CTL2_MOUSE
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 03-AUG-2022, entry version 137.
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 transporter. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with COCH. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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). Isoform 1 is expressed at higher
CC levels than isoform 2 in colon, heart, kidney, lung, cochlea, tongue
CC and muscle, as well as in the inner ear. Isoform 2 is predominant in
CC brain, liver and spleen. {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; 2.
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 GlyGen; Q8BY89; 3 sites, 3 N-linked glycans (2 sites).
DR iPTMnet; Q8BY89; -.
DR PhosphoSitePlus; Q8BY89; -.
DR SwissPalm; Q8BY89; -.
DR EPD; Q8BY89; -.
DR jPOST; Q8BY89; -.
DR MaxQB; Q8BY89; -.
DR PaxDb; Q8BY89; -.
DR PeptideAtlas; Q8BY89; -.
DR PRIDE; Q8BY89; -.
DR ProteomicsDB; 277919; -. [Q8BY89-1]
DR ProteomicsDB; 277920; -. [Q8BY89-2]
DR Antibodypedia; 1011; 137 antibodies from 24 providers.
DR DNASU; 68682; -.
DR Ensembl; ENSMUST00000034697; ENSMUSP00000034697; ENSMUSG00000057193. [Q8BY89-1]
DR Ensembl; ENSMUST00000217461; ENSMUSP00000150147; ENSMUSG00000057193. [Q8BY89-2]
DR GeneID; 68682; -.
DR KEGG; mmu:68682; -.
DR UCSC; uc009okz.2; mouse. [Q8BY89-2]
DR UCSC; uc009ola.2; mouse. [Q8BY89-1]
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; 329225at2759; -.
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 75 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 253 other tissues.
DR ExpressionAtlas; Q8BY89; baseline and differential.
DR Genevisible; Q8BY89; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0015220; F:choline transmembrane transporter activity; ISO:MGI.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015871; P:choline transport; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; ISO:MGI.
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 promoter usage; Glycoprotein; 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
