ID A0A1D6P065_MAIZE Unreviewed; 1141 AA.
AC A0A1D6P065;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=ZEAMMB73_Zm00001d045956 {ECO:0000313|EMBL:AQL03523.1};
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:AQL03523.1};
RN [1] {ECO:0000313|EMBL:AQL03523.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQL03523.1};
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; CM000785; AQL03523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6P065; -.
DR ExpressionAtlas; A0A1D6P065; 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:SF216; 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; 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 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 42..60
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 243..265
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 299..321
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 866..883
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 895..915
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 945..967
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1013..1032
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1052..1075
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 2..46
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 831..1081
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
SQ SEQUENCE 1141 AA; 130030 MW; B827EB5745365204 CRC64;
MSTTKYTLAT FLPKSLFEQF RRVANFYFLV SGILALTPLA PYTAVSALAP LCVVIVATMA
KEGVEDWRRK QQDHELNNRI VKVHRGSGHF EETKWKNIKV GDVIKLEKDN FFPADMILLS
SSYPDGICYV ETMNLDGETN LKIKQALEVT LDLQEDTKFR EVRQTIKCED PNANLYSFVG
SMEWRGQQYP LSPLQLLLRD SKLRNTDYIY GAVIFTGHDT KVMQNATDPP SKRSKIEKKM
DQIIYVLMSS LLMIALLGSI FFGIWTKEDV RDGGLKRWYL RPDATTIFYD PKRAALASFF
HLLTALMLYS YFIPISLYIS IEIVKILQAL FINQDIEMYH EESDKPTHAR TSNLNEELGM
VDTILSDKTG TLTCNMMEFI KCSIAGTAYG KGVTEVERAM AMRKGDSLDD DIENGDYKDK
KNHNSPNVKG FNFKDPRIMD GNWIHEPNKD MIRDFFRLLA ICHTCIAEID ENEKVSYEAE
SPDEAAFVIA ARELGFEFYK RSLATIIIRE QDPSWNVVEK RKYELLNILE FSSSRRRMSV
IVKEPEGRIL LLSKGADSVM FKRLAPNGRK YEEETRRHIN EYSDSGLRTL VLAYRVLDEK
EYKEFNEKLN TAKASVSADR DVKIEQAADS IEQDLILLGA TAVEDKLQQG VPECIDKLAQ
AGIKIWVLTG DKMETAINIG FACSLLRQDM TQIIVTLEQP DIIALEKDGD KYKIFKASKK
KVMSQIEDGI KQIPPSTKIS TASFALIIDG KSIPYALEDD VKFKFLDLAI NCASVICCRS
SPKQKALVTR FVKQVTHKVT LAIGDGANDV GMLQEADIGV GISGAEGMQA VMASDVAVAQ
FRFLERLLLV HGHWCYRRIS VMICYFFYKN VTFGVTLFLY EAFASFSGKP AYNDWFLSLY
NVFFTSLPVI ALGVFDQDVS ARLCIQYPQL YQEGVQNILF SWCRILGWML NGVMNAVLIF
FFCITTFEDQ VFRRDGQVAG LDALGVAMYT CIVWVVNCQM ALSVNYFTII QHIFIWGSIA
VWYLFLIVYG SMNPRFSTTA YMVFIEQLAP ALSFWLVTLF VVLATLVPYF TYAAIQIRFF
PMFHNKIQWK RYLGKAEDPE VARQLSSRHR TSSQQRMVGI SARRDGKAMQ ITRETEIEVQ
E
//
