AT8A1_MOUSE
ID AT8A1_MOUSE Reviewed; 1164 AA.
AC P70704; Q8BR88;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Phospholipid-transporting ATPase IA {ECO:0000305};
DE EC=7.6.2.1 {ECO:0000269|PubMed:20224745};
DE AltName: Full=ATPase class I type 8A member 1;
DE AltName: Full=Chromaffin granule ATPase II;
DE AltName: Full=P4-ATPase flippase complex alpha subunit ATP8A1;
GN Name=Atp8a1 {ECO:0000312|MGI:MGI:1330848}; Synonyms=Atpc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Teratocarcinoma;
RX PubMed=9548971; DOI=10.1101/gr.8.4.354;
RA Halleck M.S., Pradhan D., Blackman C.F., Berkes C., Williamson P.L.,
RA Schlegel R.A.;
RT "Multiple members of a third subfamily of P-type ATPases identified by
RT genomic sequences and ESTs.";
RL Genome Res. 8:354-361(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=16618126; DOI=10.1021/bi052359b;
RA Paterson J.K., Renkema K., Burden L., Halleck M.S., Schlegel R.A.,
RA Williamson P., Daleke D.L.;
RT "Lipid specific activation of the murine P4-ATPase Atp8a1 (ATPase II).";
RL Biochemistry 45:5367-5376(2006).
RN [5]
RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16643453; DOI=10.1111/j.1365-2141.2006.06051.x;
RA Soupene E., Kuypers F.A.;
RT "Identification of an erythroid ATP-dependent aminophospholipid
RT transporter.";
RL Br. J. Haematol. 133:436-438(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-28 AND SER-29, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=20224745; DOI=10.2147/jrlcr.s3773;
RA Soupene E., Kemaladewi D.U., Kuypers F.A.;
RT "ATP8A1 activity and phosphatidylserine transbilayer movement.";
RL J. Recept. Lig. Chann. Res. 1:1-10(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; THR-28 AND SER-29, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; THR-28; SER-29; SER-443
RP AND SER-1126, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF ASP-409.
RX PubMed=22007859; DOI=10.1111/j.1471-4159.2011.07543.x;
RA Levano K., Punia V., Raghunath M., Debata P.R., Curcio G.M., Mogha A.,
RA Purkayastha S., McCloskey D., Fata J., Banerjee P.;
RT "Atp8a1 deficiency is associated with phosphatidylserine externalization in
RT hippocampus and delayed hippocampus-dependent learning.";
RL J. Neurochem. 120:302-313(2012).
RN [11]
RP FUNCTION, FUNCTION OF THE ATP8A1:TMEM30A COMPLEX, AND INTERACTION WITH
RP TMEM30A.
RX PubMed=23269685; DOI=10.1074/jbc.m112.402701;
RA Kato U., Inadome H., Yamamoto M., Emoto K., Kobayashi T., Umeda M.;
RT "Role for phospholipid flippase complex of ATP8A1 and CDC50A proteins in
RT cell migration.";
RL J. Biol. Chem. 288:4922-4934(2013).
RN [12]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND
RP FUNCTION.
RX PubMed=27287255; DOI=10.1016/j.bbadis.2016.06.005;
RA Kerr D.J., Marsillo A., Guariglia S.R., Budylin T., Sadek R., Menkes S.,
RA Chauhan A., Wen G.Y., McCloskey D.P., Wieraszko A., Banerjee P.;
RT "Aberrant hippocampal Atp8a1 levels are associated with altered synaptic
RT strength, electrical activity, and autistic-like behavior.";
RL Biochim. Biophys. Acta 1862:1755-1765(2016).
RN [13]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND PROCESSING BY CALPAIN.
RX PubMed=30674456; DOI=10.1182/bloodadvances.2018023473;
RA Jing W., Yabas M., Broeer A., Coupland L., Gardiner E.E., Enders A.,
RA Broeer S.;
RT "Calpain cleaves phospholipid flippase ATP8A1 during apoptosis in
RT platelets.";
RL Blood Adv. 3:219-229(2019).
CC -!- FUNCTION: Catalytic component of a P4-ATPase flippase complex which
CC catalyzes the hydrolysis of ATP coupled to the transport of
CC aminophospholipids from the outer to the inner leaflet of various
CC membranes and ensures the maintenance of asymmetric distribution of
CC phospholipids (PubMed:20224745, PubMed:16618126). Phospholipid
CC translocation seems also to be implicated in vesicle formation and in
CC uptake of lipid signaling molecules. In vitro, its ATPase activity is
CC selectively and stereospecifically stimulated by phosphatidylserine
CC (PS) (PubMed:20224745, PubMed:16618126). The flippase complex
CC ATP8A1:TMEM30A seems to play a role in regulation of cell migration
CC probably involving flippase-mediated translocation of
CC phosphatidylethanolamine (PE) at the plasma membrane (PubMed:23269685).
CC Acts as aminophospholipid translocase at the plasma membrane in
CC neuronal cells; the activity is associated with hippocampus-dependent
CC learning (PubMed:22007859). May play a role in brain connectivity
CC (PubMed:27287255). {ECO:0000269|PubMed:16618126,
CC ECO:0000269|PubMed:20224745, ECO:0000269|PubMed:22007859,
CC ECO:0000269|PubMed:23269685, ECO:0000269|PubMed:27287255}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000269|PubMed:20224745};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O =
CC a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:20224745};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568;
CC Evidence={ECO:0000305|PubMed:20224745};
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by
CC phosphatidylserine (PS) and minimally by phosphatidylethanolamine (PE)
CC (PubMed:16618126, PubMed:20224745). ATPase activity is inhibited by the
CC vanadate and by the presence of calcium (PubMed:20224745).
CC {ECO:0000269|PubMed:16618126, ECO:0000269|PubMed:20224745}.
CC -!- SUBUNIT: Component of a P4-ATPase flippase complex which consists of a
CC catalytic alpha subunit and an accessory beta subunit
CC (PubMed:23269685). Interacts with TMEM30A to form a flippase complex;
CC this complex forms an intermediate phosphoenzyme (PubMed:23269685).
CC Interacts with TMEM30B; this interaction is reported conflictingly (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y2Q0,
CC ECO:0000269|PubMed:23269685}.
CC -!- INTERACTION:
CC P70704; Q8VEK0: Tmem30a; NbExp=2; IntAct=EBI-20828407, EBI-8381028;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC chromaffin granule membrane {ECO:0000269|PubMed:16643453}; Multi-pass
CC membrane protein {ECO:0000255}. Cytoplasmic granule
CC {ECO:0000269|PubMed:16643453}. Cell membrane
CC {ECO:0000269|PubMed:27287255}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9Y2Q0}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9Y2Q0}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:20224745, ECO:0000269|PubMed:27287255}.
CC Endomembrane system {ECO:0000269|PubMed:30674456}. Note=Exit from the
CC endoplasmic reticulum requires the presence of TMEM30A, but not
CC TMEM30B. In the presence of TMEM30A, predominantly located in
CC cytoplasmic punctate structures (By similarity). Localizes to plasma
CC membranes of red blood cells (PubMed:16643453). Localizes predominantly
CC in the intracellular membranes, rather than the plasma membrane of
CC platelets (PubMed:30674456). {ECO:0000250, ECO:0000269|PubMed:16643453,
CC ECO:0000269|PubMed:30674456}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P70704-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P70704-2; Sequence=VSP_055306, VSP_055307;
CC Name=3;
CC IsoId=P70704-3; Sequence=VSP_055307;
CC -!- TISSUE SPECIFICITY: Found in most tissues except liver and testis. Most
CC abundant in brain and lung. Also detected in fetal tissues. Isoform 1
CC is expressed in brain. Isoform 2 and isoform 3 are expressed in
CC reticulocytes (PubMed:16643453). Expressed in mouse hippocampus in both
CC dentate gyrus (DG) and the CA3 regions. Expressed in both neuronal as
CC well as non-neuronal cells within the DG (PubMed:27287255). Highly
CC expressed in platelets (PubMed:30674456). {ECO:0000269|PubMed:16643453,
CC ECO:0000269|PubMed:27287255, ECO:0000269|PubMed:30674456}.
CC -!- PTM: Cleaved by calpain in a caspase- and calcium influx-dependent
CC manner only during platelet apoptosis and may lead to inactivation.
CC {ECO:0000269|PubMed:30674456}.
CC -!- DISRUPTION PHENOTYPE: Mice overexpressing ATP8A1 in brain display an
CC autistic-like behavior but no difference in hippocampus-dependent
CC learning. Unlike the mice overexpressing ATP8A1,homozygous knockout
CC mice for ATP8A1 do not show any deficits in sociability behavior.
CC {ECO:0000269|PubMed:27287255}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
CC -!- CAUTION: Initial characterization studies with purified Atp8a1 enzyme
CC demonstrated similar but distinct properties compared to the plasma
CC membrane aminophospholipid flippase; however, the flippase complex
CC accessory beta subunit was not included in the assays.
CC {ECO:0000305|PubMed:16618126}.
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DR EMBL; U75321; AAB18627.1; -; mRNA.
DR EMBL; AK045367; BAC32330.1; -; mRNA.
DR EMBL; AK141559; BAE24734.1; -; mRNA.
DR EMBL; AC102916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC123662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS39104.1; -. [P70704-1]
DR CCDS; CCDS39105.1; -. [P70704-2]
DR PIR; T30869; T30869.
DR RefSeq; NP_001034088.1; NM_001038999.2. [P70704-1]
DR RefSeq; NP_001271274.1; NM_001284345.1.
DR RefSeq; NP_033857.1; NM_009727.3. [P70704-2]
DR AlphaFoldDB; P70704; -.
DR SMR; P70704; -.
DR BioGRID; 198270; 11.
DR IntAct; P70704; 1.
DR STRING; 10090.ENSMUSP00000042215; -.
DR SwissLipids; SLP:000000333; -.
DR iPTMnet; P70704; -.
DR PhosphoSitePlus; P70704; -.
DR EPD; P70704; -.
DR jPOST; P70704; -.
DR MaxQB; P70704; -.
DR PaxDb; P70704; -.
DR PeptideAtlas; P70704; -.
DR PRIDE; P70704; -.
DR ProteomicsDB; 265131; -. [P70704-1]
DR ProteomicsDB; 265132; -. [P70704-2]
DR ProteomicsDB; 265133; -. [P70704-3]
DR Antibodypedia; 43947; 88 antibodies from 19 providers.
DR DNASU; 11980; -.
DR Ensembl; ENSMUST00000037380; ENSMUSP00000042215; ENSMUSG00000037685. [P70704-1]
DR Ensembl; ENSMUST00000135930; ENSMUSP00000118379; ENSMUSG00000037685. [P70704-2]
DR GeneID; 11980; -.
DR KEGG; mmu:11980; -.
DR UCSC; uc008xqa.2; mouse. [P70704-1]
DR UCSC; uc008xqb.2; mouse. [P70704-2]
DR CTD; 10396; -.
DR MGI; MGI:1330848; Atp8a1.
DR VEuPathDB; HostDB:ENSMUSG00000037685; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000157110; -.
DR HOGENOM; CLU_000846_3_2_1; -.
DR InParanoid; P70704; -.
DR OMA; QFWYSFQ; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; P70704; -.
DR TreeFam; TF300654; -.
DR BRENDA; 7.6.2.1; 3474.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 11980; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Atp8a1; mouse.
DR PRO; PR:P70704; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P70704; protein.
DR Bgee; ENSMUSG00000037685; Expressed in left lung lobe and 265 other tissues.
DR ExpressionAtlas; P70704; baseline and differential.
DR Genevisible; P70704; MM.
DR GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031090; C:organelle membrane; IDA:UniProtKB.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; 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:0140346; F:phosphatidylserine flippase activity; IMP:ARUK-UCL.
DR GO; GO:0090556; F:phosphatidylserine floppase activity; IEA:RHEA.
DR GO; GO:0140331; P:aminophospholipid translocation; IMP:ARUK-UCL.
DR GO; GO:0007612; P:learning; IMP:UniProtKB.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0061092; P:positive regulation of phospholipid translocation; IDA:UniProtKB.
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; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Golgi apparatus; Lipid transport; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1164
FT /note="Phospholipid-transporting ATPase IA"
FT /id="PRO_0000046361"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..100
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..339
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..866
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 867..887
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 888..890
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 891..911
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 912..939
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 940..960
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 961..977
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 978..998
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 999..1008
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1009..1029
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1030..1044
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 1045..1065
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1066..1164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 409
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 409..411
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 409
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 411
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 549
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 741..748
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 801
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 804..805
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 805
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1095..1102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT SITE 139
FT /note="Cleavage; by calpain"
FT /evidence="ECO:0000305|PubMed:30674456"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 28
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 152..171
FT /note="AVGEIVKVTNGEHLPADLLS -> NVGDIVIIKGKEYIPADTVL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:9548971"
FT /id="VSP_055306"
FT VAR_SEQ 433..447
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:9548971"
FT /id="VSP_055307"
FT MUTAGEN 409
FT /note="D->K: Decreases plasma membrane aminophospholipid
FT translocation in neuronal cells."
FT /evidence="ECO:0000269|PubMed:22007859"
SQ SEQUENCE 1164 AA; 131413 MW; 2639DDDA00B15754 CRC64;
MPTMRRTVSE IRSRAEGYEK TDDVSEKTSL ADQEEVRTIF INQPQLTKFC NNHVSTAKYN
VITFLPRFLY SQFRRAANSF FLFIALLQQI PDVSPTGRYT TLVPLLFILA VAAIKEIIED
IKRHKADNAV NKKQTQVLRN GAWEIVHWEK VAVGEIVKVT NGEHLPADLL SLSSSEPQAM
CYIETSNLDG ETNLKIRQGL PATSDIKDID SLMRISGRIE CESPNRHLYD FVGNIRLDGH
GTVPLGADQI LLRGAQLRNT QWVHGIVVYT GHDTKLMQNS TSPPLKLSNV ERITNVQILI
LFCILIAMSL VCSVGSAIWN RRHSGKDWYL HLHYGGASNF GLNFLTFIIL FNNLIPISLL
VTLEVVKFTQ AYFINWDLDM HYEPTDTAAM ARTSNLNEEL GQVKYIFSDK TGTLTCNVMQ
FKKCTIAGVA YGHVPEPEDY GCSPDEWQSS QFGDEKTFND PSLLDNLQNN HPTAPIICEF
LTMMAVCHTA VPEREGDKII YQAASPDEGA LVRAAKQLNF VFTGRTPDSV IIDSLGQEER
YELLNVLEFT SARKRMSVVV RTPSGKLRLY CKGADTVIYE RLAETSKYKE ITLKHLEQFA
TEGLRTLCFA VAEISESDFE EWRAVYHRAS TSVQNRLLKL EESYELIEKN LQLLGATAIE
DKLQDQVPET IETLMKADIK IWILTGDKQE TAINIGHSCR LLKRNMGMIV INEGSLDGTR
ETLSRHCTTL GDALRKENDF ALIIDGKTLK YALTFGVRQY FLDLALSCKA VICCRVSPLQ
KSEVVEMVKK QVKVITLAIG DGANDVSMIQ TAHVGVGISG NEGLQAANSS DYSIAQFKYL
KNLLMVHGAW NYNRVSKCIL YCFYKNIVLY IIEIWFAFVN GFSGQILFER WCIGLYNVMF
TAMPPLTLGI FERSCRKENM LKYPELYKTS QNALDFNTKV FWVHCLNGLF HSVILFWFPL
KALQYGTVFG NGKTSDYLLL GNFVYTFVVI TVCLKAGLET SYWTWFSHIA IWGSIALWVV
FFGIYSSLWP AVPMAPDMSG EAAMLFSSGV FWVGLLSIPV ASLLLDVLYK VIKRTAFKTL
VDEVQELEAK SQDPGAVVLG KSLTERAQLL KNVFKKNHVN LYRSESLQQN LLHGYAFSQD
ENGIVSQSEV IRAYDTTKQR PDEW
