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Database: UniProt
Entry: A0A7J9GE85_9ROSI
LinkDB: A0A7J9GE85_9ROSI
Original site: A0A7J9GE85_9ROSI 
ID   A0A7J9GE85_9ROSI        Unreviewed;      1063 AA.
AC   A0A7J9GE85;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   28-JAN-2026, 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=Gohar_006494 {ECO:0000313|EMBL:MBA0795648.1};
OS   Gossypium harknessii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=34285 {ECO:0000313|EMBL:MBA0795648.1, ECO:0000313|Proteomes:UP000593560};
RN   [1] {ECO:0000313|EMBL:MBA0795648.1, ECO:0000313|Proteomes:UP000593560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0 {ECO:0000313|EMBL:MBA0795648.1};
RC   TISSUE=Leaf {ECO:0000313|EMBL:MBA0795648.1};
RX   PubMed=30476109;
RA   Grover C.E., Arick M.A. 2nd, Thrash A., Conover J.L., Sanders W.S.,
RA   Peterson D.G., Frelichowski J.E., Scheffler J.A., Scheffler B.E.,
RA   Wendel J.F.;
RT   "Insights into the evolution of the New World diploid cottons (Gossypium,
RT   subgenus Houzingenia) based on genome sequencing.";
RL   Genome Biol. Evol. 11:53-71(2019).
CC   -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC       calcium. {ECO:0000256|RuleBase:RU361146}.
CC   -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC       ATP coupled with the translocation of calcium from the cytosol out of
CC       the cell or into organelles. {ECO:0000256|ARBA:ARBA00053300}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Ca(2+)(in) + ATP + H2O = Ca(2+)(out) + ADP + phosphate + H(+);
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:ARBA00048694,
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:MBA0795648.1}.
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DR   EMBL; JABFAD010000004; MBA0795648.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7J9GE85; -.
DR   OrthoDB; 3352408at2759; -.
DR   Proteomes; UP000593560; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
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:0046872; F:metal ion 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   FunFam; 1.20.1110.10:FF:000039; Calcium-transporting ATPase; 1.
DR   FunFam; 2.70.150.10:FF:000006; Calcium-transporting ATPase; 1.
DR   FunFam; 3.40.1110.10:FF:000013; Calcium-transporting ATPase; 1.
DR   FunFam; 3.40.50.1000:FF:000018; Calcium-transporting ATPase; 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; IPR059000; ATPase_P-type_domA.
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; PR00121; NAKATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
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|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU361146}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361146};
KW   Reference proteome {ECO:0000313|Proteomes:UP000593560};
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};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361146}.
FT   TRANSMEM        160..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        200..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        355..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        405..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        834..852
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        858..878
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        971..990
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        1002..1021
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          111..188
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1040..1063
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1055
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1063 AA;  117200 MW;  F627C52F69B1A265 CRC64;
     MSSSDGNQMY DCGTLLFKVT TSGFTTAQKR WRIAYASIYS VRVMLSLAKE IISKRGIEQP
     SIISDLHPYV ALDVEPSSSP QWGEKFSSSS LAPKIDRKRL VETVKEKDLV SLHQLGGVEG
     IAAALGTNPE KGIRDDDREV VKRQEMFGTN TYHKPPPKGL LYFVLDAFKD TTILILLVCA
     ALSLGFGIKE HGAAEGWYEG GSIFVAVFLV IAVSALSNLR QETQFDKLSK ISNNIKVEVV
     RGGRRRQVSI FDLVVGDVVF LKIGDQIPAD GLFLDGYSLQ VDESSMTGES DHMEVDATRN
     PFLFSGSKVA DGYGQMLVAS VGMDTTWGEM MSSITSDKNE RTPLQERLDR LTSSIGKVGL
     AVAFLVLVVL LIRYFTGNTE DDNGNTEYIG SKTSVDDILN AVVRIISAAV TIVVVAIPEG
     LPLAVTLTLA YSMKRMMADQ AMVRKLSACE TMGSATIICT DKTGTLTVNQ MKVTQFWLGQ
     ESIKEDHSNI IDHTVLELFY QGVGLNTTGS VCKPVSGSLP EFSGSPTEKA ILSWAVLGLD
     LDMEKLKQKY SILHVETFNS EKKRSGVSVR RRTDETLHVH WKGAAEIIVA MCSDYYESNG
     GIRSMDEDQR SRIETIIQSM AASSLRCIAF AHKQVSQKEM ECVDDSEKTH QRIKEDGLTL
     LGIVGLKDPC RPGVKKAVEA CKSAGVDIKM ITGDNIFTAK AIAAECGILG ADYNEESGQA
     IEGIEFRNYT PEERMEKIGK IKVMARSSPF DKLLMVQCLK QKGDVVAVTG DGTNDALALK
     EADIGLSMGI QGTEVAKESS DIVILDDNFS SVATVLRWGR CVYNNIQKFI QFQLTVNVAA
     LVINFIAAVS AGEVPLTAVQ LLWVNLIMDT LGALALATDR PTKELMKKPP VGRTEPLITN
     VMWRNLLAQA VYQIAILLIL QFRGESMFNV PKRVKDTLIF NTFVLCQVFN EFNARKLEKQ
     NVFQGILQNR LFLGIVGITI ILQVVMVEFL KNFADTERLK LWQWGLCILF AAFSWPIAWV
     VKLIPVSDKP FFSYLKRSKP SSQLNKSSTT RNLQSAGMEL EVQ
//
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