ID A0A5P1FJI5_ASPOF Unreviewed; 983 AA.
AC A0A5P1FJI5;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, 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=A4U43_C02F19170 {ECO:0000313|EMBL:ONK78476.1};
OS Asparagus officinalis (Garden asparagus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asparagaceae;
OC Asparagoideae; Asparagus.
OX NCBI_TaxID=4686 {ECO:0000313|EMBL:ONK78476.1, ECO:0000313|Proteomes:UP000243459};
RN [1] {ECO:0000313|Proteomes:UP000243459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH0086 {ECO:0000313|Proteomes:UP000243459};
RX PubMed=29093472; DOI=10.1038/s41467-017-01064-8;
RA Harkess A., Zhou J., Xu C., Bowers J.E., Van der Hulst R., Ayyampalayam S.,
RA Mercati F., Riccardi P., McKain M.R., Kakrana A., Tang H., Ray J.,
RA Groenendijk J., Arikit S., Mathioni S.M., Nakano M., Shan H.,
RA Telgmann-Rauber A., Kanno A., Yue Z., Chen H., Li W., Chen Y., Xu X.,
RA Zhang Y., Luo S., Chen H., Gao J., Mao Z., Pires J.C., Luo M., Kudrna D.,
RA Wing R.A., Meyers B.C., Yi K., Kong H., Lavrijsen P., Sunseri F.,
RA Falavigna A., Ye Y., Leebens-Mack J.H., Chen G.;
RT "The asparagus genome sheds light on the origin and evolution of a young Y
RT chromosome.";
RL Nat. Commun. 8:1279-1279(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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361146}.
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DR EMBL; CM007382; ONK78476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5P1FJI5; -.
DR EnsemblPlants; ONK78476; ONK78476; A4U43_C02F19170.
DR Gramene; ONK78476; ONK78476; A4U43_C02F19170.
DR OMA; CFVLWFG; -.
DR Proteomes; UP000243459; Chromosome 2.
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; 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; 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 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|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|RuleBase:RU361146};
KW Reference proteome {ECO:0000313|Proteomes:UP000243459};
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 171..190
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 304..326
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 346..375
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 765..785
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 832..853
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 868..885
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 897..921
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 936..956
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 5..50
FT /note="Calcium-transporting P-type ATPase N-terminal
FT autoinhibitory"
FT /evidence="ECO:0000259|Pfam:PF12515"
FT DOMAIN 117..183
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT DOMAIN 785..958
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
SQ SEQUENCE 983 AA; 107697 MW; 0DE34E5B7A781819 CRC64;
MESFLKRNFE VPAKNPSEDA QRRWRGAVGK LVKNPRRRFR MVPDLDKRSE VEAKKRNIQE
KIRVALYVQK AALQFIDAAS KRHYQLTEEA KRAGFAISPD ELASIATAHD NKGLKLHGGV
EGISKKINVS LKNGTNTNDL VMRQNVYGVN RYIEKPSRSF WMFLWDAFQD LTLMILIFCA
LISVGVGLAT EGWPKGIYDG LGISLCIVLV VTVTAISDYR QSLQFKDLDR EKKKIDIQVT
RDGYRQKISI YDLVVGSKVQ DGSGKMLVIS VGMRTEWGRL MDTLSQGGED ETPLQVKLNG
VATIIGKIGL GFAIATFLVL LVRFLVQKAL HAGITKWFAS DALIILNYFA ISVTIIVVAV
PEGLPLAVTL SLAFAMKKLM NDRALVRHLS ACETMGSASC ICTDKTGTLT TNHMVVDKIW
ICGVSKSFKG KKTIKGLNSL VSGKVSSILL QCIFQNTGSE VVRGKDGKNT ILGSPTESAL
LEFGLELEGD GSSQHRDCNK LKVEPFNSVK KKMSVLVSLP NGRVRAFCKG ASEIILKMCD
KIVDTDGSTV ALSESQALDV INSFASEALR TLCLAYRDLD QADKGADIPS EGYTLIAIVG
IKDPVRPGVK DAVRICKLAG ITVRMVTGDN INTAKAIAKE CGILTDDGLA IEGPEFRSKS
PAEMKELIPK IQVMARSLPL DKHTLVKGLR DTLHEVVAVT GDGTNDAPAL HEADIGLAMG
IAGTEVAKEN ADVIVMDDNF TTIINVARWG RAVYINIQKF VQFQLTVNVV ALIINFFSAC
IAGKAPLTAV QLLWVNLIMD TLGALALATE PPNDEMMKRP PVGRGENFIT KIMWRNIIGQ
SLYQLVALGV LMFDGKRVLH LQGPDADPIL YTVIFNTFVF CQVFNEINSR DMEKLNVFSG
IFSSWVFLMV MASTVAFQII IVEFLGTFAS TVPLSWRMWV VCILIGSISM IVALILKSIP
VESEKSHVSH SGYEPLPSGP DAV
//
