AKT1_ORYSI
ID AKT1_ORYSI Reviewed; 935 AA.
AC P0C550; Q8VYX2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Potassium channel AKT1;
DE Short=OsAKT1;
GN Name=AKT1;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 76-935, AND TISSUE SPECIFICITY.
RC STRAIN=cv. IR29;
RX PubMed=12602892; DOI=10.1023/a:1020763218045;
RA Golldack D., Quigley F., Michalowski C.B., Kamasani U.R., Bohnert H.J.;
RT "Salinity stress-tolerant and -sensitive rice (Oryza sativa L.) regulate
RT AKT1-type potassium channel transcripts differently.";
RL Plant Mol. Biol. 51:71-81(2003).
CC -!- FUNCTION: Highly selective inward-rectifying potassium channel that
CC mediates potassium uptake by plant roots. {ECO:0000250}.
CC -!- SUBUNIT: The potassium channel is probably a homo- or heterotetrameric
CC complex of pore-forming subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the epidermis and endodermis of
CC roots, and at lower level in cells of the vasculature and the cortex.
CC Expressed in xylem parenchyma, phloem and mesophyll cells of leaves.
CC {ECO:0000269|PubMed:12602892}.
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}.
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DR EMBL; AY065970; AAL40894.1; -; mRNA.
DR AlphaFoldDB; P0C550; -.
DR SMR; P0C550; -.
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; 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 2: Evidence at transcript level;
KW ANK repeat; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..935
FT /note="Potassium channel AKT1"
FT /id="PRO_0000293086"
FT TOPO_DOM 1..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..136
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 289..308
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..312
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..935
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 565..594
FT /note="ANK 1"
FT REPEAT 598..627
FT /note="ANK 2"
FT REPEAT 631..660
FT /note="ANK 3"
FT REPEAT 662..691
FT /note="ANK 4"
FT REPEAT 695..724
FT /note="ANK 5"
FT REPEAT 728..757
FT /note="ANK 6"
FT DOMAIN 859..935
FT /note="KHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00823"
FT REGION 826..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 419..538
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
SQ SEQUENCE 935 AA; 104465 MW; F606E35E9CA69B23 CRC64;
MARWGAARMA ACGPWGRNRR VGAGDAFEAS EVRRDGRSRM MPACGPWGAG HGGGDPALER
ELSRDGSHYS ISSAILPSLG ARSNRRIKLR RFIISPYDRR YRIWETFLIV LVVYSAWVSP
FEFGFIPKPT GALATADNVV NAFFAVDIIL TFFVAYLDKM SYMLEDDPKK IAWRYSTTWL
VLDVASTIPS EFARRILPSK LRSYGFFNML RLWRLRRVSS LFSRLEKDRH FNYFWVRCAK
LICVTLFAVH CAACFYYLLA DRYPVPTSTW IGNYMADFHE RSLWIRYVTS VYWSITTLTT
VGYGDLHAEN TREMIFNIFY MLFNLGLTAY LIGNMTNLVV HGTSRTRNYR DTIQAATSFG
VRNQLPPRLQ DQMISHISLK YRTDSEGLQQ QEILDSLPKA IKSSISQYLF FHLVQNVYLF
QGVSNDLIFQ LVSEMKAEYF PPREDVILQN EAPTDFYILV SGSVELVEQQ NGADQVIQVA
TSGEVVGEIG VLCYRPQLFT VRTRSLCQLL RLNRTAFLSI VQSNVGDGTI IMNNLIQFLK
EQKENSVMAG VVKEIESMLA RGNLDLPITL CFAVTRGDDF LLHQLLKRGM DPNESDNDGH
TALHIAASKG NEQCVRLLLE YGADPNARDS EGKVPLWEAL CEKHAAVVQL LVEGGADLSS
GDTGLYACIA VEESDTELLN DIIHYGGDVN RARRDGTTAL HRAVCDGNVQ MAELLLEHGA
DIDKQDGNGW TPRALAEQQG HDDIQLLFRS RKAATASGHH HVPSSTTTRV APAAAAASLI
GRFNSEPMMK NMIHEDADLP SRVLPEKLRR KRVTFQNSLF GVISSSQAQR ETDHPLSRGG
LAATGSPNPS SGSRNAVIRV TISCPEKGNT AGKLVLLPQT LDMLLELGAK KFDFAPTKVL
TVEGAEVDEV ELIRDGDHLV LVSDEWDAEK MKGKS
