GORK_ARATH
ID GORK_ARATH Reviewed; 820 AA.
AC Q94A76; Q9FNY5;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Potassium channel GORK;
DE AltName: Full=Guard cell outward rectifying K(+) channel;
DE Short=AtGORK;
GN Name=GORK; OrderedLocusNames=At5g37500; ORFNames=MPA22.4;
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], TISSUE SPECIFICITY, AND CHARACTERIZATION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=11113445; DOI=10.1016/s0014-5793(00)02248-1;
RA Ache P., Becker D., Ivashikina N., Dietrich P., Roelfsema M.R.G.,
RA Hedrich R.;
RT "GORK, a delayed outward rectifier expressed in guard cells of Arabidopsis
RT thaliana, is a K(+)-selective, K(+)-sensing ion channel.";
RL FEBS Lett. 486:93-98(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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] OF 489-820.
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=11728473; DOI=10.1016/s0014-5793(01)03114-3;
RA Ivashikina N., Becker D., Ache P., Meyerhoff O., Felle H.H., Hedrich R.;
RT "K(+) channel profile and electrical properties of Arabidopsis root
RT hairs.";
RL FEBS Lett. 508:463-469(2001).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11500563; DOI=10.1104/pp.126.4.1646;
RA Maeser P., Thomine S., Schroeder J.I., Ward J.M., Hirschi K., Sze H.,
RA Talke I.N., Amtmann A., Maathuis F.J.M., Sanders D., Harper J.F.,
RA Tchieu J., Gribskov M., Persans M.W., Salt D.E., Kim S.A., Guerinot M.L.;
RT "Phylogenetic relationships within cation transporter families of
RT Arabidopsis.";
RL Plant Physiol. 126:1646-1667(2001).
RN [7]
RP CHARACTERIZATION, AND FUNCTION.
RX PubMed=12671068; DOI=10.1073/pnas.0733970100;
RA Hosy E., Vavasseur A., Mouline K., Dreyer I., Gaymard F., Poree F.,
RA Boucherez J., Lebaudy A., Bouchez D., Very A.-A., Simonneau T.,
RA Thibaud J.-B., Sentenac H.;
RT "The Arabidopsis outward K(+) channel GORK is involved in regulation of
RT stomatal movements and plant transpiration.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5549-5554(2003).
RN [8]
RP INDUCTION.
RX PubMed=14596925; DOI=10.1016/s0014-5793(03)01118-9;
RA Becker D., Hoth S., Ache P., Wenkel S., Roelfsema M.R.G., Meyerhoff O.,
RA Hartung W., Hedrich R.;
RT "Regulation of the ABA-sensitive Arabidopsis potassium channel gene GORK in
RT response to water stress.";
RL FEBS Lett. 554:119-126(2003).
CC -!- FUNCTION: Major selective outward-rectifying potassium channel of the
CC guard cell membrane. Involved in regulation of stomatal movements
CC according to the water status. Assuming opened or closed conformations
CC in response to the voltage difference across the membrane, the channel
CC is activated by depolarization. Conductance of the channel is modulated
CC in a potassium-dependent fashion. May interact with the cytoskeleton or
CC with regulatory proteins. {ECO:0000269|PubMed:12671068}.
CC -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC heterotetrameric complex of pore-forming subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in guard cell-containing tissues, in root
CC epidermal cells and in root hairs. Detected in vascular cells of the
CC root and shoot. {ECO:0000269|PubMed:11113445,
CC ECO:0000269|PubMed:11728473}.
CC -!- INDUCTION: Up-regulated under drought, salt stress and cold conditions.
CC Induced by abscisic acid (ABA) treatment in roots and shoots but not in
CC guard cells. {ECO:0000269|PubMed:14596925}.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids. The pore-
CC forming region H5 is enclosed by the transmembrane segments S5 and S6
CC in the Shaker-type (1P/6TM) and contains the GYGD signature motif which
CC seems to be involved in potassium selectivity.
CC -!- DOMAIN: The KHA domain (rich in hydrophobic and acidic residues)
CC present in the C-terminal part is likely to be important for
CC tetramerization.
CC -!- SIMILARITY: Belongs to the potassium channel family. Plant (TC 1.A.1.4)
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK83636.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ279009; CAC17380.1; -; mRNA.
DR EMBL; AB025630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED94198.1; -; Genomic_DNA.
DR EMBL; AY049294; AAK83636.1; ALT_INIT; mRNA.
DR EMBL; AY143848; AAN28787.1; -; mRNA.
DR RefSeq; NP_198566.2; NM_123109.5.
DR AlphaFoldDB; Q94A76; -.
DR SMR; Q94A76; -.
DR BioGRID; 18979; 3.
DR IntAct; Q94A76; 2.
DR STRING; 3702.AT5G37500.1; -.
DR TCDB; 1.A.1.4.4; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q94A76; -.
DR PaxDb; Q94A76; -.
DR PRIDE; Q94A76; -.
DR ProteomicsDB; 248447; -.
DR EnsemblPlants; AT5G37500.1; AT5G37500.1; AT5G37500.
DR GeneID; 833728; -.
DR Gramene; AT5G37500.1; AT5G37500.1; AT5G37500.
DR KEGG; ath:AT5G37500; -.
DR Araport; AT5G37500; -.
DR TAIR; locus:2169866; AT5G37500.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_005746_8_3_1; -.
DR InParanoid; Q94A76; -.
DR PhylomeDB; Q94A76; -.
DR PRO; PR:Q94A76; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94A76; baseline and differential.
DR Genevisible; Q94A76; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0015075; F:ion transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IMP:TAIR.
DR GO; GO:0006811; P:ion transport; IMP:TAIR.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0051592; P:response to calcium ion; IEP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.25.40.20; -; 2.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR045319; KAT/AKT.
DR InterPro; IPR021789; KHA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45743; PTHR45743; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF11834; KHA; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51490; KHA; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..820
FT /note="Potassium channel GORK"
FT /id="PRO_0000054129"
FT TOPO_DOM 1..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..168
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 260..279
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..820
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 528..559
FT /note="ANK 1"
FT REPEAT 563..592
FT /note="ANK 2"
FT REPEAT 596..625
FT /note="ANK 3"
FT REPEAT 627..656
FT /note="ANK 4"
FT REPEAT 660..689
FT /note="ANK 5"
FT REPEAT 693..722
FT /note="ANK 6"
FT DOMAIN 740..820
FT /note="KHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00823"
FT BINDING 386..508
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT CONFLICT 125
FT /note="T -> S (in Ref. 1; CAC17380)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="N -> Q (in Ref. 1; CAC17380)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="I -> V (in Ref. 1; CAC17380)"
FT /evidence="ECO:0000305"
FT CONFLICT 765
FT /note="I -> V (in Ref. 1; CAC17380)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 820 AA; 94461 MW; 65F57190056A9AE4 CRC64;
MGRLRRRQEI IDHEEEESND DVSSRRGKLS LAETFRWLDS SEHRRIETDG HNDYKYIIHP
KNRWYKAWEM FILVWAIYSS LFTPMEFGFF RGLPERLFVL DIVGQIAFLV DIVLQFFVAY
RDTQTYRTVY KPTRIAFRYL KSHFLMDFIG CFPWDLIYKA SGKHELVRYL LWIRLFRVRK
VVEFFQRLEK DTRINYLFTR ILKLLFVEVY CTHTAACIFY YLATTLPPEN EGYTWIGSLK
LGDYSYENFR EIDLWKRYTT ALYFAIVTMA TVGYGDIHAV NLREMIFVMI YVSFDMVLGA
YLIGNITALI VKGSNTERFR DKMNDLISFM NRKKLGRDLR SQITGHVRLQ YDSHYTDTVM
LQDIPASIRA KIAQLLYLPY IKKVPLFKGC STEFINQIVI RLHEEYFLPG EVITEQGNVV
DHLYFVCEGL LEALVTKTDG SEESVTLLGP HTSFGDISII CNISQPFTVR VCELCHLLRL
DKQSFSNILE IYFHDGRTIL NNIMEEKESN DRIKKLESDI VIHIGKQEAE LALKVNSAAF
QGDFYQLKSL IRSGADPNKT DYDGRSPLHL AACRGYEDIT LFLIQEGVDV NLKDKFGHTP
LFEAVKAGQE GVIGLLVKEG ASFNLEDSGN FLCTTVAKGD SDFLKRLLSS GMNPNSEDYD
HRTPLHVAAS EGLFLMAKML VEAGASVISK DRWGNSPLDE ARLCGNKKLI KLLEDVKNAQ
SSIYPSSLRE LQEERIERRK CTVFPFHPQE AKEERSRKHG VVVWIPSNLE KLIVTAAKEL
GLSDGASFVL LSEDQGRITD IDMISDGHKL YMISDTTDQT
