ID F6HDV6_VITVI Unreviewed; 1012 AA.
AC F6HDV6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN OrderedLocusNames=VIT_05s0020g04390 {ECO:0000313|EMBL:CCB50477.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB50477.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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; FN595749; CCB50477.1; -; Genomic_DNA.
DR RefSeq; XP_002279888.1; XM_002279852.3.
DR AlphaFoldDB; F6HDV6; -.
DR PaxDb; 29760-VIT_05s0020g04390-t01; -.
DR EnsemblPlants; Vitvi05g00600_t001; Vitvi05g00600_P001; Vitvi05g00600.
DR GeneID; 100254571; -.
DR Gramene; Vitvi05g00600_t001; Vitvi05g00600_P001; Vitvi05g00600.
DR KEGG; vvi:100254571; -.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_2_1; -.
DR InParanoid; F6HDV6; -.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000009183; Chromosome 5.
DR ExpressionAtlas; F6HDV6; baseline and differential.
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; 3.
DR PANTHER; PTHR24093:SF434; CALCIUM-TRANSPORTING ATPASE 13, PLASMA MEMBRANE-TYPE-RELATED; 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 Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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 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:UP000009183};
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 151..168
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 180..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 378..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 809..827
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 833..851
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 946..964
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 976..996
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 92..168
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1012 AA; 110782 MW; 83395A47E42A5489 CRC64;
MSNILHVNLN CITPILDLPT TLSKPNKRWH SAFATIYCFR ALHSLLNKKK NSSKVPISTP
SFVVLNVKPD AFSSIDQTTL NAIVKGKNLN LLLESGGVEG VADALETDIK NGISGAVDDV
ALRQEAFGSN TYKRPPAKSL FHFVVEAFKD VTILILLFCA ALSLGFGIKE HGLKEGWYDG
GSIFVAVILV ISVSAVSNFR QNRQFEKLSK VSNNIKVDVF RNGRRQQISI FEIVVGDVVS
LKIGDQVPAD GLFLDGHSLQ VDESSMTGES DHVEVNSSHN PFLFSGTKVA DGYAQMLVTS
VGMNTTWGQM MSTISRDTNE QTPLQARLNK LTSSIGKAGL AVAFLVLVVL LVRYFTGNTE
DENGNQEFNG SKTKADDIVN AVVAIIAAAV TIVVVAIPEG LPLAVTLTLA YSMKRMMADQ
AMVRKLSACE TMGSATTICT DKTGTLTMNQ MKVTKIWLGQ EPIEVSSSIS TNLLNLIQQG
VALNTTGSVY KASSGSSKFE FSGSPTEKAI LSWAVLELDM DMEILKQNCT ILHVEAFNSE
KKRSGVLVRS KADDTINVHW KGAAEMILAM CSSYYDASGS TKDMDDGERM TFEQIIQGMA
ASSLRCIAFA HKQIPEEKHE IREATQKLKE DGLTLIGLVG IKDPCRPGVR KAVEDCQYAG
VNVKMITGDN VFTARAIATE CGILRPDQGI DNEAVVEGEV FRKYTPEERM EKVDKIRVMA
RSSPFDKLLM VQCLKQKGHV VAVTGDGTND APALKEADIG LSMGIQGTEV AKQSSDIIIL
DDNFASVATV LRWGRCVYNN IQKFIQFQLT VNVAALVINF VAAVSAGEVP LTAVQLLWVN
LIMDTLGALA LSTEQPTKGL MDRPPVGRTE PLITNIMWRN LLAQALYQIA VLLTLQFKGE
SIFGVNEKVK DTLIFNTFVL CQVFNEFNAR KLEKKNVFEG IHKNKLFLGI IGITIILQVV
MVEFLKKFAD TERLNWGQWG ACLGIAAVSW PLGWVVKCIH VSNKPFLSYL KW
//
