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CLCE_ARATH
ID   CLCE_ARATH              Reviewed;         710 AA.
AC   Q8GX93; O65486; Q93XN4; Q9SVX1;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   02-FEB-2004, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Chloride channel protein CLC-e;
DE            Short=AtCLC-e;
DE   AltName: Full=CBS domain-containing protein CBSCLC3;
GN   Name=CLC-E; Synonyms=CBSCLC3; OrderedLocusNames=At4g35440;
GN   ORFNames=F15J1.10, F23E12.10;
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].
RC   STRAIN=cv. Columbia; TISSUE=Aerial part;
RA   Vinauger-Douard M., Charon C., Lapous D., Allot M., Granier F., Bouchez D.,
RA   Barbier-Brygoo H., Ephritikhine G.;
RT   "Molecular and functional characterization of AtCLC-e, a new putative
RT   Arabidopsis anion channel.";
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
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   -!- 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=Q8GX93-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC42971.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA18726.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB54872.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80260.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF366367; AAK53390.1; -; mRNA.
DR   EMBL; AL022604; CAA18726.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL117188; CAB54872.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161587; CAB80260.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86510.1; -; Genomic_DNA.
DR   EMBL; AK118357; BAC42971.1; ALT_FRAME; mRNA.
DR   PIR; T17122; T17122.
DR   RefSeq; NP_567985.1; NM_119709.1. [Q8GX93-1]
DR   AlphaFoldDB; Q8GX93; -.
DR   SMR; Q8GX93; -.
DR   STRING; 3702.AT4G35440.2; -.
DR   TCDB; 2.A.49.6.3; the chloride carrier/channel (clc) family.
DR   PaxDb; Q8GX93; -.
DR   ProteomicsDB; 240976; -. [Q8GX93-1]
DR   EnsemblPlants; AT4G35440.1; AT4G35440.1; AT4G35440. [Q8GX93-1]
DR   GeneID; 829696; -.
DR   Gramene; AT4G35440.1; AT4G35440.1; AT4G35440. [Q8GX93-1]
DR   KEGG; ath:AT4G35440; -.
DR   Araport; AT4G35440; -.
DR   eggNOG; KOG0475; Eukaryota.
DR   HOGENOM; CLU_015263_3_0_1; -.
DR   InParanoid; Q8GX93; -.
DR   OMA; ECINIAC; -.
DR   PhylomeDB; Q8GX93; -.
DR   PRO; PR:Q8GX93; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8GX93; baseline and differential.
DR   Genevisible; Q8GX93; AT.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; 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   Pfam; PF00571; CBS; 1.
DR   Pfam; PF00654; Voltage_CLC; 1.
DR   PRINTS; PR00762; CLCHANNEL.
DR   SMART; SM00116; CBS; 2.
DR   SUPFAM; SSF54631; SSF54631; 1.
DR   SUPFAM; SSF81340; SSF81340; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   2: Evidence at transcript 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..710
FT                   /note="Chloride channel protein CLC-e"
FT                   /id="PRO_0000094469"
FT   TRANSMEM        74..94
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..281
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..316
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..360
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..399
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        412..432
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        451..471
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        472..492
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        667..687
FT                   /note="Helical; Name=13"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          565..624
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          640..702
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   REGION          500..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        297
FT                   /note="Missing (in Ref. 1; AAK53390)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        453
FT                   /note="Missing (in Ref. 1; AAK53390)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   710 AA;  75556 MW;  2C7B325F7BF112DE CRC64;
     MAATLPLCAA LRSPVSSRRF APIHKTDVPF QFNVVLSPFF GSVAIGGRIF PRLPAAKQET
     DQDEVGFDQQ PSQELAIASA CLVGVLTGVS VVLFNNCVHL LRDFSWDGIP DRGASWLREA
     PIGSNWLRVI LVPTIGGLVV SILNQLRESA GKSTGDSHSS LDRVKAVLRP FLKTVAACVT
     LGTGNSLGPE GPSVEIGASI AKGVNSLFNK SPQTGFSLLA AGSAAGISSG FNAAVAGCFF
     AVESVLWPSS STDSSTSLPN TTSMVILSAV TASVVSEIGL GSEPAFKVPD YDFRSPGELP
     LYLLLGALCG LVSLALSRCT SSMTSAVDSL NKDAGIPKAV FPVMGGLSVG IIALVYPEVL
     YWGFQNVDIL LEKRPFVKGL SADLLLQLVA VKIAATAWCR ASGLVGGYYA PSLFIGGAAG
     MAYGKFIGLA LAQNPDFNLS ILEVASPQAY GLVGMAATLA GVCQVPLTAV LLLFELTQDY
     RIVLPLLGAV GMSSWITSGQ SKRQETRETK ETRKRKSQEA VQSLTSSDDE SSTNNLCEVE
     SSLCLDDSLN QSEELPKSIF VSEAMRTRFA TVMMSTSLEE ALTRMLIEKQ SCALIVDPDN
     IFLGILTLSD IQEFSKARKE GNNRPKDIFV NDICSRSGGK CKVPWTVTPD MDLLAAQTIM
     NKHELSHVAV VSGSIDAPRI HPVGVLDREC ITLTRRALAT RMYLLNSLYL
 
 
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