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Database: UniProt
Entry: W1QDF3_OGAPD
LinkDB: W1QDF3_OGAPD
Original site: W1QDF3_OGAPD 
ID   W1QDF3_OGAPD            Unreviewed;      1091 AA.
AC   W1QDF3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=P-type Na(+) transporter {ECO:0000256|ARBA:ARBA00035029};
DE            EC=7.2.2.3 {ECO:0000256|ARBA:ARBA00035029};
GN   ORFNames=HPODL_03387 {ECO:0000313|EMBL:ESW99498.1};
OS   Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS   Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=871575 {ECO:0000313|EMBL:ESW99498.1, ECO:0000313|Proteomes:UP000008673};
RN   [1] {ECO:0000313|EMBL:ESW99498.1, ECO:0000313|Proteomes:UP000008673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC   {ECO:0000313|Proteomes:UP000008673};
RX   PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA   Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA   Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA   Skryabin K.G.;
RT   "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT   DL1.";
RL   BMC Genomics 14:837-837(2013).
RN   [2] {ECO:0000313|Proteomes:UP000008673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC   {ECO:0000313|Proteomes:UP000008673};
RA   Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA   Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT   "Genome sequence of the methylotrophic yeast Hansenula polymorpha DL1.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + K(+)(in) = ADP + H(+) + K(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:75815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00035079};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + Na(+)(in) = ADP + H(+) + Na(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:14633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00034989};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14634;
CC         Evidence={ECO:0000256|ARBA:ARBA00034989};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IID subfamily. {ECO:0000256|ARBA:ARBA00035017}.
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:ESW99498.1}.
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DR   EMBL; AEOI02000007; ESW99498.1; -; Genomic_DNA.
DR   RefSeq; XP_013935170.1; XM_014079695.1.
DR   AlphaFoldDB; W1QDF3; -.
DR   STRING; 871575.W1QDF3; -.
DR   GeneID; 25772827; -.
DR   KEGG; opa:HPODL_03387; -.
DR   eggNOG; KOG0202; Eukaryota.
DR   HOGENOM; CLU_002360_3_3_1; -.
DR   OMA; NGQEYSM; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000008673; Chromosome IV.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0140679; F:ABC-type sodium transporter activity; IEA:RHEA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008554; F:P-type sodium transporter activity; IEA:RHEA.
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; 2.
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; IPR006414; P-type_ATPase_IID.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01523; ATPase-IID_K-Na; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
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; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
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};
KW   Hydrolase {ECO:0000313|EMBL:ESW99498.1};
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:UP000008673};
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        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        106..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        341..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        814..836
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        848..868
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        889..913
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        945..969
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        990..1011
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1023..1042
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..105
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   1091 AA;  120372 MW;  E8D93B06FA25D6D0 CRC64;
     MPTDRNEQAK VSATTHTEIS RESSSDESAI AFYRLAGENV VKYFGTHAVN GLSSSKAKEM
     LAKYGPNSLG DSGKINYGKI LAHQVFNAMI LVLIISMIIA LAIQDWISGG VIGFVVLLNI
     SVGFIQEMKA EKTMNSLKSL SSPSAHVTRD DDDHTIPTEE VVPGDIVHIR VGDTIPADLR
     LIDSMNLETD EALLTGESLP IPKDHTVVFA DESVPVPLGD RCNMAYSSSV VSKGRGTGVV
     VATGLNTEIG KIAKSLQGDK SFIRKVEKNP KDGSKPKKTA YVTACFGTIK DVAANFLGVA
     SGTPLQIKLS WLAIVLFWIA VVFAIVVMAS QKFRVNKEVA IYAICVALSM IPSALIVVLT
     ITMAVGAQVM VSRNVIVRNL DSLEALGGIN DICSDKTGTL TQGRMIAKKV WIPNVGTYSL
     EGSNEPYNPN QGTLSFCKYS PKFVKESDEY VPPEKELPEP APANFAKFCL TAGLANIAIV
     NSYENPETGK TEWKAHGDPT EIAIRVFTSR IPGYTKDELA EKYDHINEFP FDSSIKRMSA
     IYRSKETGEV KVYSKGAVER LLKCCKYWHS FNDKEYDSLR DSQELRPLTE EDIARIEDQM
     EVLSREGLRV LAFAYKDITN DENISLETDN REQIESDLIF QGLVGIYDPP RNETSRSVKL
     CHQAGINVRM LTGDHPGTAK AIAQDVGIVP RNLHHYAEDV VRVMIMTAHE FDKLSDSEID
     ELPVLPLVIA RCAPQTKVRM IEALHRRNKY VAMTGDGVND SPSLKKADVG VAMGMNGSDV
     AKDASDIVLT DDNFASILNA IEEGRRMSAN IQKFVLQLLA ENVAQAIFLL IGLAFMDSSG
     YSVFPLSPVE ILFILVVTSS FPAFGLGVQK AAPDVLEKKP NSTIFTTQVL TDMMVYGIWM
     AACCLFAFVV VVWGHGDGYL GIDCNATSSG AEHCDLVYRA RSTAFATMTW CALILAWECI
     HPLNSLFRMT KETDHPWWKQ TAIDLYENKF LFWSIVGGFV AVFPVVYIPV INSEVFLHSG
     ISWEWGVAFG CTGLYLLGSE LWKWIKRVYL RRREYERAKN PEAELEKSPD IFEKYASLSR
     ASTMDHSTLI V
//
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