ID A0A176WIA1_MARPO Unreviewed; 1084 AA.
AC A0A176WIA1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=P-type Na(+) transporter {ECO:0000256|ARBA:ARBA00035029};
DE EC=7.2.2.3 {ECO:0000256|ARBA:ARBA00035029};
GN ORFNames=AXG93_673s1270 {ECO:0000313|EMBL:OAE32950.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE32950.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE32950.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE32950.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) 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:OAE32950.1}.
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DR EMBL; LVLJ01000698; OAE32950.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176WIA1; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000077202; 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:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
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; 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 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};
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:UP000077202};
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 191..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 851..872
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 884..906
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 927..954
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 974..994
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1015..1037
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1049..1071
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 142..216
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1084 AA; 118339 MW; B38FF7BC4C9C5E77 CRC64;
MVEPEPEPGC SDIWDCDSEI RFCGRLSDGL VYAQHHCWRV HLSFPDRCVL SGFCSISSSK
LRTSSTLHEP ALFSPLLDFD PTLRQQAITC RIDRPGDDRK GGFSNFDYFR EIFDRFSREF
RAQASGDRMN GANGSGSGSG TEWHALPVGE VAQVLQTDVE RGLKEANVEE LQAKFGPNEL
KGQRGVNPWR VLLGQFTNGL TVILVLAAAV SYAVQDYAEG GVLAFVIIFN AAVGFVQEFR
AEKTMDALRR MASPTAKVIR DGGLSRISSP GVVPGDIIVF EVGDVVPADC RLFEVLNLEV
DEAMLTGESL PVAKAVEPIK GDNASLGDRL NMVYSSTTLT KGRGRGVAVA TGMNTEIGKI
TKSIAETSSG STPMQKRLNL MAYILFGISL LLAVVVFAVN KFNFSTDIIL YAVSLSIAVI
PEGLIAVITI VMALGVRRMA SQRALVRKLV ALESLQAVTN ICSDKTGTLT QGKMTVTSVW
RPGSERVVVT GDGWSTTGEF LVRDSAIAPS DLLGDLGFRL LVECSALCNT ANIVEASEGK
VWGDPTEIAL QVLAYKLQMG KPSFRQLKEP VTEYPFSSAT KRMSMLYRDV GRDDFELYTK
GAENVLDLCD RVLENGAEVE IASRDEFLRG VHEQIQVSAK QGLRVLVMAY RTVDERQMGK
SVTKWERADV EASLVFLGLV GIRDTPRPES KVAVDQCYKA GIIVHMLTGD HHDTALAIAK
EVGIIRAPPD RADATVVSLS NPVMTAPEFD AMSEAEIDGL EELPLVIARC TPATKVRMIE
ALHRRRKFAA MTGDGVNDAP SLKKADVGIA MGAGSDVAKQ SSEIVLTDNN FATIVMAVSE
GRRIFSNIRK FVLHLISTNV GEVIVLIIGL AFKDRSGLSV FPLAPVQILY MNMVTSTPPA
MALGVEAASR HVMSVPPHTK GLFGKELLAD MMAYGVIMGG LILTDFVLVI YAFGDGNLGL
ECNSDRNVFE CNTVFRARST ILIAFTWMML LHAYNCRNLR ASLFTKDGGG ASKIFSNKLL
VVSVFVGAIM PIPTVYIPTL NTTVFKQETI SWEWGIIFVS VVAFFFCSEF YKYCKRRVMT
NHHI
//
