ID   CTL2_MOUSE              Reviewed;         706 AA.
AC   Q8BY89; Q8K2F1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Choline transporter-like protein 2;
DE   AltName: Full=Solute carrier family 44 member 2;
GN   Name=Slc44a2; Synonyms=Ctl2;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Czech II; TISSUE=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   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187 AND ASN-200.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA   Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187 AND ASN-200.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
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).
RN   [6]
RP   CHARACTERIZATION OF ISOFORMS 1 AND 3, ALTERNATIVE PROMOTER USAGE, TISSUE
RP   SPECIFICITY, AND GLYCOSYLATION.
RX   PubMed=20665236; DOI=10.1007/s10930-010-9268-y;
RA   Kommareddi P.K., Nair T.S., Thang L.V., Galano M.M., Babu E., Ganapathy V.,
RA   Kanazawa T., McHugh J.B., Carey T.E.;
RT   "Isoforms, expression, glycosylation, and tissue distribution of
RT   CTL2/SLC44A2.";
RL   Protein J. 29:417-426(2010).
CC   -!- FUNCTION: Choline/H+ antiporter, mainly in mitochodria. Also acts as a
CC       low-affinity ethanolamine/H+ antiporter, regulating the supply of
CC       extracellular ethanolamine (Etn) for the CDP-Etn pathway, redistribute
CC       intracellular Etn and balance the CDP-Cho and CDP-Etn arms of the
CC       Kennedy pathway. {ECO:0000250|UniProtKB:Q8IWA5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=choline(out) + n H(+)(in) = choline(in) + n H(+)(out);
CC         Xref=Rhea:RHEA:75463, ChEBI:CHEBI:15354, ChEBI:CHEBI:15378;
CC         Evidence={ECO:0000250|UniProtKB:Q8IWA5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ethanolamine(out) + n H(+)(in) = ethanolamine(in) + n
CC         H(+)(out); Xref=Rhea:RHEA:75467, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57603; Evidence={ECO:0000250|UniProtKB:Q8IWA5};
CC   -!- SUBUNIT: Interacts with COCH. {ECO:0000250|UniProtKB:Q8IWA5}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IWA5};
CC       Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:Q8IWA5}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Mainly expressed in mitochondria.
CC       {ECO:0000250|UniProtKB:B4F795}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=2;
CC       Name=1; Synonyms=CTL2a, CTL2P2;
CC         IsoId=Q8BY89-1; Sequence=Displayed;
CC       Name=2; Synonyms=CTL2b, CTL2P1;
CC         IsoId=Q8BY89-2; Sequence=VSP_015432;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in lung, colon, inner ear
CC       and spleen (at protein level). Progressively lower levels in brain,
CC       tongue, liver and kidney (at protein level). In the kidney, prominent
CC       expression in glomeruli in the lining of Bowman's capsule and on the
CC       mesangial cells adjacent to the vessels within the glomerulus (at
CC       protein level). Strongly expressed on the membranes of splenocytes and
CC       in lung parenchyme (at protein level). {ECO:0000269|PubMed:20665236}.
CC   -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed at higher levels than
CC       isoform 2 in colon, heart, kidney, lung, cochlea, tongue and muscle, as
CC       well as in the inner ear. {ECO:0000269|PubMed:20665236}.
CC   -!- TISSUE SPECIFICITY: [Isoform 2]: Predominantly expressed in brain,
CC       liver and spleen. {ECO:0000269|PubMed:20665236}.
CC   -!- PTM: Glycosylated, glycosylation differs from tissue to tissue. The
CC       molecular mass of the mature glycosylated protein is highest in kidney,
CC       followed by lung, colon and spleen, then brain and tongue.
CC       {ECO:0000269|PubMed:20665236}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CTL (choline transporter-like) family.
CC       {ECO:0000305}.
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DR   EMBL; AK041533; BAC30976.1; -; mRNA.
DR   EMBL; AK048648; BAC33409.1; -; mRNA.
DR   EMBL; BC031535; AAH31535.1; -; mRNA.
DR   CCDS; CCDS22903.1; -. [Q8BY89-1]
DR   CCDS; CCDS90511.1; -. [Q8BY89-2]
DR   RefSeq; NP_001186115.1; NM_001199186.1. [Q8BY89-2]
DR   RefSeq; NP_690021.1; NM_152808.3. [Q8BY89-1]
DR   AlphaFoldDB; Q8BY89; -.
DR   BioGRID; 212989; 4.
DR   STRING; 10090.ENSMUSP00000034697; -.
DR   TCDB; 2.A.92.1.2; the choline transporter-like (ctl) family.
DR   GlyConnect; 2211; 3 N-Linked glycans (2 sites).
DR   GlyCosmos; Q8BY89; 3 sites, 3 glycans.
DR   GlyGen; Q8BY89; 4 sites, 3 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q8BY89; -.
DR   PhosphoSitePlus; Q8BY89; -.
DR   SwissPalm; Q8BY89; -.
DR   EPD; Q8BY89; -.
DR   jPOST; Q8BY89; -.
DR   MaxQB; Q8BY89; -.
DR   PaxDb; 10090-ENSMUSP00000034697; -.
DR   PeptideAtlas; Q8BY89; -.
DR   ProteomicsDB; 277919; -. [Q8BY89-1]
DR   ProteomicsDB; 277920; -. [Q8BY89-2]
DR   Pumba; Q8BY89; -.
DR   Antibodypedia; 1011; 150 antibodies from 24 providers.
DR   DNASU; 68682; -.
DR   Ensembl; ENSMUST00000034697.8; ENSMUSP00000034697.8; ENSMUSG00000057193.9. [Q8BY89-1]
DR   Ensembl; ENSMUST00000217461.2; ENSMUSP00000150147.2; ENSMUSG00000057193.9. [Q8BY89-2]
DR   GeneID; 68682; -.
DR   KEGG; mmu:68682; -.
DR   UCSC; uc009okz.2; mouse. [Q8BY89-2]
DR   UCSC; uc009ola.2; mouse. [Q8BY89-1]
DR   AGR; MGI:1915932; -.
DR   CTD; 57153; -.
DR   MGI; MGI:1915932; Slc44a2.
DR   VEuPathDB; HostDB:ENSMUSG00000057193; -.
DR   eggNOG; KOG1362; Eukaryota.
DR   GeneTree; ENSGT00940000158178; -.
DR   HOGENOM; CLU_017181_3_1_1; -.
DR   InParanoid; Q8BY89; -.
DR   OMA; CIAYWAC; -.
DR   OrthoDB; 551961at2759; -.
DR   PhylomeDB; Q8BY89; -.
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-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 68682; 0 hits in 80 CRISPR screens.
DR   ChiTaRS; Slc44a2; mouse.
DR   PRO; PR:Q8BY89; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q8BY89; Protein.
DR   Bgee; ENSMUSG00000057193; Expressed in vestibular membrane of cochlear duct and 257 other cell types or tissues.
DR   ExpressionAtlas; Q8BY89; baseline and differential.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0015220; F:choline transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0034228; F:ethanolamine transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015871; P:choline transport; ISS:UniProtKB.
DR   GO; GO:0034229; P:ethanolamine transport; ISS:UniProtKB.
DR   GO; GO:0055085; P:transmembrane transport; ISO:MGI.
DR   InterPro; IPR007603; Choline_transptr-like.
DR   PANTHER; PTHR12385; CHOLINE TRANSPORTER-LIKE (SLC FAMILY 44); 1.
DR   PANTHER; PTHR12385:SF34; CHOLINE TRANSPORTER-LIKE PROTEIN 2; 1.
DR   Pfam; PF04515; Choline_transpo; 1.
DR   Genevisible; Q8BY89; MM.
PE   1: Evidence at protein level;
KW   Alternative promoter usage; Antiport; Cell membrane; Glycoprotein;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..706
FT                   /note="Choline transporter-like protein 2"
FT                   /id="PRO_0000191718"
FT   TOPO_DOM        1..33
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..232
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        254..256
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        278..315
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        337..364
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        386..454
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        455..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        478..504
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        505..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        526..563
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        564..584
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        585..599
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        600..620
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        621..638
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        639..659
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        660..706
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         14
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWA5"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   CARBOHYD        417
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..12
FT                   /note="MGKDSQNYYGKH -> MEDDRKDAVY (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_015432"
SQ   SEQUENCE   706 AA;  80110 MW;  954AFD393C69A009 CRC64;
     MGKDSQNYYG KHGTPQKYDP TFKGPIYNRG CTDVICCVLL FLAIVGYVAV GIIAWTHGDP
     RKVIYPTDSR GEFCGQKGTK NADKPFLFYF NIVKCANPLV LLEFHCPTPQ ICVKQCPDRY
     LTLLSARNTR DFDYYKQFCV PGFQNNKGVT EILRDGECPA VITPSKPLAQ RCFPAIHASK
     GVLMVGNETT YEDGHGARKN ITDLVEGAKK ANKILEARQL AMQIFEDYTV SWYWIIIGLV
     IAMVLSLLFI VLLRFLAGIM VWVMIVMVIL VLGYGIFHCY MEYSRLRGEA GSDVSLVDLG
     FQTDLRVYLH LRQTWMAFMI ILSILEVVII LLLIFLRKRI LIAIALIKEA SRAVGHVMCS
     LLYPLVTFFL LCLCIAYWAS TSVFLSTSNT AVYKVVDDTA CPLLRKTCNP ETFPLRNESL
     QCPTARCQFA FYGGESTYHR ALLGLQIFNA FMFFWLANFV LALGQVTLAG AFASYYWAMR
     KPDDMPAFPL FSAFGRALRY HTGSLAFGSL ILAIVQIIRV MLEYLDQRLK AAQNKFAKFL
     MVCLKCCFWC LEKFIKFLNR NAYIMIAIYG TNFCTSARNA FFLLMRNIIR VAVLDKVTDF
     LFLLGKLLIV GSVGILAFFF FTHRIRIVQD TAPPLNYYWV PILTVIIGSY LIAHGFFSVY
     GMCVDTLFLC FLEDLERNDG SAERPYFMSS TLKKLLNKTN KKVAES
//