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Database: UniProt
Entry: A0A1D6MQV6_MAIZE
LinkDB: A0A1D6MQV6_MAIZE
Original site: A0A1D6MQV6_MAIZE 
ID   A0A1D6MQV6_MAIZE        Unreviewed;      1107 AA.
AC   A0A1D6MQV6;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, 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};
DE   Flags: Fragment;
GN   ORFNames=ZEAMMB73_Zm00001d040456 {ECO:0000313|EMBL:ONM31385.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM31385.1};
RN   [1] {ECO:0000313|EMBL:ONM31385.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM31385.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) 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; CM007649; ONM31385.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6MQV6; -.
DR   OMA; TGSETRI; -.
DR   ExpressionAtlas; A0A1D6MQV6; baseline and differential.
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:SF207; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   PRINTS; PR00121; NAKATPASE.
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   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        346..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        400..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        946..965
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        977..994
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1023..1045
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1057..1074
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1081..1101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          93..146
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          910..1105
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
FT   NON_TER         1107
FT                   /evidence="ECO:0000313|EMBL:ONM31385.1"
SQ   SEQUENCE   1107 AA;  122970 MW;  A036EAECA28588B6 CRC64;
     MASERPLLIA TTPGASTPDD APSPHPPAAS LLPPAQSEPP LRADRLAFSV EIPDPFRSYR
     RGDGPAADPS ASLERERDVG DDESREVIVG ESSPEFSGNA IRTAKYSFLT FLPRNLFEQF
     RRLSYVYFLA ITVLNQLPQV AVFGRGASVL PLAFVLFVTA VKDAYEDFRR HRSDRQENNR
     LATVLALGTA GEFQPKRWKH IRVGDVVRIE SNETLPADMV LLATSDPTGV AHVQTVNLDG
     ETNLKTRYAK QETHVMFSQN GGVGGVLHCE RPNRNIYGFQ ANLEIDGKRV SLGPSNIVLR
     GCELKNTTWA IGVVVYAGKE TKVMLNSSGA PSKRSRLETQ LNRETVILSI MLIGMCTTAS
     VLAGIWLLNH RRELEFTQFF REKDYTTGKN YNYYGVGMQI FITFLMAVIV YQVIIPISLY
     ISMELVRLGQ AYFMGADKDL YDESSRSKFQ CRALNINEDL GQIRYVFSDK TGTLTENKMV
     FQCASIRGVD YNSGKDTGGY SVVVGDHLWT PKMSVKIDPE LVKLLRDGGS NEEPKLVLEF
     LLALASCNTI VPLVLDTRDS KQKLIDYQGE SPDEQALAYA AASYGIVLVE RTSGYIVIDV
     LGDRQRFDIL GLHEFDSDRK RMSVIVGCPD KTVKLYVKGA DSSVFGITNN SSELDIVRAT
     EAHLHKYSSL GLRTLVVGMR KLSQSEFEEW QLAYENASTA VLGRGNLLRS VAANIEINVN
     ILGATGIEDK LQDGVPEAIE SIRQADIKVW ILTGDKQETA ISIGYSCKLL TNDMTQIVIN
     NNSKESCQRS LVEALATTKK LRAASSIGTQ GPLLASETSN VTLALIVDGN SLVYILETDL
     QDELFKLATE CSVVLCCRVA PLQKAGIVAL IKNRTNDMTL AIGDGANDVS MIQMADVGIG
     ISGQEGRQAV MASDFSMGQF RFLVPLLLVH GHWNYQRMAY MILYNFYKNA MFVLVLFWYV
     LYTAFTLTTA ITEWSSLLYT VLYTSLPTIV VGILDKDLNK ATLIAYPKLY GSGQRDDKYN
     VNLFVLNMLE ALWQSLVVFY LPYFAYRRST IDMSSLGDLW ALAPVIVVNM QLAMDIIRWN
     WIIHAFVWGT IAATTVCLFV IDSIWVL
//
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