ID A0A090MD90_OSTTA Unreviewed; 876 AA.
AC A0A090MD90;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Ankyrin repeat {ECO:0000313|EMBL:CEG00029.1};
GN ORFNames=OT_ostta13g00480 {ECO:0000313|EMBL:CEG00029.1};
OS Ostreococcus tauri.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=70448 {ECO:0000313|EMBL:CEG00029.1, ECO:0000313|Proteomes:UP000009170};
RN [1] {ECO:0000313|Proteomes:UP000009170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170};
RX PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA Van de Peer Y., Moreau H.;
RT "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT unveils many unique features.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the potassium channel family. Plant (TC 1.A.1.4)
CC subfamily. {ECO:0000256|ARBA:ARBA00007929}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CEG00029.1}.
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DR EMBL; CAID01000013; CEG00029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090MD90; -.
DR STRING; 70448.A0A090MD90; -.
DR InParanoid; A0A090MD90; -.
DR OrthoDB; 297555at2759; -.
DR Proteomes; UP000009170; Chromosome 13.
DR GO; GO:0016020; C:membrane; 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; 2.
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; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45743; POTASSIUM CHANNEL AKT1; 1.
DR PANTHER; PTHR45743:SF2; POTASSIUM CHANNEL AKT1; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SMART; SM00248; ANK; 5.
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; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009170};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 200..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 416..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 518..641
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REPEAT 710..742
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 807..839
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 1..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 876 AA; 97351 MW; FC84F2AD54685172 CRC64;
MGRRDADDAS PASTGEDVVV NPALARRRGA GGGTRGTGGS GTSGTDAASA SMRERSWDDA
SSWEGEASYG RSVSDGFEGF ASRTSEEPRE DDAASDGRGV RRVSSWFLES DDSGRGEKKT
KRRPSSSMSK TQAAASAAPE EPRRASNAAS AKTLLAASSQ PHTPRSDTFG SKRLQEEDER
VWRFILCHPA SPHARAVTRV VNLLILVVAF IEPASLAFRN ERREVLSNYQ WIDVIEILFS
IVFCVDIFMN FFRPLEKYGK LVWDMKKIAK EYLRGWFVLD FLSSLPFDLM FISKTHDNRD
VSRVIAGLGL LRLLRMYRVR RMMSEFERNS NLPYLVLLSI KFALLIGLAA HWSACLLYYI
ARIQEFNENT WVYAVDPELP NMAFYDVYTT ALYWSVVTLT TVGYGDISPV STSERAVAMV
VMIMNMGVTA YILGNVTQLV TKEDATIMAF RDHTGALQRF MRRNDIPDAV RQKVDAHIQL
EFEMGCRDDE KVLNFCPSTI QSELRHALYQ QYVQESPIFR EVSPVFIQHF LECITVEYFH
PGTLLTCEGL DATAMFYLCL GKVDIVSEDY LTNSTLANKI ETVFPGEWLN IAAVLCGKTC
FHTSVVQSTC KLLVVSTNKL QDVLRRFPID TKHIMKDLLI QYRDEMKECR SQDSRGSLYA
AFINALETKR SELNEVELHQ LTLACVTGDV ADLDMALNDN PQSVHLTDAA GRTLLMTAVE
NKQKEVVKLL LRRGADPNTL SKAGFSALSR AVSVASLELV KLLVSAGGVF TEPSEQVSVH
NAIAQGQIQH LKLLVEAGVC LHNQDYNGST GLHVAARTGS NAAIEILHRA GLEDTFVDKD
GRTALDVAEI SGNPGSVKLL KDMQISSHTK SEPRED
//
