CLCD_ARATH
ID CLCD_ARATH Reviewed; 792 AA.
AC P92943; O81491;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Chloride channel protein CLC-d;
DE Short=AtCLC-d;
DE AltName: Full=CBS domain-containing protein CBSCLC2;
GN Name=CLC-D; Synonyms=CBSCLC2; OrderedLocusNames=At5g26240;
GN ORFNames=F9D12.10, T19G15.90;
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], CHARACTERIZATION, AND MUTAGENESIS.
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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).
CC -!- FUNCTION: Voltage-gated chloride channel.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Broadly expressed in the plant, but predominantly
CC in the silique.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC26247.2; 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; Z71450; CAA96065.1; -; mRNA.
DR EMBL; AC005965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF077407; AAC26247.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93540.1; -; Genomic_DNA.
DR PIR; T01843; T01843.
DR RefSeq; NP_001330038.1; NM_001343969.1.
DR RefSeq; NP_197996.1; NM_122525.3.
DR AlphaFoldDB; P92943; -.
DR SMR; P92943; -.
DR BioGRID; 17968; 1.
DR STRING; 3702.AT5G26240.1; -.
DR iPTMnet; P92943; -.
DR PaxDb; P92943; -.
DR PRIDE; P92943; -.
DR ProteomicsDB; 246712; -.
DR EnsemblPlants; AT5G26240.1; AT5G26240.1; AT5G26240.
DR GeneID; 832693; -.
DR Gramene; AT5G26240.1; AT5G26240.1; AT5G26240.
DR KEGG; ath:AT5G26240; -.
DR Araport; AT5G26240; -.
DR TAIR; locus:2179724; AT5G26240.
DR eggNOG; KOG0474; Eukaryota.
DR HOGENOM; CLU_003181_4_0_1; -.
DR InParanoid; P92943; -.
DR OrthoDB; 410280at2759; -.
DR PhylomeDB; P92943; -.
DR PRO; PR:P92943; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P92943; baseline and differential.
DR Genevisible; P92943; 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:0005802; C:trans-Golgi network; IDA: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:0045824; P:negative regulation of innate immune response; IMP:TAIR.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0009826; P:unidimensional cell growth; 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; 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; 2.
PE 1: Evidence at protein level;
KW CBS domain; Chloride; Chloride channel; Ion channel; Ion transport;
KW Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW Transport; Voltage-gated channel.
FT CHAIN 1..792
FT /note="Chloride channel protein CLC-d"
FT /id="PRO_0000094468"
FT TRANSMEM 78..98
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..549
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TRANSMEM 731..751
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255"
FT DOMAIN 592..652
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 704..761
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT MUTAGEN 180
FT /note="I->R: Abolishes the activity."
FT /evidence="ECO:0000269|PubMed:8969232"
FT MUTAGEN 187
FT /note="L->R: Abolishes the activity."
FT /evidence="ECO:0000269|PubMed:8969232"
FT MUTAGEN 471
FT /note="P->L: Abolishes the activity."
FT /evidence="ECO:0000269|PubMed:8969232"
FT CONFLICT 775
FT /note="E -> D (in Ref. 1; CAA96065)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 792 AA; 87062 MW; 45B136A2A8CCE85A CRC64;
MLSNHLQNGI ESDNLLWSRV PESDDTSTDD ITLLNSHRDG DGGVNSLDYE VIENYAYREE
QAHRGKLYVG YYVAVKWFFS LLIGIGTGLA AVFINLSVEN FAGWKFALTF AIIQKSYFAG
FIVYLLINLV LVFSSAYIIT QFAPAAAGSG IPEIKGYLNG IDIPGTLLFR TLIGKIFGSI
GSVGGGLALG KEGPLVHTGA CIASLLGQGG STKYHLNSRW PQLFKSDRDR RDLVTCGCAA
GVAAAFRAPV GGVLFALEEV TSWWRSQLMW RVFFTSAIVA VVVRTAMGWC KSGICGHFGG
GGFIIWDVSD GQDDYYFKEL LPMAVIGVIG GLLGALFNQL TLYMTSWRRN SLHKKGNRVK
IIEACIISCI TSAISFGLPL LRKCSPCPES VPDSGIECPR PPGMYGNYVN FFCKTDNEYN
DLATIFFNTQ DDAIRNLFSA KTMREFSAQS LLTFLAMFYT LAVVTFGTAV PAGQFVPGIM
IGSTYGRLVG MFVVRFYKKL NIEEGTYALL GAASFLGGSM RMTVSLCVIM VEITNNLKLL
PLIMLVLLIS KAVGDAFNEG LYEVQARLKG IPLLESRPKY HMRQMIAKEA CQSQKVISLP
RVIRVADVAS ILGSNKHNGF PVIDHTRSGE TLVIGLVLRS HLLVLLQSKV DFQHSPLPCD
PSARNIRHSF SEFAKPVSSK GLCIEDIHLT SDDLEMYIDL APFLNPSPYV VPEDMSLTKV
YNLFRQLGLR HLFVVPRPSR VIGLITRKDL LIEENGESSA VELQQSTSVR GRYSETATRM
DAARPLLDDL LG
