ID A0A2I0B1V2_9ASPA Unreviewed; 1033 AA.
AC A0A2I0B1V2;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=AXF42_Ash008604 {ECO:0000313|EMBL:PKA61773.1};
OS Apostasia shenzhenica.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Apostasioideae; Apostasia.
OX NCBI_TaxID=1088818 {ECO:0000313|EMBL:PKA61773.1, ECO:0000313|Proteomes:UP000236161};
RN [1] {ECO:0000313|EMBL:PKA61773.1, ECO:0000313|Proteomes:UP000236161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shenzhen {ECO:0000313|Proteomes:UP000236161};
RC TISSUE=Stem {ECO:0000313|EMBL:PKA61773.1};
RX PubMed=28902843; DOI=10.1038/nature23897;
RA Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA Van de Peer Y., Liu Z.J.;
RT "The Apostasia genome and the evolution of orchids.";
RL Nature 549:379-383(2017).
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. {ECO:0000256|RuleBase:RU361146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000256|ARBA:ARBA00000363,
CC ECO:0000256|RuleBase:RU361146};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIB subfamily. {ECO:0000256|ARBA:ARBA00006124,
CC ECO:0000256|RuleBase:RU361146}.
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DR EMBL; KZ451923; PKA61773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0B1V2; -.
DR STRING; 1088818.A0A2I0B1V2; -.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000236161; Unassembled WGS sequence.
DR GO; GO:0016020; C: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:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1.
DR Gene3D; 1.20.5.170; -; 1.
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; IPR024750; Ca_ATPase_N_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR24093:SF369; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR Pfam; PF12515; CaATP_NAI; 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; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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:RU361146};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU361146};
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Hydrolase {ECO:0000313|EMBL:PKA61773.1};
KW Ion transport {ECO:0000256|RuleBase:RU361146};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361146};
KW Reference proteome {ECO:0000313|Proteomes:UP000236161};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361146};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361146}; Transport {ECO:0000256|RuleBase:RU361146}.
FT TRANSMEM 169..188
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 351..372
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 392..422
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 814..836
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 842..860
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 881..902
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 917..934
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 954..979
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 985..1005
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 114..186
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1014..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1033 AA; 113173 MW; 174D46470A3ABCB4 CRC64;
MESFLKKNFD LPAKNPSEEV QRRWRSAVGQ IVRNRKRRFR MVADLQKRSE AEARRRSIQE
KIRVALYVQK AALTFIAVGI KYQLPEDARK AGFYISPDEL ATIAREHNSE RLKTKGGVDG
ISRKLSVSLE DGIKTSDLSL RQNIFGANQF AEKPTRSFWM FVWDAVQDLT LIILMICAVV
SIGVGLATEG WPKGMYDGLG IILSIFLVVI VTAVSDYKQS LQFRDLDREK KKIFMQVTRD
GYRQKVSIYD LVVGDIVHLS IGCQVPADGL FISGYSLSID ESSLSGESDP VFVTSEKPFL
LAGTTVQDGS AIMLVTAVGM RTEWGRLMET LSQGGEDETP LQVKLNGVAT IIGKIGLAFA
TLTFVVLVAR FLVDKAIHVG LLKWFADDAL LIMNYFAISV TIIVVAVPEG LPLAVTLSLA
FAMKKLMDDK ALVRHLSACE TMGSSGTICT DKTGTLTTNH MVVDKIWICE TSNSFRSKET
SKHLRETLSE KVVCILLQCI FHNSGSEVVR GKDGKNIILG TPTETALLEF GLDLEGVIDT
THHRDCTKLK VEPFNSVKKK MSVLVSLPGG GVRAFCKGAS EIIMLMCDKI IDGEGNAAPL
SENQTKSVLD VINCFACDAL RTLCLAYKDM GDAPRDEIPT EGYTLIAVFG IKDPVRPGVK
EAVQTCLTAG IKVRMVTGDN INTAKAIAKE CGILTDDGLA IGGSEFRNKS PEEMKELIPK
LQVMARSLPL DKHTLVANLR SMGEVVAVTG DGTNDAPALH ESDIGLAMGI AGTEVAKENA
DVIVLDDNFA TIVNVARWGR AVYINIQKFV QFQLTVNVVA LILNFVSACI TGNAPLTAVQ
LLWVNMIMDT LGALALATEP PNDEMMKRPP TGRGENFITK AMWRNIIGQS IYQLLVLGVF
MFDGKRLLGL SGSNADMVLK TFIFNIFVFC QLFNEINTRQ MEKLNVFRGI FGSWIFSVVL
LSTTVFQVII VEFLGAFVST VPLSWQLWVL SIVIGSVSMI VGVVLKCIPV GPVKSQSHNH
NGYQPIPSGP PEV
//