ID A0A199W244_ANACO Unreviewed; 1058 AA.
AC A0A199W244;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=ACMD2_04342 {ECO:0000313|EMBL:OAY83326.1};
OS Ananas comosus (Pineapple) (Ananas ananas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC Bromelioideae; Ananas.
OX NCBI_TaxID=4615 {ECO:0000313|EMBL:OAY83326.1, ECO:0000313|Proteomes:UP000092600};
RN [1] {ECO:0000313|EMBL:OAY83326.1, ECO:0000313|Proteomes:UP000092600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MD2 {ECO:0000313|Proteomes:UP000092600};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY83326.1};
RX PubMed=27374615; DOI=10.1093/dnares/dsw026;
RA Redwan R.M., Saidin A., Kumar S.V.;
RT "The draft genome of MD-2 pineapple using hybrid error correction of long
RT reads.";
RL DNA Res. 0:0-0(2016).
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}.
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:OAY83326.1}.
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DR EMBL; LSRQ01000355; OAY83326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A199W244; -.
DR STRING; 4615.A0A199W244; -.
DR Proteomes; UP000092600; 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 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; 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; 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; 2.
DR PANTHER; PTHR24093:SF496; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR Pfam; PF12515; CaATP_NAI; 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 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 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:UP000092600};
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 160..185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 197..216
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 350..371
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 404..430
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 857..879
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 934..954
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 966..987
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 112..188
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1058 AA; 115749 MW; 6FC2609392A06303 CRC64;
MDLRSPERYH RRYDEECGGG GGGGGGDGEI CSSSDDAFDI PPKNAPLERL RRWRQAALVL
NASRRFRYTL DLKREEEKEN IRRKIRAHAQ VIRAAFLFKE AGEREAPGSF LAFSCLIVKG
LAKMLKSNVD RGTSEDDMEL MQRREAFGAN TYPRKKGRSF LLFLWEACQD LTLIILMVAA
VISLALGMTT ESVSEGWYDG GSIAFAVILV ILVTAISDYR QSLQFQVLNE EKQNIQLEVI
RGGRRIETSI FDLVVGDVVP LKIGDQVPAD GILISGHSLA IDESSMTGEA KIVHKDQKAP
FLMSGCKVAD GYGTMLVSAV GINTEWGLLM ANISEDNGEE TPLQVRLNGV ATFIGMVGLT
VAGAVLVVLW IRYFTGHTKN PDGTAQFIKG KTSVKEAFNG AIKILTVAVT IVVVAVPEGL
PLAVTLTLAY SMRKMMRDKA LVRRLSSCET MGSATTICSD KTGTLTLNQM TVVEAYVGGT
KLDLPENTKV LSAAASSVVI EGIAQNTTGS VFEPEDGGAT EVTGSPTEKA ILSWGVKMGM
KFSDVRSKSS IIHVFPFSSE KKRGGVAVQL VDNNVHIHWK GAAELVLASC KSWLSADDMA
EASLRCVAFA YRPYDLEKVP KGEQLSNWEL PGDDLILLGI VGIKDPCRPG VKDAVKLCTT
AGVKVRMVTG DNIQTAKAIA LECGILDSGV AVTEPTVIEG RAFRALSEGD REAIAEKITV
MGRSSPNDKL LLVQALKKKG HVVAVTGDGT NDAPALHEAD IGLAMGIQGT EVAKESSDII
ILDDNFASVV KASLIALVIN VIAAISSGDV PLNAVQLLWV NLIMDTLGAL ALATEPPTDK
LMKRSPVGRR EPLITNIMWR NLIIQAVYQV TVLLIFNFAG RSILRLKHDS RDHAERVKNT
FIFNTFVLCQ IFNEFNARKP DEKNIFRGVT KNGFFMGIIA VTILLQVLII EFLGRFTSTV
RLNWKLWLVS IGIGFVSWPL ALVGKFIPVP NIPFLEYFRR CWKSPQQEHF ATKKRSALFL
QQWEPEMRSS SPLRKTMAMP SVRELHSKCE VQFALLIV
//
