CTL1_MOUSE
ID CTL1_MOUSE Reviewed; 653 AA.
AC Q6X893; Q14DK0; Q6X894; Q8R0Y4; Q91Z29;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 125.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Fibroblast;
RX PubMed=15474312; DOI=10.1016/j.gene.2004.07.042;
RA Yuan Z., Wagner L., Poloumienko A., Bakovic M.;
RT "Identification and expression of a mouse muscle-specific CTL1 gene.";
RL Gene 341:305-312(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver, and Mammary gland;
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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Choline transporter. May be involved in membrane synthesis
CC and myelin production. {ECO:0000269|PubMed:15474312,
CC ECO:0000269|PubMed:19357133}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Mitochondrion outer membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A;
CC IsoId=Q6X893-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q6X893-2; Sequence=VSP_015428;
CC -!- TISSUE SPECIFICITY: Specifically abundant in skeletal muscle (at
CC protein level). {ECO:0000269|PubMed:15474312}.
CC -!- SIMILARITY: Belongs to the CTL (choline transporter-like) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25941.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY249865; AAP81042.1; -; mRNA.
DR EMBL; AY249866; AAP81043.1; -; mRNA.
DR EMBL; AL805900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL807745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010258; AAH10258.1; -; mRNA.
DR EMBL; BC025941; AAH25941.1; ALT_INIT; mRNA.
DR EMBL; BC113167; AAI13168.1; -; mRNA.
DR EMBL; BC113169; AAI13170.1; -; mRNA.
DR CCDS; CCDS18189.1; -. [Q6X893-1]
DR RefSeq; NP_598652.3; NM_133891.3. [Q6X893-1]
DR AlphaFoldDB; Q6X893; -.
DR BioGRID; 221443; 4.
DR STRING; 10090.ENSMUSP00000099975; -.
DR TCDB; 2.A.92.1.1; the choline transporter-like (ctl) family.
DR GlyConnect; 2210; 5 N-Linked glycans (1 site).
DR GlyGen; Q6X893; 1 site, 4 N-linked glycans (1 site).
DR iPTMnet; Q6X893; -.
DR PhosphoSitePlus; Q6X893; -.
DR SwissPalm; Q6X893; -.
DR jPOST; Q6X893; -.
DR MaxQB; Q6X893; -.
DR PaxDb; Q6X893; -.
DR PRIDE; Q6X893; -.
DR ProteomicsDB; 285393; -. [Q6X893-1]
DR ProteomicsDB; 285394; -. [Q6X893-2]
DR Antibodypedia; 14793; 301 antibodies from 30 providers.
DR DNASU; 100434; -.
DR Ensembl; ENSMUST00000102911; ENSMUSP00000099975; ENSMUSG00000028412. [Q6X893-1]
DR GeneID; 100434; -.
DR KEGG; mmu:100434; -.
DR UCSC; uc008swz.2; mouse. [Q6X893-1]
DR CTD; 23446; -.
DR MGI; MGI:2140592; Slc44a1.
DR VEuPathDB; HostDB:ENSMUSG00000028412; -.
DR eggNOG; KOG1362; Eukaryota.
DR GeneTree; ENSGT00940000157174; -.
DR InParanoid; Q6X893; -.
DR OMA; YCLEKFI; -.
DR TreeFam; TF313325; -.
DR Reactome; R-MMU-1483191; Synthesis of PC.
DR Reactome; R-MMU-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR Reactome; R-MMU-6798163; Choline catabolism.
DR BioGRID-ORCS; 100434; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Slc44a1; mouse.
DR PRO; PR:Q6X893; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6X893; protein.
DR Bgee; ENSMUSG00000028412; Expressed in hair follicle and 285 other tissues.
DR ExpressionAtlas; Q6X893; baseline and differential.
DR Genevisible; Q6X893; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; Cell membrane; Lipoprotein; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Myristate; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..653
FT /note="Choline transporter-like protein 1"
FT /id="PRO_0000191713"
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="Mitochondrial intermembrane"
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="Mitochondrial intermembrane"
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="Mitochondrial intermembrane"
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..536
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..565
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..653
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 650..653
FT /note="LRKR -> VGSEEEAAALHDFPFHFFSVCVFTDCTSSGEALVVCITQDMLLF
FT LFACLPITWMAEVLSQLRLPSVKVS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15474312"
FT /id="VSP_015428"
FT CONFLICT 426
FT /note="P -> L (in Ref. 1; AAP81042/AAP81043)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="L -> F (in Ref. 1; AAP81042/AAP81043)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="F -> L (in Ref. 1; AAP81042/AAP81043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 653 AA; 73067 MW; 639979730CFE5913 CRC64;
MGCCSSASAA QSSKREWKPL EDRSCTDIPW LLLFVLFCIG MGFICGFSVA TGAAARLVSG
YDSYGNICGQ RNAKLEAIPN SGLDHTHRKY VFFLDPCNLD LINRKIKSIA LCVAACPRQE
LKTLSDVQKF AEINGSALCS YNIKPSEYTL TSKSSGFCPK LPVPASAPIP FFHRCAPVNI
SCYAKFAEAL ITFVSDNSVL HRLISGVMTS KEIILGLCLL SLVLSMILMV IIRYISRVLV
WILTVLVILG SLGGTGVLWW LYAKQRRSPK EAVIPEQLQI AEDNLRALLI YAISATVFTV
ILFLIMLVMR KRVALTIALF HVAGKVFIHL PLLVFQPFWT FFALVLFWAY WIMTLLFLGT
TGSAVQNEQG FVEYKISGPL QYMWWYHVVG LIWISEFILA CQQMTVAGAV VTYYFTRDKR
NLPFTPILAS VNRLIRYHLG TVAKGSFIIT LVKIPRMVLM YIHSQLKGKE NACARCMLKS
CICCLWCLEK CLSYLNQNAY TATAINSTNF CTSAKDAFVI LVENALRVAA INTVGDFMLF
LGKVLIVCST GLAGIMLLNY QQDYTVWVLP LIIVCLFAFL VAHCFLSIYE MVVDVLFLCF
AIDTKYNDGS PGREFYMDKV LMEFVENSRK AMKEAGKGGA ADARELKPML RKR
