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Database: UniProt
Entry: AKT3_ORYSJ
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Original site: AKT3_ORYSJ 
ID   AKT3_ORYSJ              Reviewed;         907 AA.
AC   Q8H569; C7J4T3;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 104.
DE   RecName: Full=Potassium channel AKT3;
GN   OrderedLocusNames=Os07g0175400, LOC_Os07g07910; ORFNames=OJ1656_E11.135;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
CC   -!- FUNCTION: Probable inward-rectifying potassium channel. Assuming opened
CC       or closed conformations in response to the voltage difference across
CC       the membrane, the channel is activated by hyperpolarization (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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 (By similarity).
CC       {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the potassium channel family. Plant (TC 1.A.1.4)
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAH93802.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP003843; BAC24865.1; -; Genomic_DNA.
DR   EMBL; AP008213; BAH93802.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q8H569; -.
DR   SMR; Q8H569; -.
DR   STRING; 39947.Q8H569; -.
DR   PaxDb; 39947-Q8H569; -.
DR   eggNOG; KOG0498; Eukaryota.
DR   InParanoid; Q8H569; -.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 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:SF10; POTASSIUM CHANNEL AKT3; 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; 4.
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; 1.
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; 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..907
FT                   /note="Potassium channel AKT3"
FT                   /id="PRO_0000410876"
FT   TOPO_DOM        1..75
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..102
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        124..146
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        168..174
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        196..209
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        231..257
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        258..277
FT                   /note="Pore-forming; Name=Segment H5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        278..288
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..309
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        310..907
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          539..568
FT                   /note="ANK 1"
FT   REPEAT          572..601
FT                   /note="ANK 2"
FT   REPEAT          605..634
FT                   /note="ANK 3"
FT   REPEAT          636..665
FT                   /note="ANK 4"
FT   REPEAT          670..699
FT                   /note="ANK 5"
FT   DOMAIN          827..907
FT                   /note="KHA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00823"
FT   REGION          726..779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..824
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..779
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         388..512
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
SQ   SEQUENCE   907 AA;  99462 MW;  A0D9BAB721BD6E6E CRC64;
     MPTTKCAVPL VSGAAGGGGS AELTRQLSST QASPRFSFSS GVLPSLGSRG GGERHARLRR
     FIVSPYDRRY ELWNNYLILL VVYSAWVTPF EFGFVPEPAG ALAAADNAVN AFFAVDIVLT
     FFVAYTDPKT FLLQDDPRKI ALRYITTWFV LDVVATIPTE LARRILPPDL RSYGFFGILR
     LWRLHRVGIL FARLEKDRKF SYFWVRCVKL VCVTLFAVHC SACFYYLLAD RYPDPTNTWI
     SAYMPNFHKA SIWSRYVASM YWSITTLSTV GYGDMHAENT GEMVFTTTYM LFNLGLTAYI
     IGNMTNLVVH GTSRTRKFRD MIQAATSFAQ RHQLPARLQE QMVSHLSLKF RTNSEGLHQQ
     ETFEALPKAI KSSISHHLFF GLVQNVYLFE GVSNDLIFQL VSEMNAEYFA PREDIILQNE
     APADFYIIVS GSMELIELHN GIEQASVLTL AGMAKSGDVV GEIGVLCYRP QLFTARTRSL
     CQLLRLDRAA FLRIIQSNIA DGTIVMNNLI QYLREKKEIA SIVAVAKEID DMLARGQMDF
     PITLCFAASK GDSFLLHQLL KRGLDPNESD HYGRTALHIA ASNGNEQCVR LLLENGADSN
     SRDPEGRVPL WEALCRRHQT VVQLLVDAGA DLSGGDAAPY ARVAVEQNDA ALLGEIVRHG
     GDVSGACSGD GTTALHRAVL DGNVQMARLL LEHGADADAE DVNGLTPRAV AEQGGHADMQ
     LAFASATRHE PRKARPPPPA SAIVPVPLRD GVDSSPSSSS RRGRTSSTSA ASARSTPQRM
     ANFRNSLFGV ISSSHAFHHE GGYRGGGGGG GAAAERERSS SSPPLVRVAI SCPESRGGKD
     HSSKLVFMPE TLRGLLELGA ARFGVSPTRV VTSGGADVDD ARLVRDGDHL LLVTDKWVPP
     ENRSRNQ
//
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