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 03-AUG-2022, entry version 98.
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; 4530.OS07T0175400-00; -.
DR PaxDb; Q8H569; -.
DR PRIDE; Q8H569; -.
DR eggNOG; KOG0498; Eukaryota.
DR InParanoid; Q8H569; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
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; -; 1.
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; 1.
DR Pfam; PF13857; Ank_5; 1.
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; 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 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
