ID A0A5B6WCP9_9ROSI Unreviewed; 1068 AA.
AC A0A5B6WCP9;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-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=EPI10_020005 {ECO:0000313|EMBL:KAA3479501.1};
OS Gossypium australe.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=47621 {ECO:0000313|EMBL:KAA3479501.1, ECO:0000313|Proteomes:UP000325315};
RN [1] {ECO:0000313|Proteomes:UP000325315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PA1801 {ECO:0000313|Proteomes:UP000325315};
RX PubMed=31479566; DOI=10.1111/pbi.13249;
RA Cai Y., Cai X., Wang Q., Wang P., Zhang Y., Cai C., Xu Y., Wang K.,
RA Zhou Z., Wang C., Geng S., Li B., Dong Q., Hou Y., Wang H., Ai P., Liu Z.,
RA Yi F., Sun M., An G., Cheng J., Zhang Y., Shi Q., Xie Y., Shi X., Chang Y.,
RA Huang F., Chen Y., Hong S., Mi L., Sun Q., Zhang L., Zhou B., Peng R.,
RA Zhang X., Liu F.;
RT "Genome sequencing of the Australian wild diploid species Gossypium
RT australe highlights disease resistance and delayed gland morphogenesis.";
RL Plant Biotechnol. J. 0:0-0(2019).
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:KAA3479501.1}.
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DR EMBL; SMMG02000003; KAA3479501.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B6WCP9; -.
DR Proteomes; UP000325315; Chromosome 10.
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; 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; 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; 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; 1.
DR PANTHER; PTHR24093:SF520; CALCIUM-TRANSPORTING ATPASE 9, PLASMA MEMBRANE-TYPE; 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 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 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:UP000325315};
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 195..220
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 232..251
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 382..406
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 988..1008
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 149..220
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1068 AA; 116490 MW; 64EE555CF73383F3 CRC64;
MSGTSSGNGL LHLNDVEAGL SKDNADLDHH LDPDAGTSDP FDIAHTKNAA PETLKRWRQA
ALVLNASRRF RYTLDLKKEE EKEQRKRMIR AHAQVIRAAL LFKLAGENQI VSGAPVASPS
ACDDYKIGLE QLASMTRDHK LSALEQYGGV KGLSGLLRTN LEKGIDEDEA DLLNRRNAFG
SNTYPRKKGR SFWMFLWEAW QDLTLIILII AAAVSLGLGI KTEGLKEGWY DGGSIFFAVF
LVILVTATSD YRQSLQFQNL NEEKRNIQLE VVRGGRTVKV SIYDLVVGDV VPLKIGDQVP
ADGVLITGHS LAIDESSMTG ESKIVHKNQN DPFLMSGCKV ADGFGTMLVT GVGINTEWGL
LMASISEDTG EETPLQVRLN GVATFIGIVG LSVAVSVLAI LLARYFTGNT EDPGGATQFI
KGRTKFDDAF NDVVKIFTIA VTIVVVAVPE GLPLAVRRLS ACETMGSATT ICSDKTGTLT
LNEMTVVEAF VGKKKINPPA DSSQLHLSVV SLLSEGVAQS TTGNVFVSKD GDDVEISGSP
TEKAILSWAI ELGMKFDAIR SESTILHVFP FNSEKKRGGV ALRRSDAEVH IHWKGAAEIL
LAACSGYLDS NGCLQSMNED KEFFEAAIDE MAANSLRCIA LAFRLCEQEK VPGNEESFDD
WVLPEDNLVL LAIVGIKDPC RPGVKDAVKI CTDAGVKVRM VTGDNIQTAH AIALECGILS
SAQDVTEPTI IEGRVFRALT EKEREQVARK IMVMGRSSPN DKLLLVQALR KGGDVVAVTG
DGTNDAPALH EADIGLSMGI QGTEVAKESS DIIILDDNFA SVVKVVRWGR SVYANIQKFI
QFQLTVNVAA LVINVVAAIS SGDVPLNSVQ LLWVNLIMDT LGALALATEP PTDNLMHRSP
VGRREPLITN IMWRNLLIQA LYQVTVLLVL NFRGMTILQL EDDGNREHAY KVKNSLIFNA
FVMCQIFNEF NARKLEEINC FKGVTKNYLF MGIIGFTFIL QIIIIEFLGK FTSTVRLDWQ
LWLLASCNCG KADSGSQDTG CLVLHKAIST MQKIQGCMNL LFLLFLAI
//
