CLCC_ARATH
ID CLCC_ARATH Reviewed; 779 AA.
AC Q96282; O04753; O04837;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 154.
DE RecName: Full=Chloride channel protein CLC-c;
DE Short=AtCLC-c;
DE AltName: Full=CBS domain-containing protein CBSCLC4;
GN Name=CLC-C; Synonyms=CBSCLC4; OrderedLocusNames=At5g49890; ORFNames=K9P8.3;
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], AND CHARACTERIZATION.
RC STRAIN=cv. Columbia;
RX PubMed=8969232; DOI=10.1074/jbc.271.52.33632;
RA Hechenberger M., Schwappach B., Fischer W.N., Frommer W.B., Jentsch T.J.,
RA Steinmeyer K.;
RT "A family of putative chloride channels from Arabidopsis and functional
RT complementation of a yeast strain with a CLC gene disruption.";
RL J. Biol. Chem. 271:33632-33638(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. C24;
RA Weigmann N., Zimmermann S., Mueller-Roeber B.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19400948; DOI=10.1186/1471-2164-10-200;
RA Kushwaha H.R., Singh A.K., Sopory S.K., Singla-Pareek S.L., Pareek A.;
RT "Genome wide expression analysis of CBS domain containing proteins in
RT Arabidopsis thaliana (L.) Heynh and Oryza sativa L. reveals their
RT developmental and stress regulation.";
RL BMC Genomics 10:200-200(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-672, AND
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-672, AND
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).
RN [9]
RP INTERACTION WITH PP2A5.
RX PubMed=27676158; DOI=10.1111/pce.12837;
RA Hu R., Zhu Y., Wei J., Chen J., Shi H., Shen G., Zhang H.;
RT "Overexpression of PP2A-C5 that encodes the catalytic subunit 5 of protein
RT phosphatase 2A in Arabidopsis confers better root and shoot development
RT under salt conditions.";
RL Plant Cell Environ. 40:150-164(2017).
CC -!- FUNCTION: Voltage-gated chloride channel.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with PP2A5
CC (PubMed:27676158). {ECO:0000250, ECO:0000269|PubMed:27676158}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Broadly expressed in the plant.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC {ECO:0000305}.
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DR EMBL; Z71447; CAA96059.1; -; mRNA.
DR EMBL; Y09095; CAA70310.1; -; mRNA.
DR EMBL; AB024032; BAA97010.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95868.1; -; Genomic_DNA.
DR EMBL; AY120754; AAM53312.1; -; mRNA.
DR EMBL; BT001211; AAN65098.1; -; mRNA.
DR RefSeq; NP_199800.1; NM_124367.4.
DR AlphaFoldDB; Q96282; -.
DR SMR; Q96282; -.
DR BioGRID; 20298; 8.
DR IntAct; Q96282; 8.
DR STRING; 3702.AT5G49890.1; -.
DR iPTMnet; Q96282; -.
DR PaxDb; Q96282; -.
DR PRIDE; Q96282; -.
DR ProteomicsDB; 246820; -.
DR EnsemblPlants; AT5G49890.1; AT5G49890.1; AT5G49890.
DR GeneID; 835052; -.
DR Gramene; AT5G49890.1; AT5G49890.1; AT5G49890.
DR KEGG; ath:AT5G49890; -.
DR Araport; AT5G49890; -.
DR TAIR; locus:2158809; AT5G49890.
DR eggNOG; KOG0474; Eukaryota.
DR HOGENOM; CLU_003181_4_0_1; -.
DR InParanoid; Q96282; -.
DR OMA; FMHEHIS; -.
DR OrthoDB; 410280at2759; -.
DR PhylomeDB; Q96282; -.
DR PRO; PR:Q96282; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q96282; baseline and differential.
DR Genevisible; Q96282; AT.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 3.10.580.10; -; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR InterPro; IPR002251; Cl_channel_pln.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR PRINTS; PR01120; CLCHANNELPLT.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF81340; SSF81340; 1.
DR PROSITE; PS51371; CBS; 1.
PE 1: Evidence at protein level;
KW CBS domain; Chloride; Chloride channel; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..779
FT /note="Chloride channel protein CLC-c"
FT /id="PRO_0000094467"
FT TRANSMEM 92..112
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..561
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TRANSMEM 741..761
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255"
FT DOMAIN 601..659
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 713..777
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
SQ SEQUENCE 779 AA; 85232 MW; 1717716DB1EE5867 CRC64;
MDDRHEGDHH DIEVEGGALH GFERKISGIL DDGSVGFRQP LLARNRKNTT SQIAIVGANT
CPIESLDYEI FENDFFKQDW RSRKKIEILQ YTFLKWALAF LIGLATGLVG FLNNLGVENI
AGFKLLLIGN LMLKEKYFQA FFAFAGCNLI LATAAASLCA FIAPAAAGSG IPEVKAYLNG
IDAYSILAPS TLFVKIFGSI FGVAAGFVVG KEGPMVHTGA CIANLLGQGG SKKYRLTWKW
LRFFKNDRDR RDLITCGAAA GVAAAFRAPV GGVLFALEEA ASWWRNALLW RTFFTTAVVA
VVLRSLIEFC RSGRCGLFGK GGLIMFDVNS GPVLYSTPDL LAIVFLGVIG GVLGSLYNYL
VDKVLRTYSI INEKGPRFKI MLVMAVSILS SCCAFGLPWL SQCTPCPIGI EEGKCPSVGR
SSIYKSFQCP PNHYNDLSSL LLNTNDDAIR NLFTSRSENE FHISTLAIFF VAVYCLGIIT
YGIAIPSGLF IPVILAGASY GRLVGRLLGP VSQLDVGLFS LLGAASFLGG TMRMTVSLCV
ILLELTNNLL MLPLVMLVLL ISKTVADCFN RGVYDQIVTM KGLPYMEDHA EPYMRNLVAK
DVVSGALISF SRVEKVGVIW QALKMTRHNG FPVIDEPPFT EASELCGIAL RSHLLVLLQG
KKFSKQRTTF GSQILRSCKA RDFGKAGLGK GLKIEDLDLS EEEMEMYVDL HPITNTSPYT
VLETLSLAKA AILFRQLGLR HLCVVPKTPG RPPIVGILTR HDFMPEHVLG LYPHIDPLK
