SKOR_ARATH
ID SKOR_ARATH Reviewed; 828 AA.
AC Q9M8S6; O82630; Q9SB86;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Potassium channel SKOR;
DE AltName: Full=Stelar K(+) outward rectifying channel;
GN Name=SKOR; OrderedLocusNames=At3g02850; ORFNames=F13E7.21;
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 [GENOMIC DNA / MRNA], TISSUE SPECIFICITY,
RP CHARACTERIZATION, AND FUNCTION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9741629; DOI=10.1016/s0092-8674(00)81606-2;
RA Gaymard F., Pilot G., Lacombe B., Bouchez D., Bruneau D., Boucherez J.,
RA Michaux-Ferriere N., Thibaud J.-B., Sentenac H.;
RT "Identification and disruption of a plant shaker-like outward channel
RT involved in K+ release into the xylem sap.";
RL Cell 94:647-655(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 PROTON SENSITIVITY.
RX PubMed=10682858; DOI=10.1016/s0014-5793(00)01093-0;
RA Lacombe B., Pilot G., Gaymard F., Sentenac H., Thibaud J.-B.;
RT "pH control of the plant outwardly-rectifying potassium channel SKOR.";
RL FEBS Lett. 466:351-354(2000).
RN [5]
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 [6]
RP INDUCTION.
RX PubMed=12678562; DOI=10.1023/a:1022597102282;
RA Pilot G., Gaymard F., Mouline K., Cherel I., Sentenac H.;
RT "Regulated expression of Arabidopsis shaker K(+) channel genes involved in
RT K(+) uptake and distribution in the plant.";
RL Plant Mol. Biol. 51:773-787(2003).
CC -!- FUNCTION: Highly selective outward-rectifying potassium channel.
CC Involved in potassium release into the xylem sap toward the shoots.
CC Assuming opened or closed conformations in response to the voltage
CC difference across the membrane, the channel is activated by
CC depolarization. The voltage-dependence of the channel is abolished by
CC internal or external acidification. May interact with the cytoskeleton
CC or with regulatory proteins. {ECO:0000269|PubMed:9741629}.
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 root pericycle and xylem parenchyma,
CC and in flower at a lower level. {ECO:0000269|PubMed:9741629}.
CC -!- INDUCTION: In roots, strongly inhibited by 2,4-dichlorophenoxyacetic
CC acid (2,4-D), abscisic acid (ABA) and benzyladenine (BA) treatment or
CC by potassium starvation. {ECO:0000269|PubMed:12678562}.
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 -!- MISCELLANEOUS: Loss-of-function mutation skor-1 leads to a reduced
CC shoot potassium content.
CC -!- SIMILARITY: Belongs to the potassium channel family. Plant (TC 1.A.1.4)
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ223357; CAA11280.1; -; Genomic_DNA.
DR EMBL; AJ223358; CAA11281.1; -; mRNA.
DR EMBL; AC018363; AAF26975.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73866.1; -; Genomic_DNA.
DR PIR; T52046; T52046.
DR RefSeq; NP_186934.1; NM_111153.4.
DR AlphaFoldDB; Q9M8S6; -.
DR SMR; Q9M8S6; -.
DR BioGRID; 6385; 2.
DR IntAct; Q9M8S6; 1.
DR STRING; 3702.AT3G02850.1; -.
DR TCDB; 1.A.1.4.5; the voltage-gated ion channel (vic) superfamily.
DR PaxDb; Q9M8S6; -.
DR PRIDE; Q9M8S6; -.
DR ProteomicsDB; 232637; -.
DR EnsemblPlants; AT3G02850.1; AT3G02850.1; AT3G02850.
DR GeneID; 821052; -.
DR Gramene; AT3G02850.1; AT3G02850.1; AT3G02850.
DR KEGG; ath:AT3G02850; -.
DR Araport; AT3G02850; -.
DR TAIR; locus:2075442; AT3G02850.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_005746_8_3_1; -.
DR InParanoid; Q9M8S6; -.
DR OrthoDB; 160363at2759; -.
DR PhylomeDB; Q9M8S6; -.
DR BioCyc; ARA:AT3G02850-MON; -.
DR BioCyc; MetaCyc:MON-14560; -.
DR PRO; PR:Q9M8S6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M8S6; baseline and differential.
DR Genevisible; Q9M8S6; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IDA:TAIR.
DR GO; GO:0055075; P:potassium ion homeostasis; IMP:TAIR.
DR GO; GO:0006813; P:potassium ion transport; IDA:TAIR.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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; PR01415; ANKYRIN.
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..828
FT /note="Potassium channel SKOR"
FT /id="PRO_0000054128"
FT TOPO_DOM 1..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..114
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..185
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 277..296
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..300
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..828
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 545..576
FT /note="ANK 1"
FT REPEAT 580..609
FT /note="ANK 2"
FT REPEAT 613..642
FT /note="ANK 3"
FT REPEAT 644..673
FT /note="ANK 4"
FT REPEAT 677..706
FT /note="ANK 5"
FT REPEAT 710..740
FT /note="ANK 6"
FT DOMAIN 756..828
FT /note="KHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00823"
FT BINDING 403..523
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT CONFLICT 16
FT /note="E -> R (in Ref. 1; CAA11281)"
FT /evidence="ECO:0000305"
FT CONFLICT 547..548
FT /note="EL -> DV (in Ref. 1; CAA11280/CAA11281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 828 AA; 93899 MW; C6C7B161C8904D03 CRC64;
MGGSSGGGVS YRSGGESDVE LEDYEVDDFR DGIVESRGNR FNPLTNFLGL DFAGGSGGKF
TVINGIRDIS RGSIVHPDNR WYKAWTMFIL IWALYSSFFT PLEFGFFRGL PENLFILDIA
GQIAFLVDIV LTFFVAYRDS RTYRMIYKRS SIALRYLKST FIIDLLACMP WDIIYKAAGE
KEEVRYLLLI RLYRVHRVIL FFHKMEKDIR INYLFTRIVK LIFVELYCTH TAACIFYYLA
TTLPASQEGY TWIGSLKLGD YSYSKFREID LWTRYTTSMY FAVVTMATVG YGDIHAVNMR
EMIFAMVYIS FDMILGAYLI GNMTALIVKG SKTERFRDKM ADIMRYMNRN KLGRNIRGQI
TGHLRLQYES SYTEAAVLQD IPVSIRAKIA QTLYLPYIEK VPLFRGCSSE FINQIVIRLH
EEFFLPGEVI MEQGSVVDQL YFVCHGVLEE IGITKDGSEE IVAVLQPDHS FGEISILCNI
PQPYTVRVAE LCRILRLDKQ SFMNILEIFF HDGRRILNNL LEGKESNVRI KQLESDITFH
ISKQEAELAL KLNSAAFYGD LYQLKSLIRA GGDPNKTDYD GRSPLHLAAS RGYEDITLYL
IQESVDVNIK DKLGSTPLLE AIKNGNDRVA ALLVKEGATL NIENAGTFLC TVVAKGDSDF
LKRLLSNGID PNSKDYDHRT PLHVAASEGF YVLAIQLVEA SANVLAKDRW GNTPLDEALG
CGNKMLIKLL EDAKNSQISS FPSGSKEPKD KVYKKKCTVY FSHPGDSKEK RRRGIVLWVP
RSIEELIRTA KEQLNVPEAS CVLSEDEAKI IDVDLISDGQ KLYLAVET
