CLCG_ARATH
ID CLCG_ARATH Reviewed; 765 AA.
AC P60300; F4KH90;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Putative chloride channel-like protein CLC-g;
DE AltName: Full=CBS domain-containing protein CBSCLC6;
GN Name=CLC-G; Synonyms=CBSCLC6; OrderedLocusNames=At5g33280;
GN ORFNames=F19N02.1, T29A4.90;
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 [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 [2]
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 [3]
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 [4]
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: Putative 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 -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC {ECO:0000305}.
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DR EMBL; AC051625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93891.1; -; Genomic_DNA.
DR RefSeq; NP_198313.2; NM_122852.4.
DR AlphaFoldDB; P60300; -.
DR SMR; P60300; -.
DR BioGRID; 18558; 2.
DR IntAct; P60300; 1.
DR STRING; 3702.AT5G33280.1; -.
DR PaxDb; P60300; -.
DR PRIDE; P60300; -.
DR ProteomicsDB; 246713; -.
DR EnsemblPlants; AT5G33280.1; AT5G33280.1; AT5G33280.
DR GeneID; 833300; -.
DR Gramene; AT5G33280.1; AT5G33280.1; AT5G33280.
DR KEGG; ath:AT5G33280; -.
DR Araport; AT5G33280; -.
DR TAIR; locus:2183068; AT5G33280.
DR eggNOG; KOG0474; Eukaryota.
DR HOGENOM; CLU_003181_4_0_1; -.
DR InParanoid; P60300; -.
DR OMA; DYDVCEN; -.
DR OrthoDB; 410280at2759; -.
DR PRO; PR:P60300; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P60300; baseline and differential.
DR Genevisible; P60300; 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: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 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; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..765
FT /note="Putative chloride channel-like protein CLC-g"
FT /id="PRO_0000094471"
FT TRANSMEM 67..87
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TRANSMEM 715..735
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255"
FT DOMAIN 568..640
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 687..748
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96282"
SQ SEQUENCE 765 AA; 83858 MW; 2775DEC053469D54 CRC64;
MPNSTTEDSV AVPLLPSLRR ATNSTSQVAI VGANVCPIES LDYEIAENDF FKQDWRGRSK
VEIFQYVFMK WLLCFCIGII VSLIGFANNL AVENLAGVKF VVTSNMMIAG RFAMGFVVFS
VTNLILTLFA SVITAFVAPA AAGSGIPEVK AYLNGVDAPE IFSLRTLIIK IIGNISAVSA
SLLIGKAGPM VHTGACVASI LGQGGSKRYR LTWRWLRFFK NDRDRRDLVT CGAAAGIAAS
FRAPVGGVLF ALEEMSSWWR SALLWRIFFS TAVVAIVLRA LIDVCLSGKC GLFGKGGLIM
FDVYSENASY HLGDVLPVLL LGVVGGILGS LYNFLLDKVL RAYNYIYEKG VTWKILLACA
ISIFTSCLLF GLPFLASCQP CPVDALEECP TIGRSGNFKK YQCPPGHYND LASLIFNTND
DAIKNLFSKN TDFEFHYFSV LVFFVTCFFL SIFSYGIVAP AGLFVPVIVT GASYGRFVGM
LLGSNSNLNH GLFAVLGAAS FLGGTMRMTV STCVILLELT NNLLLLPMMM VVLLISKTVA
DGFNANIYNL IMKLKGFPYL YSHAEPYMRQ LLVGDVVTGP LQVFNGIEKV ETIVHVLKTT
NHNGFPVVDG PPLAAAPVLH GLILRAHILT LLKKRVFMPS PVACDSNTLS QFKAEEFAKK
GSGRSDKIED VELSEEELNM YLDLHPFSNA SPYTVVETMS LAKALILFRE VGIRHLLVIP
KTSNRPPVVG ILTRHDFMPE HILGLHPSVS RSKWKRLRIR LPFFS
