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 27-MAR-2024, entry version 160.
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}.
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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 PDB; 7XA9; EM; 2.84 A; A/B=1-775.
DR PDB; 8IAB; EM; 2.96 A; A/B=1-775.
DR PDB; 8IAD; EM; 3.16 A; A/B=1-775.
DR PDBsum; 7XA9; -.
DR PDBsum; 8IAB; -.
DR PDBsum; 8IAD; -.
DR AlphaFoldDB; P92941; -.
DR EMDB; EMD-35299; -.
DR EMDB; EMD-35300; -.
DR SMR; P92941; -.
DR BioGRID; 19341; 5.
DR IntAct; P92941; 5.
DR STRING; 3702.P92941; -.
DR iPTMnet; P92941; -.
DR PaxDb; 3702-AT5G40890-1; -.
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; AT5G40890; CLC-A.
DR eggNOG; KOG0474; Eukaryota.
DR InParanoid; P92941; -.
DR OrthoDB; 315083at2759; -.
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:0015112; F:nitrate transmembrane transporter activity; IDA:TAIR.
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:0010167; P:response to nitrate; IMP:TAIR.
DR CDD; cd04591; CBS_pair_voltage-gated_CLC_euk_bac; 1.
DR CDD; cd03685; ClC_6_like; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 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 PANTHER; PTHR11689; CHLORIDE CHANNEL PROTEIN CLC FAMILY MEMBER; 1.
DR PANTHER; PTHR11689:SF67; CHLORIDE CHANNEL PROTEIN CLC-A; 1.
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; CBS-domain pair; 1.
DR SUPFAM; SSF81340; Clc chloride channel; 1.
DR PROSITE; PS51371; CBS; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; CBS domain; Chloride; Chloride channel;
KW Ion channel; Ion transport; Membrane; Reference proteome; Repeat;
KW Transmembrane; 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"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:8IAB"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:8IAB"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 76..123
FT /evidence="ECO:0007829|PDB:8IAB"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 128..153
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:8IAB"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 180..194
FT /evidence="ECO:0007829|PDB:8IAB"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 203..219
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 238..257
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 262..269
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 277..300
FT /evidence="ECO:0007829|PDB:8IAB"
FT TURN 301..306
FT /evidence="ECO:0007829|PDB:8IAB"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:8IAD"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:8IAD"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 331..363
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 367..387
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:8IAB"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:8IAB"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:8IAD"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:8IAD"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:8IAD"
FT STRAND 421..427
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 435..442
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 453..470
FT /evidence="ECO:0007829|PDB:8IAB"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 480..498
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 506..522
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 526..536
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 539..541
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 542..557
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 563..570
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 582..585
FT /evidence="ECO:0007829|PDB:8IAB"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 589..592
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 593..595
FT /evidence="ECO:0007829|PDB:8IAB"
FT STRAND 602..607
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 608..617
FT /evidence="ECO:0007829|PDB:8IAB"
FT STRAND 621..626
FT /evidence="ECO:0007829|PDB:8IAB"
FT STRAND 639..642
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 643..652
FT /evidence="ECO:0007829|PDB:8IAB"
FT STRAND 656..659
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 664..670
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 673..677
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 683..685
FT /evidence="ECO:0007829|PDB:8IAB"
FT TURN 690..694
FT /evidence="ECO:0007829|PDB:8IAB"
FT STRAND 695..698
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 700..702
FT /evidence="ECO:0007829|PDB:8IAB"
FT STRAND 703..705
FT /evidence="ECO:0007829|PDB:8IAB"
FT STRAND 709..711
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 716..726
FT /evidence="ECO:0007829|PDB:8IAB"
FT STRAND 731..734
FT /evidence="ECO:0007829|PDB:8IAB"
FT STRAND 747..749
FT /evidence="ECO:0007829|PDB:8IAB"
FT TURN 751..754
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 756..762
FT /evidence="ECO:0007829|PDB:8IAB"
FT HELIX 764..766
FT /evidence="ECO:0007829|PDB:8IAB"
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
//
