ID A0A1U7ZZ59_NELNU Unreviewed; 1044 AA.
AC A0A1U7ZZ59;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN Name=LOC104598680 {ECO:0000313|RefSeq:XP_010259161.2};
GN ORFNames=HUJ06_017898 {ECO:0000313|EMBL:DAD47961.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010259161.2};
RN [1] {ECO:0000313|EMBL:DAD47961.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:DAD47961.1};
RX PubMed=32343808;
RA Shi T., Rahmani R.S., Gugger P.F., Wang M., Li H., Zhang Y., Li Z.,
RA Wang Q., Van de Peer Y., Marchal K., Chen J.;
RT "Distinct Expression and Methylation Patterns for Genes with Different
RT Fates following a Single Whole-Genome Duplication in Flowering Plants.";
RL Mol. Biol. Evol. 37:2394-2413(2020).
RN [2] {ECO:0000313|RefSeq:XP_010259161.2}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361146}.
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DR EMBL; DUZY01000008; DAD47961.1; -; Genomic_DNA.
DR RefSeq; XP_010259161.2; XM_010260859.2.
DR STRING; 4432.A0A1U7ZZ59; -.
DR GeneID; 104598680; -.
DR KEGG; nnu:104598680; -.
DR eggNOG; KOG0204; Eukaryota.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000189703; Unplaced.
DR Proteomes; UP000607653; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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; IBA:GO_Central.
DR CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 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; 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; 2.
DR PANTHER; PTHR24093:SF455; CALCIUM-TRANSPORTING ATPASE 12, PLASMA MEMBRANE-TYPE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING 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; 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 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:UP000189703};
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 205..224
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 414..436
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 838..856
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 862..882
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 975..993
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 117..193
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1044 AA; 115374 MW; 8C397705F0A05DCA CRC64;
MTFVSNALGS LGSLIDYLSI ATKKLHHSQS QNSLPPALTI SHKRWRIART FIYSSRVLVT
LAIDVITRKQ DQLVITILPS SPSFTTLDIK QTTPTFSAID QTKLTQIVKN KNLDLLRHEY
GGAQEVALAL DTHTENGILG DDDDVRHRRE AFGSNTYHKP PPKGFLHFVL EAFKDTTILI
LLVCATLSLA FGIKEHGLKE GWYDGGSIFV AVFLVISVSA GSNFRQSRQF EKLSSISNNI
QVDVVRGGRR QQISIFDVVV GDIACLKIGD QIPADGLFLD GHSLQVDESS MTGESDHVEV
DKTRNPFLIS GAKVADGYGH MLVTSVGMNT GWGEMMNSIN RDSSERTPLQ SRLDKLTSSI
GKVGLAVAFL VLVVLLVRYF TGNTEDENGN REFNGSKAKI NDVLNSVVRI VADAVTIVVV
AIPEGLPLAV TLTLAYSMKR MMVDQALVRK LSACETMGSA TTICTDKTGT LTMNHMKVTE
FWLGQQTISD VASSAIAPTV LQLFHQGVGL NTTGSVFRPT SGETPEFSGS PTEKAVLSWA
VLELDMDMEE LKKNYTIMHV EAFNSEKKRS GISMKKKGEK TINVHWKGAA EIILAMCSSY
YESSGSMKTM HEEDRMKFKQ IIQSMAGKSL RCIAFAHRQI PNEESRDNTD KRAHQSLEET
NLTLLGLVGI KDPCRPGVQE AIKACRKAGV NIKMITGDNV FTARAIAIEC GILEPNLDMN
NGEIVEGVEF RNYTQEERIE KVERIRVMAR SSPLDKLLMV QCLKQKGHVV AVTGDGTNDA
PALKEADIGL SMGIQGTEVA KESSDIVILD DNFASIATVL KWGRCVYNNI QKFIQFQLTV
NVAALVINFV AAISAGKVPL TAVQLLWVNL IMDTLGALAL ATERPTEELM EKPPVGRTKP
LITKVMWRNL MAQALYQIVM LLTLQFKGES IFGVNEKVKD TLIFNVFVLC QVFNEFNARK
LEKKNVFKGI HKNKLFLGIV AITIILQVIM VEFLKKFADT ERLNWRQWCA CFGIAAMSWP
IAWVVKCIPV SDNPFLRSQV VGRL
//
