CLCA_ARATH
ID CLCA_ARATH Reviewed; 775 AA.
AC P92941; O64990; Q93YS0;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Chloride channel protein CLC-a;
DE Short=AtCLC-a;
DE AltName: Full=CBS domain-containing protein CBSCLC5;
GN Name=CLC-A; Synonyms=CBSCLC5; OrderedLocusNames=At5g40890;
GN ORFNames=MHK7.12;
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], FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=10758477; DOI=10.1046/j.1365-313x.2000.00680.x;
RA Geelen D., Lurin C., Bouchez D., Frachisse J.-M., Lelievre F., Courtial B.,
RA Barbier-Brygoo H., Maurel C.;
RT "Disruption of putative anion channel gene AtCLC-a in Arabidopsis suggests
RT a role in the regulation of nitrate content.";
RL Plant J. 21:259-267(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 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 [8]
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 that could play a role in the
CC regulation of nitrate content. {ECO:0000269|PubMed:10758477}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P92941-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Broadly expressed in the plant.
CC -!- INDUCTION: In shoots and roots by nitrate treatment.
CC {ECO:0000269|PubMed:10758477}.
CC -!- DISRUPTION PHENOTYPE: Loss-of-function mutation clca-1 leads to an
CC altered nitrate content and hypersensitivity to chlorate.
CC {ECO:0000269|PubMed:10758477}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC {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; Z71445; CAA96057.1; -; mRNA.
DR EMBL; AF044313; AAC05742.1; -; mRNA.
DR EMBL; AB011477; BAB11351.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94612.1; -; Genomic_DNA.
DR EMBL; AY059791; AAL24139.1; -; mRNA.
DR EMBL; AY150506; AAN13022.1; -; mRNA.
DR PIR; T52107; T52107.
DR RefSeq; NP_198905.1; NM_123454.3. [P92941-1]
DR AlphaFoldDB; P92941; -.
DR SMR; P92941; -.
DR BioGRID; 19341; 5.
DR IntAct; P92941; 5.
DR STRING; 3702.AT5G40890.1; -.
DR iPTMnet; P92941; -.
DR PaxDb; P92941; -.
DR PRIDE; P92941; -.
DR ProteomicsDB; 246817; -. [P92941-1]
DR EnsemblPlants; AT5G40890.1; AT5G40890.1; AT5G40890. [P92941-1]
DR GeneID; 834090; -.
DR Gramene; AT5G40890.1; AT5G40890.1; AT5G40890. [P92941-1]
DR KEGG; ath:AT5G40890; -.
DR Araport; AT5G40890; -.
DR TAIR; locus:2164466; AT5G40890.
DR eggNOG; KOG0474; Eukaryota.
DR InParanoid; P92941; -.
DR OrthoDB; 410280at2759; -.
DR PhylomeDB; P92941; -.
DR PRO; PR:P92941; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P92941; baseline and differential.
DR Genevisible; P92941; 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:0009705; C:plant-type vacuole membrane; IBA:GO_Central.
DR GO; GO:0015112; F:nitrate transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0009671; F:nitrate:proton symporter activity; IBA:GO_Central.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR GO; GO:0006821; P:chloride transport; IDA:TAIR.
DR GO; GO:0015706; P:nitrate transmembrane transport; IDA:TAIR.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0010167; P:response to nitrate; IMP:TAIR.
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; 2.
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; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; CBS domain; Chloride; Chloride channel; Ion channel;
KW Ion transport; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..775
FT /note="Chloride channel protein CLC-a"
FT /id="PRO_0000094465"
FT TRANSMEM 88..108
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TRANSMEM 730..750
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255"
FT DOMAIN 595..658
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 703..768
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 330
FT /note="D -> H (in Ref. 1; CAA96057)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="Q -> L (in Ref. 5; AAL24139)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 775 AA; 85406 MW; A352FB24583E714E CRC64;
MDEDGNLQIS NSNYNGEEEG EDPENNTLNQ PLLKRHRTLS STPLALVGAK VSHIESLDYE
INENDLFKHD WRSRSKAQVF QYIFLKWTLA CLVGLFTGLI ATLINLAVEN IAGYKLLAVG
YYIAQDRFWT GLMVFTGANL GLTLVATVLV VYFAPTAAGP GIPEIKAYLN GIDTPNMFGF
TTMMVKIVGS IGAVAAGLDL GKEGPLVHIG SCIASLLGQG GPDNHRIKWR WLRYFNNDRD
RRDLITCGSA SGVCAAFRSP VGGVLFALEE VATWWRSALL WRTFFSTAVV VVVLRAFIEI
CNSGKCGLFG SGGLIMFDVS HVEVRYHAAD IIPVTLIGVF GGILGSLYNH LLHKVLRLYN
LINQKGKIHK VLLSLGVSLF TSVCLFGLPF LAECKPCDPS IDEICPTNGR SGNFKQFNCP
NGYYNDLSTL LLTTNDDAVR NIFSSNTPNE FGMVSLWIFF GLYCILGLIT FGIATPSGLF
LPIILMGSAY GRMLGTAMGS YTNIDQGLYA VLGAASLMAG SMRMTVSLCV IFLELTNNLL
LLPITMFVLL IAKTVGDSFN LSIYEIILHL KGLPFLEANP EPWMRNLTVG ELNDAKPPVV
TLNGVEKVAN IVDVLRNTTH NAFPVLDGAD QNTGTELHGL ILRAHLVKVL KKRWFLNEKR
RTEEWEVREK FTPVELAERE DNFDDVAITS SEMQLYVDLH PLTNTTPYTV VQSMSVAKAL
VLFRSVGLRH LLVVPKIQAS GMSPVIGILT RQDLRAYNIL QAFPHLDKHK SGKAR
