ID A0A444CCN6_ENSVE Unreviewed; 1030 AA.
AC A0A444CCN6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=GW17_00054788 {ECO:0000313|EMBL:RWV83581.1};
OS Ensete ventricosum (Abyssinian banana) (Musa ensete).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Ensete.
OX NCBI_TaxID=4639 {ECO:0000313|EMBL:RWV83581.1, ECO:0000313|Proteomes:UP000288739};
RN [1] {ECO:0000313|EMBL:RWV83581.1, ECO:0000313|Proteomes:UP000288739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Bedadit {ECO:0000313|Proteomes:UP000288739};
RC TISSUE=Leaf {ECO:0000313|EMBL:RWV83581.1};
RX PubMed=29896517; DOI=10.1016/j.dib.2018.03.026;
RA Yemataw Z., Muzemil S., Ambachew D., Tripathi L., Tesfaye K., Chala A.,
RA Farbos A., O'Neill P., Moore K., Grant M., Studholme D.J.;
RT "Genome sequence data from 17 accessions of Ensete ventricosum, a staple
RT food crop for millions in Ethiopia.";
RL Data Brief 18:285-293(2018).
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:RWV83581.1}.
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DR EMBL; JTFG03013853; RWV83581.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444CCN6; -.
DR Proteomes; UP000288739; 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; 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; 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 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 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:UP000288739};
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 142..167
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 179..198
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 388..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 808..828
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 840..859
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 950..968
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 980..1000
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 90..167
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1030 AA; 112960 MW; AD9215024D628AA3 CRC64;
MDCATFLIGS GRRITSVPHR RWRVAFAMIC SCRAMYSLAK KQLASVLRSP SYVVLEVDAD
DDGNHHSQPS FSHVETDSLK SLVKERRLEE LHRLGGAAGL VGTLGSDTEA GIIGSDNDLR
ARREAFGSNS YPRPKPKGFF RFLYEALNDF FLLILMGCAI VSLAFGIKEH GIKEGWYDGA
SIFLAIILVS VVSAVSNFRQ MKRFDRLSTE CNNINVSVVR DGHRQDVSIF DVVVGDVVFL
KIGDQVPADG IFLHGHSLQI DESSMTGESH PVDIDAGKNP FLTSGVKVID GYASMLVTGV
GMDTTWGEMM STITRETTEA TPLQERLEKL TTSIGKIGIV VAALVFAVLM IRHFTGSTKD
ENGQPKFDKD KVTASNVISA IVSIFQDAVT IIVVAIPEGL PLAVTLTLAF SMKRMMKDNA
MVRMLSACET MGSVTTICTD KTGTLTLNQM KVTKFWIGNE EGGPMGSGGS TPFVAPRVLS
LLRQAVGLNT TGSVYRANAT AETEISGSPT EKALLSWAVL DLGMDMGEMR RKCSVIHVEA
FNSEKKRSGV LVQEEGSRAT ITHWKGAAEM ILIRCSHYFD RNGSVRDIDA EARMKFEEVI
RGMAASSLRC IAFAFKDTEA EDHLRVDQGK APRLDDDGLT LLGLVGLKDP CRPEVESAIG
ACRSAGVAVK MITGDNVFTA RAIAVECGII GADDFDGLVV EGQEFRNYSA EERMEKVDQI
RVMARSSPFD KLLMVKCLKE KGHVVAVTGD GTNDAPALKE ADVGLSMGIQ GTEVAKESSD
IVILNDNFST VVTVMRWGRC VYNNIQKFLQ FQLTVNIAAL VVNFVSAIST GEVPLTTVQL
LWVNLIMDTM GALALATDKP TKELMTKRPV GRTEPLITNI MWRNLAAQAM FQIAVLLVFH
FRGESIFGVS QEVNNTLVFN TFVLCQVFNE FNSRKLEKKN VFEGIHQNKL FLGIVAATIV
LQVMMVEFLR KFADTVRLDW GQWGICLGIA AFSWPIGWFV KCIPVSDTPF LEVIDHIRAS
CSRRRIPSCL
//
