UniProt: A0A1D6P156

Database: UniProt
Entry: A0A1D6P156_MAIZE

LinkDB:  A0A1D6P156_MAIZE 
Original site:  A0A1D6P156_MAIZE

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (1)   
All databases (23)   

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ID   A0A1D6P156_MAIZE        Unreviewed;      1229 AA.
AC   A0A1D6P156;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   ORFNames=ZEAMMB73_Zm00001d046194 {ECO:0000313|EMBL:AQL03813.1};
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:AQL03813.1};
RN   [1] {ECO:0000313|EMBL:AQL03813.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQL03813.1};
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; AQL03813.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6P156; -.
DR   SMR; A0A1D6P156; -.
DR   IntAct; A0A1D6P156; 1.
DR   STRING; 4577.A0A1D6P156; -.
DR   PaxDb; 4577-GRMZM2G135236_P01; -.
DR   eggNOG; KOG0206; Eukaryota.
DR   InParanoid; A0A1D6P156; -.
DR   OMA; GSIRLYC; -.
DR   ExpressionAtlas; A0A1D6P156; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
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:SF150; 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        311..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        364..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        951..974
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        980..1000
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1030..1054
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1066..1086
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1098..1116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1136..1154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          52..117
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          916..1164
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1229 AA;  138402 MW;  F038BA7ACBF9139D CRC64;
     MGRSGRRRRD RMRWSNLYTF SCFRAQHEHA GDAGPSSDGA GAVGGPGFSR VVYCNNAALQ
     KPLKYITNYI TTTKYNVVTF FPKAIFEQFR RVANLYFLLT AILSLTPVCP FSAVSMIAPL
     AFVVGLSMMK EGLEDWRRFM QDMKVNNRNV SVHKSDGEFD YRHWEDLCVG DVVRVEKDQF
     FPADLLLLSS SYEDGICYVE TMNLDGETNL KVKRSLEVTL PLEEDESFKD FQAVIRCEDP
     NPSLYTFTGN FEYERQVYAL DPSQILLRDS KLRNTAFVYG VVIFTGHDSK VMQNSTESPS
     KRSRIERKMD LIIYILFTVL VLISLISSIG FAVRIKLDLP RWWYLQPQKS NKLDDPSRPA
     LSGIFHLITA LILYGYLIPI SLYVSIELVK VLQAHFINQD IHMFDEETGN TAQARTSNLN
     EELGQVHTIL SDKTGTLTCN QMDFLKCSIA GVSYGVGSSE VELAAAKQMA SGADDQDIPI
     QDIWEENNED QIELVEGVTF SVGNNRKPSI KGFSFEDDRL MQGNWTKEPN SSTILLFFRI
     LALCHTAIPE INEATGSIAY EAESPDEGAF LVAAREFGFE FFKRTQSSVF VREKHTSSKG
     TIEREFKILN LLEFNSKRKR MTVILQDEDG QILLLCKGAD SIIFDRLAKN GRMYEVDTTK
     HLNEYGEAGL RTLALSYRVL DESEYSSWNA EFLKAKTSIG PDRELQLERV SELIERELIL
     VGATAVEDKL QKGVPQCIDR LAQAGLKIWV LTGDKMETAI NIGYACSLLR QGMKQICLSI
     PTGEQVAQDA KKALLSSLTT EQAAKESLLS QIANGSQMVK LEKDPDAAFA LVIDGKALAF
     ALEDDMKHMF LNLAIECASV ICCRVSPKQK ALVTRLVKEG IGQTTLAVGD GANDVGMIQE
     ADIGVGISGV EGMQAVMASD FSISQFRFLE RLLVVHGHWC YKRIAQMICY FFYKNIAFGL
     TIFYFEAFAG FSGQSVYDDW FMLLFNVVLT SLPVISLGVF EQDVSSEICL QFPALYQQGP
     KNLFFDWYRI LGWMGNGLFS SLAIFFLNLC IFYDQAIRAG GQTADMAAVG TTMFTCIIWA
     VNIQIALTMS HFTWIQHLFV WGSITTWYIF ILAYGMTLRS GDNYQILLEV LGPAPIYWAG
     TLLVTAACNI PYLIHISYQR SCNPLDHHVI QEIKYLKKDV EDQTMWKRER SKARQKTKIG
     FTARVDAKIK QIKGKLHKKG PSLTIQTVS
//

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