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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.
23-MAY-2018, entry version 109.
RecName: Full=Choline transporter protein 1 {ECO:0000303|PubMed:25008948};
Short=AtCTL1 {ECO:0000303|PubMed:25008948};
AltName: Full=Protein SIGNIFICANT IONOME CHANGES 1 {ECO:0000303|PubMed:29284002};
Name=CHER1 {ECO:0000303|PubMed:25008948};
Synonyms=CTL1 {ECO:0000303|PubMed:25008948},
SIC1 {ECO:0000303|PubMed:29284002};
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;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[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).
[7]
FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-247, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=cv. Columbia;
PubMed=29284002; DOI=10.1371/journal.pbio.2002978;
Gao Y.-Q., Chen J.-G., Chen Z.-R., An D., Lv Q.-Y., Han M.-L.,
Wang Y.-L., Salt D.E., Chao D.-Y.;
"A new vesicle trafficking regulator CTL1 plays a crucial role in ion
homeostasis.";
PLoS Biol. 15:E2002978-E2002978(2017).
[8]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=29283991; DOI=10.1371/journal.pbio.2004310;
Wang Y., Yang L., Tang Y., Tang R., Jing Y., Zhang C., Zhang B.,
Li X., Cui Y., Zhang C., Shi J., Zhao F., Lan W., Luan S.;
"Arabidopsis choline transporter-like 1 (CTL1) regulates secretory
trafficking of auxin transporters to control seedling growth.";
PLoS Biol. 15:E2004310-E2004310(2017).
-!- FUNCTION: Regulator of vesicle trafficking, including endocytosis.
Necessary for secondary plasmodesmata (PD) formation and
development via the secretory trafficking regulation of proteins
required for PD development, thus influencing intercellular
communication (PubMed:27743414, PubMed:29284002). Modulates ion
homeostasis, especially in roots, by monitoring the transport and
subsequent subcellular localization of some ion transporters
(PubMed:29284002). Choline transporter involved in the regulation
of choline metabolite homeostasis during root and phloem
development (PubMed:25008948). Modulates phloem morphogenesis and
conductivity (PubMed:25008948). 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). Involved in the regulation of intracellular
trafficking of PIN-type auxin transporters (e.g. PIN1 and PIN3), a
process controlling seedling growth, apical dominance, cell
elongation and apical hook development. Modulates also membrane
lipids (e.g. phospholipids and sphingolipids) homeostasis
(PubMed:29283991). {ECO:0000269|PubMed:25008948,
ECO:0000269|PubMed:27743414, ECO:0000269|PubMed:29283991,
ECO:0000269|PubMed:29284002}.
-!- FUNCTION: (Microbial infection) Required for PD localization of
MP17, the luteoviral movement protein.
{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,
ECO:0000269|PubMed:29283991}; Multi-pass membrane protein
{ECO:0000255}. Cytoplasm, cytoskeleton, phragmoplast
{ECO:0000269|PubMed:25008948}. Prevacuolar compartment membrane
{ECO:0000269|PubMed:29283991}; Multi-pass membrane protein
{ECO:0000255}. Cell membrane {ECO:0000269|PubMed:29283991}; Multi-
pass membrane protein {ECO:0000255}. Note=Associated transiently
with the phragmoplast during cytokinesis. Follows a polar
localization in the forming sieve plates.
{ECO:0000269|PubMed:25008948}.
-!- TISSUE SPECIFICITY: Expressed in both roots and shoots.
{ECO:0000269|PubMed:29283991, ECO:0000269|PubMed:29284002}.
-!- DEVELOPMENTAL STAGE: In roots, observed in all cells of the root
tip, inculding both meristem and elongation zones, but restricted
to vascular tissues of the maturation zone (PubMed:29284002,
PubMed:29283991). Also observed in shoot apical meristems, lateral
root primordia and the vascular system. Under dark conditions,
present in the concave side of the apical hook (PubMed:29283991).
{ECO:0000269|PubMed:29283991, ECO:0000269|PubMed:29284002}.
-!- DISRUPTION PHENOTYPE: Impaired plasmodesmata (PD) mediated cell-
to-cell communication (PubMed:29284002). 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). Altered ion
profile due to both PD defects and ion transporter misregulation.
Increased leaf concentrations of sodium (Na), lithium (Li), boron
(B) ions, and decreased leaf concentrations of phosphorus (P),
potassium (K), calcium (Ca), cobalt (Co), nickel (Ni), and copper
(Cu), manganese (Mn), iron (Fe), zinc (Zn) and molybdenum (Mo)
ions. Defects in leaf and root elongation as well as fewer leaves
are also observed, associated with irregular cell organization in
roots, probably as a result of irregular cell division
(PubMed:29284002). Impaired intracellular trafficking of PIN-type
auxin transporters (e.g. PIN1 and PIN3) to the plasma membrane,
resulting in abnormal seedling growth, lack of apical dominance,
cell elongation defect and apical hook development. Perturbated
membrane lipids (e.g. phospholipids and sphingolipids)
homeostasis. Reduced sensitivity to auxin (e.g. 1-naphthylacetic
acid, NAA) (PubMed:29283991). {ECO:0000269|PubMed:25008948,
ECO:0000269|PubMed:27743414, ECO:0000269|PubMed:29283991,
ECO:0000269|PubMed:29284002}.
-!- 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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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
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; -.
SwissPalm; Q94AN2; -.
PaxDb; Q94AN2; -.
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; QTWMAFM; -.
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-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:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0009524; C:phragmoplast; IDA:TAIR.
GO; GO:0009705; C:plant-type vacuole membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0050801; P:ion homeostasis; IMP:UniProtKB.
GO; GO:0048366; P:leaf development; IMP:UniProtKB.
GO; GO:0055088; P:lipid homeostasis; IMP:UniProtKB.
GO; GO:0010088; P:phloem development; IMP:TAIR.
GO; GO:0009663; P:plasmodesma organization; IMP:UniProtKB.
GO; GO:0010497; P:plasmodesmata-mediated intercellular transport; IMP:UniProtKB.
GO; GO:0010067; P:procambium histogenesis; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; IMP:UniProtKB.
GO; GO:2000012; P:regulation of auxin polar transport; IMP:UniProtKB.
GO; GO:0030100; P:regulation of endocytosis; IMP:UniProtKB.
GO; GO:0051510; P:regulation of unidimensional cell growth; IMP:UniProtKB.
GO; GO:0048364; P:root development; IMP:UniProtKB.
GO; GO:0090603; P:sieve element differentiation; IMP:TAIR.
GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
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;
Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton;
Developmental protein; Endocytosis; Endosome; Glycoprotein;
Golgi apparatus; Membrane; Protein transport; 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 and sic1; impaired
secondary plasmodesmata (PD) formation
(e.g. blocked or shrunken) and
development leading to starch and soluble
sugars excess accumulation, abnormal
cell-to-cell communication, and stunted
growth. Altered PD localization of the
luteoviral movement protein MP17.
Abnormal subcellular localization.
Increased leaf concentrations of sodium
(Na), lithium (Li), boron (B) ions, and
decreased leaf concentrations of
phosphorus (P), potassium (K), calcium
(Ca), cobalt (Co), nickel (Ni), and
copper (Cu), manganese (Mn), iron (Fe),
zinc (Zn) and molybdenum (Mo) ions.
{ECO:0000269|PubMed:27743414,
ECO:0000269|PubMed:29284002}.
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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