CCC1_ARATH
ID CCC1_ARATH Reviewed; 975 AA.
AC Q2UVJ5; Q9S9Q8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Cation-chloride cotransporter 1;
DE Short=AtCCC1;
DE AltName: Full=Protein HAPLESS 5;
GN Name=CCC1; Synonyms=HAP5; OrderedLocusNames=At1g30450; ORFNames=F26G16.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=17355435; DOI=10.1111/j.1365-313x.2007.03048.x;
RA Colmenero-Flores J.M., Martinez G., Gamba G., Vazquez N., Iglesias D.J.,
RA Brumos J., Talon M.;
RT "Identification and functional characterization of cation-chloride
RT cotransporters in plants.";
RL Plant J. 50:278-292(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=15514068; DOI=10.1534/genetics.104.029447;
RA Johnson M.A., von Besser K., Zhou Q., Smith E., Aux G., Patton D.,
RA Levin J.Z., Preuss D.;
RT "Arabidopsis hapless mutations define essential gametophytic functions.";
RL Genetics 168:971-982(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Cation/chloride cotransporter that mediates potassium-
CC chloride and sodium-chloride cotransports. Involved in plant
CC development and Cl(-) homeostasis. May be involved in long distance
CC Cl(-) transport. Does not function as an H(+)-dependent cotransporter.
CC {ECO:0000269|PubMed:17355435}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in young seedlings cotyledon tips, plant
CC vasculature, root tips and axillary buds. Expressed in root vascular
CC strand in the pericycle and other parenchyma cells bordering xylem
CC vessels. Expressed in the xylem/symplast boundaries of rosette stems,
CC rosette leaves and cauline leaves. Expressed in stipules, trichomes and
CC hydathodes. Expressed in pollen grains. {ECO:0000269|PubMed:17355435}.
CC -!- DISRUPTION PHENOTYPE: Bushy plants with small leaves, short roots and
CC short inflorescences containing a higher number of stems. Alteration in
CC pollen grain development, high number of aborted siliques and few
CC siliques with low number of seeds. {ECO:0000269|PubMed:15514068,
CC ECO:0000269|PubMed:17355435}.
CC -!- MISCELLANEOUS: Cotransport is inhibited by the loop diuretic
CC bumetanide.
CC -!- SIMILARITY: Belongs to the SLC12A transporter family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19744.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM113986; CAJ34849.1; -; mRNA.
DR EMBL; AC009917; AAF19744.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31217.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31218.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31219.1; -; Genomic_DNA.
DR EMBL; AK226602; BAE98715.1; -; mRNA.
DR PIR; H86428; H86428.
DR RefSeq; NP_174333.2; NM_102781.3.
DR RefSeq; NP_849731.1; NM_179400.1.
DR RefSeq; NP_849732.1; NM_179401.2.
DR AlphaFoldDB; Q2UVJ5; -.
DR SMR; Q2UVJ5; -.
DR STRING; 3702.AT1G30450.2; -.
DR iPTMnet; Q2UVJ5; -.
DR PaxDb; Q2UVJ5; -.
DR PRIDE; Q2UVJ5; -.
DR ProteomicsDB; 223959; -.
DR EnsemblPlants; AT1G30450.1; AT1G30450.1; AT1G30450.
DR EnsemblPlants; AT1G30450.2; AT1G30450.2; AT1G30450.
DR EnsemblPlants; AT1G30450.3; AT1G30450.3; AT1G30450.
DR GeneID; 839924; -.
DR Gramene; AT1G30450.1; AT1G30450.1; AT1G30450.
DR Gramene; AT1G30450.2; AT1G30450.2; AT1G30450.
DR Gramene; AT1G30450.3; AT1G30450.3; AT1G30450.
DR KEGG; ath:AT1G30450; -.
DR Araport; AT1G30450; -.
DR TAIR; locus:2028170; AT1G30450.
DR eggNOG; KOG2082; Eukaryota.
DR HOGENOM; CLU_001883_1_2_1; -.
DR InParanoid; Q2UVJ5; -.
DR OrthoDB; 349744at2759; -.
DR PhylomeDB; Q2UVJ5; -.
DR PRO; PR:Q2UVJ5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q2UVJ5; baseline and differential.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IBA:GO_Central.
DR GO; GO:0008511; F:sodium:potassium:chloride symporter activity; IDA:TAIR.
DR GO; GO:0006884; P:cell volume homeostasis; IBA:GO_Central.
DR GO; GO:0055064; P:chloride ion homeostasis; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0055075; P:potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR018491; SLC12_C.
DR InterPro; IPR004842; SLC12A_fam.
DR PANTHER; PTHR11827; PTHR11827; 1.
DR Pfam; PF00324; AA_permease; 1.
DR Pfam; PF03522; SLC12; 2.
DR TIGRFAMs; TIGR00930; 2a30; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Ion transport; Membrane; Potassium; Potassium transport;
KW Reference proteome; Sodium; Sodium transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..975
FT /note="Cation-chloride cotransporter 1"
FT /id="PRO_0000410466"
FT TOPO_DOM 1..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..359
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..434
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..515
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..544
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 566..571
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 593..975
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 975 AA; 106648 MW; DA1AFD63FADC535C CRC64;
MDSGDIEEAG GNGEEEFRSG PRLGGSKYRP VVAHDRAVVE MSSIDPGSSS STLKNIKVVA
PGDVGAGVRG PEDGVNGHQK ESKLELFGFD SLVNILGLKS MTGEQIQAPS SPRDGEDISI
TQGHPKPPAL KMGTMMGVFV PCLQNILGII YYIRFTWIVG MAGIGQGLVL VFLCGLCTFL
TTISLSAIAT NGAMKGGGPY YLIGRALGPE VGISIGLCFF LGNAVAGALY VLGAVETFLK
AFPAAGIFRE TITKVNGTAV SESIQSPNSH DLQVYGIVVT ILLCFIVFGG VKMINRVAPA
FLVPVLLSIF CIFIGIFLAK TDDPDNGITG LRLKSFKDNW GSAYQMTNDA GIPDPTGGTY
WSFNELVGLF FPAVTGIMAG SNRSASLKDT QKSIPVGTLA ATLTTTSLYL ISVLFFGAVA
TRDKLLTDRL LTATIAWPFP AIVHVGIILS TLGAALQSLT GAPRLLAAIA NDDILPILNY
FKVADTSEPH IATLFTAFIC IGCVVIGNLD LITPTVTMFY LLCYSGVNLS CFLLDLLDAP
SWRPRWKYHH WSLSFVGASL CIVIMFLISW SFTVVAIALA SLIYKYVGLK GKAGDWGDGF
KSAYFQLALR SLRSLGANQV HPKNWYPIPL VFCRPWGQLP ENVPCHPKLA DFANCMKKKG
RGMSIFVSIL DGDYYECAEE AKEACKQLAT YIEYKRCEGV AEIVVAPNMT EGFRGIIQTM
GLGNLKPNIV VMRYPEIWRR ENLTEIPSTF VGIINDCITA NKAVVIIKGL DEWPNEYQRQ
YGTIDLYWIV RDGGLMLLLS QLLLTKESFE SCKIQLFCIA EEDSDAEALK ADVKKFLYDL
RMHAEVIVVT MKSWDIRSEG NSQEDSLEAF DAAQRRISDY LGEIKRQGSN PLLANGKPMV
VNEQQVEKFL YTMLKLNSTI LSYSRMAAVV LVSLPPPPLN HPAYFYMEYM DLLVENVPRM
LIVRGYHRDV VTLFT
