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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
 
 
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