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Database: UniProt
Entry: A0A1D6LW78_MAIZE
LinkDB: A0A1D6LW78_MAIZE
Original site: A0A1D6LW78_MAIZE 
ID   A0A1D6LW78_MAIZE        Unreviewed;       842 AA.
AC   A0A1D6LW78;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Potassium channel {ECO:0000256|RuleBase:RU369015};
GN   ORFNames=ZEAMMB73_Zm00001d037289 {ECO:0000313|EMBL:AQK83498.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK83498.1};
RN   [1] {ECO:0000313|EnsemblPlants:Zm00001eb280210_P006, ECO:0000313|Proteomes:UP000007305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb280210_P006,
RC   ECO:0000313|Proteomes:UP000007305};
RX   PubMed=19965430; DOI=10.1126/science.1178534;
RA   Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA   Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA   Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA   Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA   Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA   Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA   Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA   Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA   Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA   Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA   Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA   Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA   Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA   Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA   Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA   Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA   Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA   Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA   Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA   Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA   SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA   Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA   Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA   Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA   Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA   Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT   "The B73 maize genome: complexity, diversity, and dynamics.";
RL   Science 326:1112-1115(2009).
RN   [2] {ECO:0000313|EMBL:AQK83498.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK83498.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:Zm00001eb280210_P006}
RP   IDENTIFICATION.
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb280210_P006};
RG   EnsemblPlants;
RL   Submitted (MAY-2021) to UniProtKB.
CC   -!- FUNCTION: Potassium channel. {ECO:0000256|RuleBase:RU369015}.
CC   -!- SUBUNIT: The potassium channel is composed of a homo- or
CC       heterotetrameric complex of pore-forming subunits.
CC       {ECO:0000256|RuleBase:RU369015}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU369015}; Multi-
CC       pass membrane protein {ECO:0000256|RuleBase:RU369015}.
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. {ECO:0000256|RuleBase:RU369015}.
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       {ECO:0000256|RuleBase:RU369015}.
CC   -!- SIMILARITY: Belongs to the potassium channel family. Plant (TC 1.A.1.4)
CC       subfamily. {ECO:0000256|ARBA:ARBA00007929,
CC       ECO:0000256|RuleBase:RU369015}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU369015}.
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DR   EMBL; CM000782; AQK83498.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6LW78; -.
DR   EnsemblPlants; Zm00001eb280210_T006; Zm00001eb280210_P006; Zm00001eb280210.
DR   Gramene; Zm00001eb280210_T006; Zm00001eb280210_P006; Zm00001eb280210.
DR   OMA; VWIPHTI; -.
DR   Proteomes; UP000007305; Chromosome 6.
DR   ExpressionAtlas; A0A1D6LW78; baseline and differential.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0034765; P:regulation of monoatomic ion transmembrane transport; IEA:UniProtKB-UniRule.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 1.10.287.630; Helix hairpin bin; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
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; POTASSIUM CHANNEL AKT1; 1.
DR   PANTHER; PTHR45743:SF3; POTASSIUM CHANNEL SKOR; 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; Ankyrin repeat; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 3.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS51490; KHA; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023};
KW   Ion channel {ECO:0000256|RuleBase:RU369015, ECO:0000313|EMBL:AQK83498.1};
KW   Ion transport {ECO:0000256|RuleBase:RU369015};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU369015};
KW   Potassium {ECO:0000256|RuleBase:RU369015};
KW   Potassium channel {ECO:0000256|RuleBase:RU369015};
KW   Potassium transport {ECO:0000256|RuleBase:RU369015};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU369015};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU369015}; Transport {ECO:0000256|RuleBase:RU369015};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU369015}.
FT   TRANSMEM        84..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369015"
FT   TRANSMEM        114..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369015"
FT   TRANSMEM        275..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369015"
FT   TRANSMEM        303..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369015"
FT   DOMAIN          403..523
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REPEAT          579..611
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          612..644
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          676..708
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          755..842
FT                   /note="KHA"
FT                   /evidence="ECO:0000259|PROSITE:PS51490"
SQ   SEQUENCE   842 AA;  95432 MW;  6CB12ADD13D5FF65 CRC64;
     MVRGLGSKRR VAEEESSEEE YEVEVVRDHI ASSRGSRLAL FGSELRLGRF RPRRRRRLPL
     AGEGAAEGFF HGLVIHPDNK WYRLWTKFIL VWAVYSSFFT PLEFGFFRGL PKNLFFLDVA
     GQTAFLIDIV VRFFVAYRDP DTYRVVYSPA AIALRYCKSS FVFDLLGCLP WDAIYKACGS
     KEEVRYLLWI RLTRVTKVTE FFWRLEKDIR VNYLFTRIVK LIVVELYCTH TAACIFYYLA
     TTLPESMEGH TWIGSLQLGD YRFTHFREID LAKRYITSLY FAIVTMATVG YGDIHAVNIR
     EMIFIMIYVS FDMILGAYLI GNMTALIVKG SRTERFRDKM KEVIRYMNRN KLGKEIREQI
     KGHLRLQYES SYTEASVLQD IPISIRAKIS QTLYKPYIES IPLFKGCSAE FIQQIVIRLQ
     EEFFLPGEVI LEQGSAVDQL YFVCHGALEG VGIGEDGQEE TLLMLEPESS FGEISILCNI
     PQPYTVRVCE LCRLLRLDKQ SFTNILEIYF VDGRRILSNL SESEYGGRVK QLESDITFHI
     GKQEAELTLR VNSAAFYGDL HQLKSLIRAG ADPKNTDYDG RSPLHLAASR GYEDVVQFLI
     NEGVDIDLTD QFGNTPLLEA VKQGHERVAA LLFAKGAKLS LKNAGSHLCT AVAKGDSDFI
     RRALAYGADP NCRDYDHRTP LHIAAAEGLY LIAKMLVEAG ASVFTTDRWG TTPLDEARKC
     GGRTLGALLE EARASELSMF PERGEEVRDK VHPRRCSVFP YHPWRASAGE ERRAEGVVLW
     IPHTIESLVA SAQEKLGLPG PAASRLRLLC EDGARVLDVD MVNDGQKLYL VGGEDGDQEG
     GQ
//
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