ID A4RQL0_OSTLU Unreviewed; 1007 AA.
AC A4RQL0;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
GN ORFNames=OSTLU_48492 {ECO:0000313|EMBL:ABO93700.1};
OS Ostreococcus lucimarinus (strain CCE9901).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=436017 {ECO:0000313|EMBL:ABO93700.1, ECO:0000313|Proteomes:UP000001568};
RN [1] {ECO:0000313|EMBL:ABO93700.1, ECO:0000313|Proteomes:UP000001568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCE9901 {ECO:0000313|EMBL:ABO93700.1,
RC ECO:0000313|Proteomes:UP000001568};
RX PubMed=17460045; DOI=10.1073/pnas.0611046104;
RA Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N.,
RA Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R.,
RA Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K.,
RA Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M.,
RA Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I.,
RA Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D.,
RA Van de Peer Y., Moreau H., Grigoriev I.V.;
RT "The tiny eukaryote Ostreococcus provides genomic insights into the paradox
RT of plankton speciation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362084};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000256|ARBA:ARBA00006934,
CC ECO:0000256|RuleBase:RU362084}.
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DR EMBL; CP000581; ABO93700.1; -; Genomic_DNA.
DR RefSeq; XP_001415408.1; XM_001415371.1.
DR AlphaFoldDB; A4RQL0; -.
DR STRING; 436017.A4RQL0; -.
DR EnsemblPlants; ABO93700; ABO93700; OSTLU_48492.
DR GeneID; 4999638; -.
DR Gramene; ABO93700; ABO93700; OSTLU_48492.
DR KEGG; olu:OSTLU_48492; -.
DR eggNOG; KOG0203; Eukaryota.
DR HOGENOM; CLU_002360_3_3_1; -.
DR OMA; FQDWSTK; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000001568; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005775; P-type_ATPase_IIC.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01106; ATPase-IIC_X-K; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362084};
KW Ion transport {ECO:0000256|RuleBase:RU362084};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362084};
KW Metal-binding {ECO:0000256|RuleBase:RU362084};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362084}; Potassium {ECO:0000256|RuleBase:RU362084};
KW Potassium transport {ECO:0000256|RuleBase:RU362084};
KW Reference proteome {ECO:0000313|Proteomes:UP000001568};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362084};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362084}; Transport {ECO:0000256|RuleBase:RU362084}.
FT TRANSMEM 77..96
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 108..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 301..330
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 835..855
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 898..916
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 937..957
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 969..988
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT DOMAIN 23..97
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 191..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1007 AA; 110923 MW; D7C6477F2E6D53EC CRC64;
MSAAKAAAKA ERAAALRKDV DFVEHTWAAE KLYAHFGCTL EDGLSNERVL ENRAKYGENR
LTPPEVTPWY IKFLMQFANF FALLLLGGGV LCFVGYAIDS EKDQTNLYLG VVLFTVVMIT
ATFSFLQEAK SEAIMEGFKS MIPKKCKAIR GGKAVVIDAW ELVPGDVVDL NDGDQVPADI
RVMRSNELKV DNSSLTGESE PQDRTPELAV DSNGNIVTQP LESTNLCFYT TIINSGSGRG
VVIGSGDRTV MGQIAGLATE TSGEDSPISK EIKKFIQLIS IVAITLGIVF FVVGLTNGTA
IIQNVVFMIG IIVANVPEGL LATVTVSLAL TAKRMHAKNV LVKNLEAVET LGSTTVIASD
KTGTLTQNRM TVQHAWYDNK VISEPGQTPD GEPFYDQSSE AFQRLLQVAT LCNNAEYLTK
SEDGSFIDLK AEMMNPNFNI LKQPATGDAS EQGLLKLVQP LNDALDTRAK YPKLFEIKFN
STNKWQLSIH GQPGGRPPLL VLKGAPERVL AKCTSYFSNG KTSSKDAEFE RTYTQSYEDL
GGRGERVLGF AFKELSGFKN DFKFSQKPKP NFPIDDLTFV GLFSLIDPPR EGVPEAVTKC
NRARIKVYMV TGDHPITAAA IAKQVNIVSQ ENLDNGTACV VKGDDIRAWT EIEDPVAQRA
KWDAALDHKQ IVWARVSPAH KLLIVENCQR RGEIVAVTGD GVNDAPALKK GDIGIAMGIA
GKDVSKEAAD MILMDDNFAS IVNGVEEGRL IFDNLKKSIA YTLSSNIPEI APFLCYITAK
IPSPLTTVLI LCVDLGTDMV PAISMAYEEK EADIMDRPPR NAQTDRLVNF RLISFAYLQI
GIIQALAGFF TYMLVLNDYG YTPSILMGNG LKWTKNSLLC TLNGDSITQP NVDYQTAALE
YAQTAYFITI IIVQWADLMI AKTRKLSIFE QGMGNDFMNF GLIFETVLGA TLCYTPIFNK
VFGTRPLHVL HWFSGVPWSI LIFTYDELRK SLIRSNPKGW LDRWTYW
//
