CTL2_DICDI
ID CTL2_DICDI Reviewed; 628 AA.
AC Q54I48;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Choline transporter-like protein 2;
DE AltName: Full=Solute carrier family 44 member 2;
GN Name=slc44a2; Synonyms=ctl2; ORFNames=DDB_G0289013;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CTL (choline transporter-like) family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000129; EAL62922.1; -; Genomic_DNA.
DR RefSeq; XP_636423.1; XM_631331.1.
DR AlphaFoldDB; Q54I48; -.
DR PaxDb; Q54I48; -.
DR EnsemblProtists; EAL62922; EAL62922; DDB_G0289013.
DR GeneID; 8626914; -.
DR KEGG; ddi:DDB_G0289013; -.
DR dictyBase; DDB_G0289013; slc44a2.
DR eggNOG; KOG1362; Eukaryota.
DR HOGENOM; CLU_017181_3_1_1; -.
DR InParanoid; Q54I48; -.
DR OMA; YCLEKFI; -.
DR PhylomeDB; Q54I48; -.
DR Reactome; R-DDI-1483191; Synthesis of PC.
DR Reactome; R-DDI-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR Reactome; R-DDI-6798163; Choline catabolism.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q54I48; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR007603; Choline_transptr-like.
DR PANTHER; PTHR12385; PTHR12385; 1.
DR Pfam; PF04515; Choline_transpo; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..628
FT /note="Choline transporter-like protein 2"
FT /id="PRO_0000327935"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..204
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..282
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..381
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..530
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..559
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 581..628
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 628 AA; 71809 MW; B095D3138E9305A6 CRC64;
MSSEDLQDHH EIGNEVIKKK GVYTKKKCQD CFFLILFLLF WAGMIVVAAF GVKNGKPDRI
VKGTDQYGNI CGVNNIEQGI LNETQARDTT NEPYVYFIYY PDLIGINYRV ICIEECPNST
YTDLNDPNQL ICDYGTVPAT NQISPNGTCM GKIKSKLIFN RCIPDVTNTS VVLNSIVDEI
YQFVNNQLTS DLSVEILTDL TNSWRYLIYG ALIAMGLGLT WIFLLRFFAG FITWLTVFAA
YACLGLLTAQ VYFQWQDSKD AYENTIPSQR LVMQEKNILA LKVIFIILCV VCGIFALILL
ALFSRIRIAI RIIKECSRAI GIMPSIFFFP IFIFLLLCGF TVYWVYIGVY LATAGSPTYD
DQYRFTGYEA DSKLQKIQIY HFFGYLWTFA FILALNQTTI AGAISSWYWV QDKKDTPFFP
VWSSFFRVIR YHLGSIALGS LILAIVQFIR WVLRFLEKKF KGKEAYLARF IVRCLNCIFG
CFERFIKFLD KNAYIMVSIY GYSFCQGAKR GFQLVLTNIL RVAAVNLVSS FLMFLGRVFI
TAATVGISLY LLKEHENLSF YIIPVILIGF IAFAISTGFM SVYDMSIDTM LLCFCEDCER
NDGSPERPYY MSKSLRKFVD GKGRSKCC
