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Choline transporter protein 1 (AtCTL1)

 CHER1_ARATH             Reviewed;         700 AA.
Q94AN2; Q9LUQ4; Q9M7X1;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 105.
RecName: Full=Choline transporter protein 1 {ECO:0000303|PubMed:25008948};
Short=AtCTL1 {ECO:0000303|PubMed:25008948};
Name=CHER1 {ECO:0000303|PubMed:25008948};
Synonyms=CTL1 {ECO:0000303|PubMed:25008948};
OrderedLocusNames=At3g15380 {ECO:0000312|Araport:AT3G15380};
ORFNames=MJK13.4 {ECO:0000312|EMBL:AAF35404.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10819329; DOI=10.1093/dnares/7.2.131;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
features of the regions of 4,504,864 bp covered by sixty P1 and TAC
clones.";
DNA Res. 7:131-135(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=25008948; DOI=10.1038/ncomms5276;
Dettmer J., Ursache R., Campilho A., Miyashima S., Belevich I.,
O'Regan S., Mullendore D.L., Yadav S.R., Lanz C., Beverina L.,
Papagni A., Schneeberger K., Weigel D., Stierhof Y.D., Moritz T.,
Knoblauch M., Jokitalo E., Helariutta Y.;
"CHOLINE TRANSPORTER-LIKE1 is required for sieve plate development to
mediate long-distance cell-to-cell communication.";
Nat. Commun. 5:4276-4276(2014).
[6]
FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-247, AND
SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=27743414; DOI=10.1111/tpj.13393;
Kraner M.E., Link K., Melzer M., Ekici A.B., Uebe S., Tarazona P.,
Feussner I., Hofmann J., Sonnewald U.;
"Choline transporter-like1 (CHER1) is crucial for plasmodesmata
maturation in Arabidopsis thaliana.";
Plant J. 89:394-406(2017).
-!- FUNCTION: Choline transporter involved in the regulation of
choline metabolite homeostasis during root and phloem development
(PubMed:25008948). Necessary for secondary plasmodesmata (PD)
formation and development. Required for PD localization of MP17,
the luteoviral movement protein (PubMed:27743414). Modulates
phloem morphogenesis and conductivity. Required for procambium
maintenance and sieve plate development (e.g. sieve plate and
sieve pore elaboration) to mediate long-distance cell-to-cell
communication via symplastic transport through the phloem
(PubMed:25008948). {ECO:0000269|PubMed:25008948,
ECO:0000269|PubMed:27743414}.
-!- SUBCELLULAR LOCATION: Early endosome membrane
{ECO:0000269|PubMed:27743414}; Multi-pass membrane protein
{ECO:0000255}. Golgi apparatus, trans-Golgi network membrane
{ECO:0000269|PubMed:25008948, ECO:0000269|PubMed:27743414}; Multi-
pass membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton,
phragmoplast {ECO:0000269|PubMed:25008948}. Note=Associated
transiently with the phragmoplast during cytokinesis. Follows a
polar localization in the forming sieve plates.
{ECO:0000269|PubMed:25008948}.
-!- DISRUPTION PHENOTYPE: Altered choline metabolite profile. Several
phenotypic abnormalities (e.g. dwarf with defects in both shoot
and root architecture), including reduced pore density and altered
pore structure in the sieve areas, associated with defective
symplastic transport through phloem. Increased number of sieve
elements (SE)-like cells instead of two companion cells (CCs) and
two SEs. Defects in procambium maintenance and phloem patterning.
Abnormal retaining of desmotubules in the symplastic space in
sieve pores (PubMed:25008948). In cher1-4, impaired secondary
plasmodesmata (PD) formation and development leading to starch and
soluble sugars excess accumulation, and stunted growth. Altered PD
localization of the luteoviral movement protein MP17. Reduced
level of choline and phosphocholine (PubMed:27743414).
{ECO:0000269|PubMed:25008948, ECO:0000269|PubMed:27743414}.
-!- SIMILARITY: Belongs to the CTL (choline transporter-like) family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF35404.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAB02367.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB022218; BAB02367.1; ALT_SEQ; Genomic_DNA.
EMBL; AC024081; AAF35404.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002686; AEE75661.1; -; Genomic_DNA.
EMBL; AY045917; AAK76591.1; -; mRNA.
EMBL; BT001974; AAN71973.1; -; mRNA.
RefSeq; NP_566511.1; NM_112406.5.
UniGene; At.11972; -.
UniGene; At.49625; -.
EnsemblPlants; AT3G15380.1; AT3G15380.1; AT3G15380.
GeneID; 820777; -.
Gramene; AT3G15380.1; AT3G15380.1; AT3G15380.
KEGG; ath:AT3G15380; -.
Araport; AT3G15380; -.
TAIR; locus:2090171; AT3G15380.
eggNOG; KOG1362; Eukaryota.
eggNOG; ENOG410XS0P; LUCA.
HOGENOM; HOG000241130; -.
KO; K15377; -.
OMA; VYWIMTL; -.
OrthoDB; EOG0936037I; -.
Reactome; R-ATH-1483191; Synthesis of PC.
Reactome; R-ATH-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
Reactome; R-ATH-6798163; Choline catabolism.
Reactome; R-ATH-6798695; Neutrophil degranulation.
PRO; PR:Q94AN2; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q94AN2; baseline and differential.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0009524; C:phragmoplast; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0009551; C:secondary plasmodesma; IMP:UniProtKB.
GO; GO:0097218; C:sieve plate; IDA:TAIR.
GO; GO:0055044; C:symplast; IMP:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
GO; GO:0015220; F:choline transmembrane transporter activity; IDA:TAIR.
GO; GO:0015871; P:choline transport; IDA:TAIR.
GO; GO:0010088; P:phloem development; IMP:TAIR.
GO; GO:0009663; P:plasmodesma organization; IMP:UniProtKB.
GO; GO:0010067; P:procambium histogenesis; IMP:UniProtKB.
GO; GO:0048364; P:root development; IMP:TAIR.
GO; GO:0090603; P:sieve element differentiation; IMP:TAIR.
GO; GO:0010051; P:xylem and phloem pattern formation; IMP:TAIR.
InterPro; IPR007603; Choline_transptr-like.
PANTHER; PTHR12385; PTHR12385; 1.
Pfam; PF04515; Choline_transpo; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein;
Endosome; Glycoprotein; Golgi apparatus; Membrane; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 700 Choline transporter protein 1.
/FTId=PRO_0000440037.
TOPO_DOM 1 33 Cytoplasmic. {ECO:0000305}.
TRANSMEM 34 54 Helical. {ECO:0000255}.
TOPO_DOM 55 241 Extracellular. {ECO:0000305}.
TRANSMEM 242 262 Helical. {ECO:0000255}.
TOPO_DOM 263 264 Cytoplasmic. {ECO:0000305}.
TRANSMEM 265 285 Helical. {ECO:0000255}.
TOPO_DOM 286 322 Extracellular. {ECO:0000305}.
TRANSMEM 323 343 Helical. {ECO:0000255}.
TOPO_DOM 344 364 Cytoplasmic. {ECO:0000305}.
TRANSMEM 365 385 Helical. {ECO:0000255}.
TOPO_DOM 386 432 Extracellular. {ECO:0000305}.
TRANSMEM 433 453 Helical. {ECO:0000255}.
TOPO_DOM 454 493 Cytoplasmic. {ECO:0000305}.
TRANSMEM 494 514 Helical. {ECO:0000255}.
TOPO_DOM 515 595 Extracellular. {ECO:0000305}.
TRANSMEM 596 616 Helical. {ECO:0000255}.
TOPO_DOM 617 633 Cytoplasmic. {ECO:0000305}.
TRANSMEM 634 654 Helical. {ECO:0000255}.
TOPO_DOM 655 700 Extracellular. {ECO:0000305}.
CARBOHYD 163 163 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 194 194 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 403 403 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
MUTAGEN 247 247 G->E: In cher1-5; impaired secondary
plasmodesmata (PD) formation and
development leading to starch and soluble
sugars excess accumulation, stunted
growth. Altered PD localization of the
luteoviral movement protein MP17.
Abnormal subcellular localization.
{ECO:0000269|PubMed:27743414}.
SEQUENCE 700 AA; 78737 MW; DF9F0E38C4E36C25 CRC64;
MRGPLGAVIG RYTSSDGSAP NDGIIKHNRK CRDITFLIIF IAFWVSMIVN SSFGFNQGNP
LRLTYGLDYE GNVCGSKHRH RDLTQLELRY WLNPNQVYES GLKDGELKLA NARTICLLDC
PAPSDDTLNW VCDYPDGEIR LKMNDWIDRN YDYFEFLTPE MRNSSLQLQG PCYPVIFPSV
NVYWSCQYIA RASNSSLRHW QQMGGVNIQE DMIIDKSIRR SMNSRASVLK RYVADIGKSW
PVLIVCGGLV PLFLSIIWLL LIRHFVAAMP WITVVLFNML LISVTVFYYL KAGWIGNDAV
TPIIGEHDPY FHVYGRELTH VRGVAILMTF ISVVAILTSI AIIRRILMAT SVLKVAAKVI
GEVQALIIFP AIPFAMLAIF YMFWISAALH LFSSGQVVQN NCNNTNCCAY DLVLKKVNCD
RCCGYSIHYT PHITIAIFFH LFGCYWATQF FIASSATVIA GSVASYYWAQ GEASPEIPFL
PVFASMKRLA RYNLGSVALG SLIVSFVESV RFILEAIRRK TKVSGTIPDH WFWRMAHYTS
RGCLKSVEWT IKSVNRNAYI MIAITGKSFC KSSAIATELI ISNILRIGKV NVIGDVILFL
GKLCVSLFSA LFGFLMLDSH RYRASHNKVS SPLLPVLACW ALGYIVATLF FAVVEMSIDT
IILSFCQDSE ENQGNAQHAP PLLLETLDSN QEEEVQSLTH


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