ID A0A0D2WNK9_CAPO3 Unreviewed; 1448 AA.
AC A0A0D2WNK9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Na+ P-type-ATPase {ECO:0000313|EMBL:KJE91998.1, ECO:0000313|EMBL:KJE91999.1};
DE SubName: Full=Na+ P-type-ATPase, variant 2 {ECO:0000313|EMBL:KJE92000.1};
DE SubName: Full=Na+ P-type-ATPase, variant 3 {ECO:0000313|EMBL:KJE92001.1};
GN ORFNames=CAOG_003039 {ECO:0000313|EMBL:KJE91998.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE91998.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|EMBL:KJE91998.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|EMBL:KJE91998.1};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KE346363; KJE91998.1; -; Genomic_DNA.
DR EMBL; KE346363; KJE91999.1; -; Genomic_DNA.
DR EMBL; KE346363; KJE92000.1; -; Genomic_DNA.
DR EMBL; KE346363; KJE92001.1; -; Genomic_DNA.
DR RefSeq; XP_004363878.1; XM_004363821.2.
DR STRING; 595528.A0A0D2WNK9; -.
DR EnsemblProtists; KJE91998; KJE91998; CAOG_003039.
DR EnsemblProtists; KJE91999; KJE91999; CAOG_003039.
DR EnsemblProtists; KJE92000; KJE92000; CAOG_003039.
DR EnsemblProtists; KJE92001; KJE92001; CAOG_003039.
DR GeneID; 14899635; -.
DR eggNOG; KOG0202; Eukaryota.
DR InParanoid; A0A0D2WNK9; -.
DR OMA; FGIDDYI; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000008743; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
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; 3.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF14; SODIUM TRANSPORT ATPASE 1-RELATED; 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; 2.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ion transport {ECO:0000256|ARBA:ARBA00023201};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008743};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023201}.
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 465..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 686..707
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 713..739
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1281..1303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1323..1342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1363..1381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1393..1413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 390..464
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1448 AA; 154733 MW; 0268119C2135FEEC CRC64;
MDYNTTPGTN HERRDDEPQR AAGEEAVAAT EFVATVSAPA PAPARDVHPA DPAAAPVIAD
DVSHVSTAAA FNEPATLPAP TAPAPAPAPA PAVPRSGSAL SFEAAVRGGP TVLFRDDGSG
SDTDHDDETS GADAAQKPQG TVTAAMMMAG AVPSALSSGD QLQHRSSGAS SPVHGSGPSS
RRLTPVASYT SLMAMGDTVK MPHVTTIASR NAFHADDEEL WDEQARMMAQ FYPHGHSASH
PSDLHDAASS PGLMTAAAAA AAAAAAAAAG GSGTPRPTSP TLQASASMAR PKSANRLDQL
KHSFAINQVP SSGEVAGLAS PPSAMRLSMH SHHRVTALAT SASSERANFL RQRSHLQFEV
NALVEGHSMH AGFEILPEAV PVELATAQQL AFTMSVATVA ASFETNIQRG LTRQEAEDRL
ERFGYNELAL EAGVSAWRVF VSNLINAMNM VLLIAVAVSA AVQDVVNVVV ILIVLVTNTG
IGFFQEYRSE RTMEALQKLS APTARVLRDG ELSVEGSAFV VPGDIVYLEE GDQVPADLRL
VSGVNLEIDE ALLTGEPLPV RKHPALINDP NIPLGDRINM VFKNTLITKG RGVGIAVTTG
LATEIGKIAL IVANKAPSEK NKQETTAMQE VTVRTDVETE EERLDAIDDA NTTRLILPLR
VIRRFWDNTF GKHSGKSPLQ RRLEKLMFIL LGVAVVLAII VFAANRFVGE SVIALYAIAV
AIAIIPEGLP AVITVTMALG VRRMATQKAV VRKISALEQL GDTTNICSDK TGTITVGKMV
VTEVWAGERL YQVRGNGIVP EGEIVDSDEQ VVDVTRLPSD LSDAALVCSM CNGSRIQFVD
EKWSATGDPT EVALLVFGYK ADKNREELDK QMDTICELPF DSVVKRMTVV YRQNTAYHIF
LKGATESVLA CCEAYQCGNE VKPLTPEIVQ HIMSQVDSLA SKGLRVLALA RNTMPSNLHS
PANPVKEKGA RFTVGPSTNS LGLSEADEHE DEHDGSDGVL LGGGPTGKYA PSAWTTDFRD
EIEQRLTFVG LAGMFDPPRS TTAGAVVQAH EAGISVHMAT GDHPATAAAI AKMVGIVTEE
DMRANPKLVM VARDFDAMTD AELDAADELP RVLARCSPAS KVRLIHCLHR RKKRVAMTGD
GVNDAPAVKQ ADVGIAMGFG GSDVTKQASD IVLTDDNFAT ILVAISEGRR IFANISKFIV
HLMASNLAEM VVLIIGLCVQ DANNISVFPL SPLQILWLNM ITSSPPALAL GVEGPAPDIM
TNKPRPNDVG LFTREVVVDM VFYGCVMGVL GLVAFILRVF AFSDGINSTE CNTSYSDACE
NVFRARSTVF LMLNFFFLYI AYNCRHARMS TFKLKVFGNM AMLYTMAIGG SITLATVYIP
YVNTRILEQA PISWEWAIIA VGCVIFVIST EIYKYGKRRH YAQVDARAAA THAPSNQLEM
VAISTHST
//
