 161-174; 186-211;
RP 271-286; 421-433; 516-527; 620-629; 631-644 AND 646-656, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
RP INDUCTION.
RX PubMed=12007839; DOI=10.1016/s0169-328x(02)00182-1;
RA Che Y.H., Yamashita T., Higuchi H., Tohyama M.;
RT "Changes in mRNA for choline transporter-like protein following facial
RT nerve transection.";
RL Brain Res. Mol. Brain Res. 101:122-125(2002).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16000150; DOI=10.1111/j.1471-4159.2005.03299.x;
RA Inazu M., Takeda H., Matsumiya T.;
RT "Molecular and functional characterization of an Na-independent choline
RT transporter in rat astrocytes.";
RL J. Neurochem. 94:1427-1437(2005).
RN [6]
RP INDUCTION.
RX PubMed=15691711; DOI=10.1016/j.mcn.2004.09.014;
RA Lecomte M.-J., De Gois S., Guerci A., Ravassard P., Faucon Biguet N.,
RA Mallet J., Berrard S.;
RT "Differential expression and regulation of the high-affinity choline
RT transporter CHT1 and choline acetyltransferase in neurons of superior
RT cervical ganglia.";
RL Mol. Cell. Neurosci. 28:303-313(2005).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-134 AND ASN-179, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: Probable choline transporter. May be involved in membrane
CC synthesis and myelin production. {ECO:0000269|PubMed:15715662,
CC ECO:0000269|PubMed:16000150}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=CTL1a;
CC IsoId=Q8VII6-1; Sequence=Displayed;
CC Name=2; Synonyms=CTL1b;
CC IsoId=Q8VII6-2; Sequence=VSP_015429, VSP_015430;
CC -!- TISSUE SPECIFICITY: Expressed in neurons, oligodendrocytes and
CC astrocytes. Also expressed in the mucosal cell layer of the colon. In
CC the developing brain, isoform 1 is expressed in both neurones and
CC oligodendroglial cells, whereas isoform 2 is restricted to
CC oligodendroglial cells. {ECO:0000269|PubMed:10677542,
CC ECO:0000269|PubMed:15715662, ECO:0000269|PubMed:16000150}.
CC -!- INDUCTION: By leukemia inhibitory factor or retinoic acid in vitro. In
CC vivo, induced during the axonal elongation period following axotomy.
CC {ECO:0000269|PubMed:12007839, ECO:0000269|PubMed:15691711}.
CC -!- SIMILARITY: Belongs to the CTL (choline transporter-like) family.
CC {ECO:0000305}.
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DR EMBL; AJ245619; CAB75555.1; -; mRNA.
DR EMBL; AJ420809; CAD12728.1; -; mRNA.
DR RefSeq; NP_001029024.1; NM_001033852.1.
DR RefSeq; NP_445944.2; NM_053492.3.
DR AlphaFoldDB; Q8VII6; -.
DR SMR; Q8VII6; -.
DR STRING; 10116.ENSRNOP00000024229; -.
DR GlyGen; Q8VII6; 2 sites, 6 N-linked glycans (2 sites).
DR iPTMnet; Q8VII6; -.
DR SwissPalm; Q8VII6; -.
DR jPOST; Q8VII6; -.
DR PaxDb; Q8VII6; -.
DR PRIDE; Q8VII6; -.
DR GeneID; 85254; -.
DR KEGG; rno:85254; -.
DR UCSC; RGD:621426; rat. [Q8VII6-1]
DR CTD; 23446; -.
DR RGD; 621426; Slc44a1.
DR eggNOG; KOG1362; Eukaryota.
DR InParanoid; Q8VII6; -.
DR OrthoDB; 329225at2759; -.
DR PhylomeDB; Q8VII6; -.
DR Reactome; R-RNO-1483191; Synthesis of PC.
DR Reactome; R-RNO-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR Reactome; R-RNO-6798163; Choline catabolism.
DR PRO; PR:Q8VII6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0015220; F:choline transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015871; P:choline transport; IMP:ARUK-UCL.
DR GO; GO:0055085; P:transmembrane transport; IMP:ARUK-UCL.
DR InterPro; IPR007603; Choline_transptr-like.
DR PANTHER; PTHR12385; PTHR12385; 1.
DR Pfam; PF04515; Choline_transpo; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Glycoprotein; Lipoprotein;
KW Membrane; Myristate; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..656
FT /note="Choline transporter-like protein 1"
FT /id="PRO_0000191714"
FT TOPO_DOM 2..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..337
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..441
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..565
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..656
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 635..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWI5"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT VAR_SEQ 650..653
FT /note="ASGA -> LRKR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10677542"
FT /id="VSP_015429"
FT VAR_SEQ 654..656
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10677542"
FT /id="VSP_015430"
FT CONFLICT 267
FT /note="R -> S (in Ref. 1; CAB75555)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="K -> E (in Ref. 1; CAB75555)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 656 AA; 73092 MW; 217AAD02F6E4D138 CRC64;
MGCCSSASAA QSSKREWKPL EDRSCTDIPW LLLFVLFCIG MGFICGFSVA TGAAARLVSG
YDSYGNICGQ RNAKLEAIAN SGLDHTHRKY VFFLDPCNLD LINRKIKSMA LCVAACPRQE
LKTLSDVQKF AEINGSALCS YNIKPSEYTL TAKSSAFCPK LPVPASAPIP FFHRCAPVNI
SCYAKFAEAL ITFVSDNSVL HRLISGVMTS KEIILGLCLL SLVLSMILMV IIRYISRVLV
WILTILVILG SLGGTGVLWW LYAKQRRSPK ETVIPEQLQI AEDNLRALLI YAISATVFTV
ILFLIMLVMR KRVALTIALF HVAGKVFIHL PLLVFQPFWT FFALVLFWAY WIMTLLFLGT
TGSAVQNEQG FVEYKISGPL QYMWWYHVVG LIWISEFILA CQQMTVAGAV VTYYFTRDKR
NLPFTPILAS VNRLIRYHLG TVAKGSFIIT LVKIPRMILM YIHSQLKGKE NACARCMLKS
CICCLWCLEK CLSYLNQNAY TATAINSTNF CTSAKDAFVI LVENALRVAA INTVGDFMLF
LGKVLIVCST GLAGIMLLNY QQDYTVWVLP LIIVCLFAFL VAHCFLSIYE MVVDVLFLCF
AIDTKYNDGS PGREFYMDKV LMEFVENSRK AMKEAGKGGA ADARKLKPMA SGASSA
