CTL1_HUMAN
ID CTL1_HUMAN Reviewed; 657 AA.
AC Q8WWI5; A6NLZ9; Q5VUB3; Q8WVB0; Q96KU3; Q9NY69;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Choline transporter-like protein 1;
DE AltName: Full=CDw92;
DE AltName: Full=Solute carrier family 44 member 1;
DE AltName: CD_antigen=CD92;
GN Name=SLC44A1; Synonyms=CD92, CDW92, CTL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 2).
RC TISSUE=Ewing sarcoma;
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 3), TISSUE SPECIFICITY, AND VARIANT
RP ALA-644.
RX PubMed=11698453; DOI=10.4049/jimmunol.167.10.5795;
RA Wille S., Szekeres A., Majdic O., Prager E., Staffler G., Stoeckl J.,
RA Kunthalert D., Prieschl E.E., Baumruker T., Burtscher H., Zlabinger G.J.,
RA Knapp W., Stockinger H.;
RT "Characterization of CDw92 as a member of the choline transporter-like
RT protein family regulated specifically on dendritic cells.";
RL J. Immunol. 167:5795-5804(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Ewing sarcoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP FUNCTION, TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=19357133; DOI=10.1096/fj.08-121491;
RA Michel V., Bakovic M.;
RT "The solute carrier 44A1 is a mitochondrial protein and mediates choline
RT transport.";
RL FASEB J. 23:2749-2758(2009).
RN [8]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP INVOLVEMENT IN CONATOC, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31855247; DOI=10.1093/brain/awz376;
RA Fagerberg C.R., Taylor A., Distelmaier F., Schroeder H.D., Kibaek M.,
RA Wieczorek D., Tarnopolsky M., Brady L., Larsen M.J., Jamra R.A., Seibt A.,
RA Hejboel E.K., Gade E., Markovic L., Klee D., Nagy P., Rouse N., Agarwal P.,
RA Dolinsky V.W., Bakovic M.;
RT "Choline transporter-like 1 deficiency causes a new type of childhood-onset
RT neurodegeneration.";
RL Brain 143:94-111(2020).
CC -!- FUNCTION: Choline transporter. Involved in membrane synthesis and
CC myelin production. {ECO:0000269|PubMed:19357133,
CC ECO:0000269|PubMed:31855247}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19357133,
CC ECO:0000269|PubMed:31855247}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19357133}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:19357133}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19357133, ECO:0000269|PubMed:31855247}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=A;
CC IsoId=Q8WWI5-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q8WWI5-2; Sequence=VSP_015424, VSP_015425;
CC Name=3; Synonyms=C;
CC IsoId=Q8WWI5-3; Sequence=VSP_015426, VSP_015427;
CC -!- TISSUE SPECIFICITY: Expressed in various cells of the hematopoietic
CC system. {ECO:0000269|PubMed:11698453}.
CC -!- DISEASE: Neurodegeneration, childhood-onset, with ataxia, tremor, optic
CC atrophy, and cognitive decline (CONATOC) [MIM:618868]: An autosomal
CC recessive neurodegenerative disease characterized by progressive
CC ataxia, tremor, cognitive decline, dysphagia, optic atrophy,
CC dysarthria, as well as urinary and bowel incontinence. Brain MRI
CC demonstrates cerebellar atrophy and leukoencephalopathy.
CC {ECO:0000269|PubMed:31855247}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CTL (choline transporter-like) family.
CC {ECO:0000305}.
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DR EMBL; AJ245620; CAB75541.2; -; Genomic_DNA.
DR EMBL; AJ272365; CAC82175.1; -; mRNA.
DR EMBL; AJ420812; CAD12764.1; -; mRNA.
DR EMBL; AL161627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450265; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018213; AAH18213.1; -; mRNA.
DR EMBL; BC049203; AAH49203.1; -; mRNA.
DR CCDS; CCDS6763.1; -. [Q8WWI5-1]
DR CCDS; CCDS75868.1; -. [Q8WWI5-3]
DR CCDS; CCDS83390.1; -. [Q8WWI5-2]
DR RefSeq; NP_001273659.1; NM_001286730.1. [Q8WWI5-3]
DR RefSeq; NP_001317660.1; NM_001330731.1. [Q8WWI5-2]
DR RefSeq; NP_536856.2; NM_080546.4. [Q8WWI5-1]
DR AlphaFoldDB; Q8WWI5; -.
DR BioGRID; 117012; 41.
DR IntAct; Q8WWI5; 13.
DR MINT; Q8WWI5; -.
DR STRING; 9606.ENSP00000363852; -.
DR DrugBank; DB00122; Choline.
DR DrugBank; DB14006; Choline salicylate.
DR GuidetoPHARMACOLOGY; 1204; -.
DR TCDB; 2.A.92.1.6; the choline transporter-like (ctl) family.
DR GlyConnect; 1110; 2 N-Linked glycans (2 sites).
DR GlyGen; Q8WWI5; 3 sites, 2 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q8WWI5; -.
DR PhosphoSitePlus; Q8WWI5; -.
DR SwissPalm; Q8WWI5; -.
DR BioMuta; SLC44A1; -.
DR DMDM; 73918923; -.
DR EPD; Q8WWI5; -.
DR jPOST; Q8WWI5; -.
DR MassIVE; Q8WWI5; -.
DR MaxQB; Q8WWI5; -.
DR PaxDb; Q8WWI5; -.
DR PeptideAtlas; Q8WWI5; -.
DR PRIDE; Q8WWI5; -.
DR ProteomicsDB; 74892; -. [Q8WWI5-1]
DR ProteomicsDB; 74893; -. [Q8WWI5-2]
DR ProteomicsDB; 74894; -. [Q8WWI5-3]
DR Antibodypedia; 14793; 301 antibodies from 30 providers.
DR DNASU; 23446; -.
DR Ensembl; ENST00000374720.8; ENSP00000363852.3; ENSG00000070214.16. [Q8WWI5-1]
DR Ensembl; ENST00000374723.5; ENSP00000363855.1; ENSG00000070214.16. [Q8WWI5-3]
DR Ensembl; ENST00000374724.1; ENSP00000363856.1; ENSG00000070214.16. [Q8WWI5-2]
DR Ensembl; ENST00000470972.5; ENSP00000433072.1; ENSG00000070214.16. [Q8WWI5-1]
DR GeneID; 23446; -.
DR KEGG; hsa:23446; -.
DR MANE-Select; ENST00000374720.8; ENSP00000363852.3; NM_080546.5; NP_536856.2.
DR UCSC; uc004bcn.5; human. [Q8WWI5-1]
DR CTD; 23446; -.
DR DisGeNET; 23446; -.
DR GeneCards; SLC44A1; -.
DR HGNC; HGNC:18798; SLC44A1.
DR HPA; ENSG00000070214; Tissue enhanced (brain).
DR MalaCards; SLC44A1; -.
DR MIM; 606105; gene.
DR MIM; 618868; phenotype.
DR neXtProt; NX_Q8WWI5; -.
DR OpenTargets; ENSG00000070214; -.
DR PharmGKB; PA134958011; -.
DR VEuPathDB; HostDB:ENSG00000070214; -.
DR eggNOG; KOG1362; Eukaryota.
DR GeneTree; ENSGT00940000157174; -.
DR HOGENOM; CLU_017181_2_0_1; -.
DR InParanoid; Q8WWI5; -.
DR OMA; YCLEKFI; -.
DR OrthoDB; 329225at2759; -.
DR PhylomeDB; Q8WWI5; -.
DR TreeFam; TF313325; -.
DR PathwayCommons; Q8WWI5; -.
DR Reactome; R-HSA-1483191; Synthesis of PC.
DR Reactome; R-HSA-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR Reactome; R-HSA-6798163; Choline catabolism.
DR SignaLink; Q8WWI5; -.
DR BioGRID-ORCS; 23446; 11 hits in 1075 CRISPR screens.
DR ChiTaRS; SLC44A1; human.
DR GeneWiki; SLC44A1; -.
DR GenomeRNAi; 23446; -.
DR Pharos; Q8WWI5; Tbio.
DR PRO; PR:Q8WWI5; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8WWI5; protein.
DR Bgee; ENSG00000070214; Expressed in endothelial cell and 200 other tissues.
DR ExpressionAtlas; Q8WWI5; baseline and differential.
DR Genevisible; Q8WWI5; HS.
DR GO; GO:0005829; C:cytosol; IDA:ARUK-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:ARUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0015220; F:choline transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042426; P:choline catabolic process; TAS:Reactome.
DR GO; GO:0015871; P:choline transport; IDA:ARUK-UCL.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS: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; Cell membrane; Lipoprotein; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Myristate; Neurodegeneration; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:22223895,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..657
FT /note="Choline transporter-like protein 1"
FT /id="PRO_0000191712"
FT TOPO_DOM 2..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..212
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..288
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..338
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..537
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 559..566
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 567..587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 588..653
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 635..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:22223895"
FT VAR_SEQ 651..654
FT /note="ASGA -> LKKR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_015424"
FT VAR_SEQ 651..652
FT /note="AS -> IK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11698453"
FT /id="VSP_015426"
FT VAR_SEQ 653..657
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11698453"
FT /id="VSP_015427"
FT VAR_SEQ 655..657
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_015425"
FT VARIANT 644
FT /note="S -> A (in dbSNP:rs3199966)"
FT /evidence="ECO:0000269|PubMed:11698453"
FT /id="VAR_048837"
FT CONFLICT 79
FT /note="I -> V (in Ref. 2; CAC82175)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 657 AA; 73302 MW; 10D70CAB8E33E3AC CRC64;
MGCCSSASSA AQSSKREWKP LEDRSCTDIP WLLLFILFCI GMGFICGFSI ATGAAARLVS
GYDSYGNICG QKNTKLEAIP NSGMDHTQRK YVFFLDPCNL DLINRKIKSV ALCVAACPRQ
ELKTLSDVQK FAEINGSALC SYNLKPSEYT TSPKSSVLCP KLPVPASAPI PFFHRCAPVN
ISCYAKFAEA LITFVSDNSV LHRLISGVMT SKEIILGLCL LSLVLSMILM VIIRYISRVL
VWILTILVIL GSLGGTGVLW WLYAKQRRSP KETVTPEQLQ IAEDNLRALL IYAISATVFT
VILFLIMLVM RKRVALTIAL FHVAGKVFIH LPLLVFQPFW TFFALVLFWV YWIMTLLFLG
TTGSPVQNEQ GFVEFKISGP LQYMWWYHVV GLIWISEFIL ACQQMTVAGA VVTYYFTRDK
RNLPFTPILA SVNRLIRYHL GTVAKGSFII TLVKIPRMIL MYIHSQLKGK ENACARCVLK
SCICCLWCLE KCLNYLNQNA YTATAINSTN FCTSAKDAFV ILVENALRVA TINTVGDFML
FLGKVLIVCS TGLAGIMLLN YQQDYTVWVL PLIIVCLFAF LVAHCFLSIY EMVVDVLFLC
FAIDTKYNDG SPGREFYMDK VLMEFVENSR KAMKEAGKGG VADSRELKPM ASGASSA
