ID A0A0D2QE47_GOSRA Unreviewed; 1227 AA.
AC A0A0D2QE47;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=B456_002G166300 {ECO:0000313|EMBL:KJB15231.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB15231.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB15231.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
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DR EMBL; CM001741; KJB15231.1; -; Genomic_DNA.
DR RefSeq; XP_012467127.1; XM_012611673.1.
DR AlphaFoldDB; A0A0D2QE47; -.
DR STRING; 29730.A0A0D2QE47; -.
DR EnsemblPlants; KJB15231; KJB15231; B456_002G166300.
DR GeneID; 105785566; -.
DR Gramene; KJB15231; KJB15231; B456_002G166300.
DR KEGG; gra:105785566; -.
DR eggNOG; KOG0206; Eukaryota.
DR OMA; MHSFWSW; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000032304; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF180; PHOSPHOLIPID-TRANSPORTING ATPASE 3; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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|RuleBase:RU362033};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}.
FT TRANSMEM 304..327
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 350..374
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 912..933
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 945..965
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 992..1013
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1028..1047
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1059..1081
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1093..1117
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 45..109
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 881..1131
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1227 AA; 139922 MW; B77BFA0ECE11B6BE CRC64;
MSGWDNIRSS TRSQQGRSHS LNQREPSRTV TLGRVQPQAP AFRTIYCNDR DANFAHRYRG
NSVSTTKYNF FTFLPKGLYE QFRRVANLYF LMVSILSATP YSPVHPVTNV VPLSLVLLVS
LIKEAFEDWK RFQNDMAINS TPVDVLQDQR WESIPWKKLQ VGDIIRVKQD GFFPADMLLL
ASTNADGVCY IETANLDGET NLKIRKALER TWDYVTPEKA CEFKGEVQCE QPNNSLYTFT
GNLVIDNQTL PLSPNQILLR GCSLKNTEFV VGVVIFTGHE TKVMMNSMNV PSKRSTLERK
LDKLILTLFG TLFTMCLIGA IGSGVFIDRK YYFLGLSKSV EDQFNPNRRF LVVLLTMLTL
LTLYSTIIPI SLYVSIEMVK FIQSTQFINK DLNMYHAETD TPALARTSNL NEELGQVEYI
FSDKTGTLTR NLMEFFKCTI GGEIYGTGMT EIERGVAERK GIKVQEVPTS INSVREKGFN
FDDVRLMRGA WRNEPNPEAC KEFFRCLAIC HTVLPEGDES PEKIKYQAAS PDEAALVLAA
KHFGYFFYRR TPTMIYVRES HVERMGKIQD VSYEILNVLE FNSTRKRQSV VCRYPDGRLV
LYCKGADTVI YERLVGGSDD LKKVTREHLE KFGSAGLRTL CLAYKDLAPD VYESWNEKFI
QAKSSLRDRE RKLDEVAELI EKDLILIGAT AIEDKLQEGV PDCIETLSRA GIKIWVLTGD
KMETAINIAY ACNLLNNEMK QFIISSETDA IREVEERGDQ VEIARFIKEE VKKQLKKCLD
EAQQYFHGVS GPKLALIIDG KCLMYALDPS LRIMLLNLSL NCSSVVCCRV SPLQKAQVTS
LVKKGARKIT LSIGDGANDV SMIQAAHIGV GISGLEGMQA VMASDFAIAQ FRFLKDLLLV
HGRWSYIRLC KVVTYFFYKN LTFTLTQFWF TFYTGFSGQR FYDDWFQSLY NVIFTALPVI
IVGLFDKDVS SSLSKRYPEL YKEGIKNMFF KWRVVAIWAF FAVYQSLVFY YFVTVSSSTS
QGSSGKMFGL WDVSTMAFTC VVVTVNLRLL MICNSITRWH YISVGGSIVA WFLFIFLYSG
IMTPYDRQEN IFWVIYVLMS TFYFYITLLL VPVAALLGDF LYLGVQRWFF PYDYQIVQEI
HKDEADDSGR TDLLGIDNQL TPDEARSYAL SQLPRELSKH TGFAFDSPGY ESFFASQLGV
YAPQKAWDVA RRASMRSKPK PKPNKIN
//
