ALA12_ARATH
ID ALA12_ARATH Reviewed; 1184 AA.
AC P57792;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Probable phospholipid-transporting ATPase 12 {ECO:0000303|PubMed:11402198};
DE Short=AtALA12 {ECO:0000303|PubMed:11402198};
DE EC=7.6.2.1 {ECO:0000305|PubMed:11402198};
DE AltName: Full=Aminophospholipid flippase 12 {ECO:0000303|PubMed:11402198};
GN Name=ALA12 {ECO:0000303|PubMed:11402198};
GN OrderedLocusNames=At1g26130 {ECO:0000312|Araport:AT1G26130};
GN ORFNames=F14G11.10, F28B23.19 {ECO:0000312|EMBL:AAG50692.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11402198; DOI=10.1104/pp.126.2.696;
RA Axelsen K.B., Palmgren M.G.;
RT "Inventory of the superfamily of P-type ion pumps in Arabidopsis.";
RL Plant Physiol. 126:696-706(2001).
CC -!- FUNCTION: Involved in transport of phospholipids.
CC {ECO:0000305|PubMed:11402198}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000305|PubMed:11402198};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=P57792-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50529.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC079829; AAG50692.1; -; Genomic_DNA.
DR EMBL; AC084221; AAG50529.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30652.1; -; Genomic_DNA.
DR PIR; D86387; D86387.
DR RefSeq; NP_001319082.1; NM_001332685.1. [P57792-1]
DR AlphaFoldDB; P57792; -.
DR SMR; P57792; -.
DR STRING; 3702.AT1G26130.2; -.
DR iPTMnet; P57792; -.
DR PaxDb; P57792; -.
DR PRIDE; P57792; -.
DR ProteomicsDB; 244899; -. [P57792-1]
DR EnsemblPlants; AT1G26130.1; AT1G26130.1; AT1G26130. [P57792-1]
DR GeneID; 839154; -.
DR Gramene; AT1G26130.1; AT1G26130.1; AT1G26130. [P57792-1]
DR KEGG; ath:AT1G26130; -.
DR Araport; AT1G26130; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR InParanoid; P57792; -.
DR PhylomeDB; P57792; -.
DR BioCyc; ARA:AT1G26130-MON; -.
DR PRO; PR:P57792; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P57792; baseline and differential.
DR Genevisible; P57792; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW Alternative splicing; ATP-binding; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1184
FT /note="Probable phospholipid-transporting ATPase 12"
FT /id="PRO_0000046396"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..364
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..921
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 922..941
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 942..955
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 956..975
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 976..1005
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1006..1028
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1029..1041
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1042..1064
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1065..1070
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1071..1091
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1092..1108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1109..1133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1134..1184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 430
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 866
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 870
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1184 AA; 133793 MW; D9B6BC0C79CDAE74 CRC64;
MATVSGRRRK RKIQLSKLFT LTGAKACFKP DHSKIGRSGF SRVVFCNQPD SPEAESRNYC
DNYVRTTKYT LATFLPKSLF EQFRRVANFY FLVVGILSFT PLAPYTAVSA IVPLTFVILA
TMFKEGVEDW RRKQQDIEVN NRKVRVHRGN GNFDLREWKT LRVGDILKVE KNEFFPADLV
LLSSSYEDAV CYVETMNLDG ETNLKLKQGL EVTLSLREEL NFRDFEAFIK CEDPNANLYS
FVGTMDLKGE KYPLSPQQLL LRGSKLRNTD YIYGVVIFTG PDTKVVQNST DPPSKRSMIE
RKMDKIIYLM FLMVFSLAFF GSVLFGIWTR DDFQNGVMER WYLKPDDSSI FFDPKRAPMA
AIYHFLTALM LNSYFIPISL YVSIEIVKVL QSIFINQDIH MYYEEADKPA HARTSNLNEE
LGQVGTILSD KTGTLTCNSM EFIKCSIAGT AYGRGVTEVE MAMDKRKGSA LVNQSNGNST
EDAVAAEPAV KGFNFRDERI MDGNWVTETH ADVIQKFFQL LAVCHTVIPE VDEDTGKISY
EAESPDEAAF VIAARELGFE FFTRTQTTIS VRELDLVTGE RVERLYSVLN VLEFSSSKKR
MSVIVQDQDG KLLLLCKGAD SVMFERLSES GRKYEKETRD HVNEYADAGL RTLILAYREL
DENEYEVFTE RISEAKNSVS ADREALIDEV TEKIEKNLVL LGATAVEDKL QNGVPDCINK
LAQAGIKIWV LTGDKMETAI NIGFACSLLR RDMKQIIINL ETPEIQQLEK SGEKDAIAAL
KENVLHQITS GKAQLKASGG NAKAFALIID GKSLAYALEE DMKGIFLELA IGCASVICCR
SSPKQKALVT RLVKTGSGQT TLAIGDGAND VGMLQEADIG VGISGVEGMQ AVMSSDIAIA
QFRYLERLLL VHGHWCYRRI SKMICYFFYK NITFGFTLFL YEAYTSFSAT PAYNDWYLSL
YSVFFTSLPV ICLGIFDQDV SAPFCLKFPV LYQEGVQNLL FSWRRILSWM FHGFCSAIII
FFLCKTSLES QAFNHEGKTA GRDILGGTMY TCVVWVVSLQ MVLTISYFTL IQHVVVWGSV
VIWYLFLMVY GSLPIRMSTD AYMVFLEALA PAPSYWITTL FVVLSTMMPY FIFSAIQMRF
FPMSHGTVQL LRYEDQCSNS GNFEMGRQGS VRPTLVMRSH QPES
