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Database: UniProt
Entry: A0A5D2SEY9_GOSMU
LinkDB: A0A5D2SEY9_GOSMU
Original site: A0A5D2SEY9_GOSMU 
ID   A0A5D2SEY9_GOSMU        Unreviewed;      1106 AA.
AC   A0A5D2SEY9;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   ORFNames=E1A91_D12G161400v1 {ECO:0000313|EMBL:TYI51232.1};
OS   Gossypium mustelinum (Cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=34275 {ECO:0000313|EMBL:TYI51232.1, ECO:0000313|Proteomes:UP000323597};
RN   [1] {ECO:0000313|EMBL:TYI51232.1, ECO:0000313|Proteomes:UP000323597}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1408120.09 {ECO:0000313|EMBL:TYI51232.1};
RA   Chen Z.J., Sreedasyam A., Ando A., Song Q., De L., Hulse-Kemp A., Ding M.,
RA   Ye W., Kirkbride R., Jenkins J., Plott C., Lovell J., Lin Y.-M., Vaughn R.,
RA   Liu B., Li W., Simpson S., Scheffler B., Saski C., Grover C., Hu G.,
RA   Conover J., Carlson J., Shu S., Boston L., Williams M., Peterson D.,
RA   Mcgee K., Jones D., Wendel J., Stelly D., Grimwood J., Schmutz J.;
RT   "WGS assembly of Gossypium mustelinum.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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; CM017660; TYI51232.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5D2SEY9; -.
DR   Proteomes; UP000323597; Chromosome d12.
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; cd07536; P-type_ATPase_APLT; 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:SF19; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 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:UP000323597};
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        44..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        268..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        818..839
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        894..915
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        922..941
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        953..977
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        989..1010
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          5..70
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          778..1017
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   REGION          1046..1106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1053..1106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1106 AA;  124871 MW;  BFC3B0D6660529FB CRC64;
     MKRYVYINDN ESSHELYCDN RISNRKYTVL NFLPKNLWEQ FSRFMNQYFL LIACLQLWSL
     ITPVNPASTW GPLIFIFAVS ASKEAWDDYN RYLSDKKANE KLVWVVRQGI RKHIQAQDIH
     VGNIVWLREN DEVPCDLVLI GTSDPQGLCY VETAALDGET DLKTRVIPSA CMGIDFELLH
     KIKGVIECPN PDKDITRFDA NLRLFPPFID NDVCPLTIKN TILQSCYLRN TEWACGVAVY
     TGNETKLGMS RGIPEPKLTA MDAMIDKLTG AIFVFQIVVV MVLGIAGNVW KDTEARKQWY
     VQYPIEGPWY ELLVIPLRFE LLCSIMIPIS IKVSLDLVKS LYAKFIDWDA EMIDYETGIP
     SHATNTAISE DLGQVEYIMT DKTGTLTENR MIFRRCCISG VFYGNESGDA LKDTKLLNAV
     AGSSPDVVQF LTVMAICNTV VPIKSKTGAI SYKAQSQDED ALVNAAAQLH MVYANKNANI
     LEIRFNGSVI KYEVLEILEF TSDRKRMSVV VKDCQNGKIV LLSKGADEAI LPFAYVGQQT
     RTFIEAVEQY AQLGLRTLCL ACRELREDEY QEWSLLFKEA SSTLVDREWR IAEVCQRLEH
     DFEVLGVTAI EDRLQDGVPE TIETLRKAGI NFWMLTGDKQ NTAIQIALSC NFISPEPKGQ
     LLLIDGKTED EVCRSLERVL LTMRITSSEP KDVAFVVDGW ALEIALKHYR KAFTELAILS
     RTAICCRVTP SQKAQLVELL KSCDYRTLAI GDGGNDVRMI QQADIGVGIS GREGLQAARA
     ADYSIGKFRF LKRLILVHGR YSYNRTAFLS QYSFYKSLVI CFIQIFFSFI SGVSGTSLFN
     SVSLMAYNVF YTSIPVLVSV LDKDLSEGTV MQHPQILFYC QAGRLLNPST FAGWFGRSLF
     HAIVVFVITI HAYAYEKSEM EELSMVALSG CIWLQAFVVA LETNSFTILQ HLAIWGNLVA
     FYVINWIFSA IPASGMYTIM FRLCRHPSYW ITMSLIVAAG MGPVLALKYF RYTYRPSKIN
     TLQQAERMGG PILTLGNIEP HPRPMEKEVV SPLQISQPKN RNPVYEPLLS DSPNSSRRSL
     GSGTPFDFFQ SQSRLSSSYS RNCKDN
//
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