ID   AT10A_HUMAN             Reviewed;        1499 AA.
AC   O60312; Q4G0S9; Q969I4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-2002, sequence version 2.
DT   24-JAN-2024, entry version 211.
DE   RecName: Full=Phospholipid-transporting ATPase VA;
DE            EC=7.6.2.1 {ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:29599178};
DE   AltName: Full=ATPase class V type 10A;
DE   AltName: Full=Aminophospholipid translocase VA;
DE   AltName: Full=P4-ATPase flippase complex alpha subunit ATP10A;
GN   Name=ATP10A {ECO:0000303|PubMed:25947375};
GN   Synonyms=ATP10C, ATPVA, ATPVC, KIAA0566;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=11326269; DOI=10.1038/ng0501-19;
RA   Meguro M., Kashiwagi A., Mitsuya K., Nakao M., Kondo I., Saitoh S.,
RA   Oshimura M.;
RT   "A novel maternally expressed gene, ATP10C, encodes a putative
RT   aminophospholipid translocase associated with Angelman syndrome.";
RL   Nat. Genet. 28:19-20(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11353404; DOI=10.1086/320616;
RA   Herzing L.B.K., Kim S.-J., Cook E.H. Jr., Ledbetter D.H.;
RT   "The human aminophospholipid-transporting ATPase gene ATP10C maps adjacent
RT   to UBE3A and exhibits similar imprinted expression.";
RL   Am. J. Hum. Genet. 68:1501-1505(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Skin, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-1499 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA   Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA   Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. IX. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:31-39(1998).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=21914794; DOI=10.1074/jbc.m111.281006;
RA   Takatsu H., Baba K., Shima T., Umino H., Kato U., Umeda M., Nakayama K.,
RA   Shin H.W.;
RT   "ATP9B, a P4-ATPase (a putative aminophospholipid translocase), localizes
RT   to the trans-Golgi network in a CDC50 protein-independent manner.";
RL   J. Biol. Chem. 286:38159-38167(2011).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH
RP   TMEM30A, AND MUTAGENESIS OF GLU-203.
RX   PubMed=25947375; DOI=10.1074/jbc.m115.655191;
RA   Naito T., Takatsu H., Miyano R., Takada N., Nakayama K., Shin H.W.;
RT   "Phospholipid Flippase ATP10A Translocates Phosphatidylcholine and Is
RT   Involved in Plasma Membrane Dynamics.";
RL   J. Biol. Chem. 290:15004-15017(2015).
RN   [8]
RP   VARIANT TRP-208.
RX   PubMed=26637798; DOI=10.1016/j.neuron.2015.11.009;
RA   D'Gama A.M., Pochareddy S., Li M., Jamuar S.S., Reiff R.E., Lam A.T.,
RA   Sestan N., Walsh C.A.;
RT   "Targeted DNA Sequencing from Autism Spectrum Disorder Brains Implicates
RT   Multiple Genetic Mechanisms.";
RL   Neuron 88:910-917(2015).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP   GLU-203.
RX   PubMed=29599178; DOI=10.15252/embj.201797705;
RA   Takada N., Naito T., Inoue T., Nakayama K., Takatsu H., Shin H.W.;
RT   "Phospholipid-flipping activity of P4-ATPase drives membrane curvature.";
RL   EMBO J. 37:0-0(2018).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   98-ASN-PHE-99 AND GLU-203.
RX   PubMed=30530492; DOI=10.1074/jbc.ra118.005876;
RA   Roland B.P., Naito T., Best J.T., Arnaiz-Yepez C., Takatsu H., Yu R.J.,
RA   Shin H.W., Graham T.R.;
RT   "Yeast and human P4-ATPases transport glycosphingolipids using conserved
RT   structural motifs.";
RL   J. Biol. Chem. 294:1794-1806(2019).
CC   -!- FUNCTION: Catalytic component of P4-ATPase flippase complex, which
CC       catalyzes the hydrolysis of ATP coupled to the transport of
CC       phosphatidylcholine (PC) from the outer to the inner leaflet of the
CC       plasma membrane (PubMed:25947375, PubMed:29599178, PubMed:30530492).
CC       Initiates inward plasma membrane bending and recruitment of
CC       Bin/amphiphysin/Rvs (BAR) domain-containing proteins involved in
CC       membrane tubulation and cell trafficking (PubMed:29599178). Facilitates
CC       ITGB1/beta1 integrin endocytosis, delaying cell adhesion and cell
CC       spreading on extracellular matrix (PubMed:29599178, PubMed:25947375).
CC       Has low flippase activity toward glucosylceramide (GlcCer)
CC       (PubMed:30530492). {ECO:0000269|PubMed:25947375,
CC       ECO:0000269|PubMed:29599178, ECO:0000269|PubMed:30530492}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC         phospholipidSide 2.; EC=7.6.2.1;
CC         Evidence={ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:29599178,
CC         ECO:0000269|PubMed:30530492};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a
CC         1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate;
CC         Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:25947375,
CC         ECO:0000269|PubMed:29599178, ECO:0000269|PubMed:30530492};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38584;
CC         Evidence={ECO:0000305|PubMed:25947375, ECO:0000305|PubMed:29599178,
CC         ECO:0000305|PubMed:30530492};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(out) + ATP +
CC         H2O = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(in) + ADP +
CC         H(+) + phosphate; Xref=Rhea:RHEA:66036, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:22801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:30530492};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66037;
CC         Evidence={ECO:0000305|PubMed:30530492};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y2Q0};
CC   -!- ACTIVITY REGULATION: Inhibited under hypotonic conditions.
CC       {ECO:0000269|PubMed:29599178}.
CC   -!- SUBUNIT: Component of a P4-ATPase flippase complex which consists of a
CC       catalytic alpha subunit ATP10A and an accessory beta subunit TMEM30A.
CC       {ECO:0000269|PubMed:25947375}.
CC   -!- INTERACTION:
CC       O60312; Q9NV96: TMEM30A; NbExp=3; IntAct=EBI-26444318, EBI-2836942;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21914794,
CC       ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:30530492}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:21914794}. Endoplasmic reticulum
CC       membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:25947375}.
CC       Note=Exit from the endoplasmic reticulum requires the presence of
CC       TMEM30A, but not that of TMEM30B.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O60312-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O60312-2; Sequence=VSP_056604, VSP_056605;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in kidney,
CC       followed by lung, brain, prostate, testis, ovary and small intestine.
CC   -!- PTM: Autophosphorylated at the conserved aspartate of the P-type ATPase
CC       signature sequence. {ECO:0000250|UniProtKB:O94823}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IV subfamily. {ECO:0000305}.
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DR   EMBL; AB051358; BAB47392.1; -; mRNA.
DR   EMBL; AY029504; AAK33100.1; -; Genomic_DNA.
DR   EMBL; AY029487; AAK33100.1; JOINED; Genomic_DNA.
DR   EMBL; AY029488; AAK33100.1; JOINED; Genomic_DNA.
DR   EMBL; AY029489; AAK33100.1; JOINED; Genomic_DNA.
DR   EMBL; AY029490; AAK33100.1; JOINED; Genomic_DNA.
DR   EMBL; AY029491; AAK33100.1; JOINED; Genomic_DNA.
DR   EMBL; AY029492; AAK33100.1; JOINED; Genomic_DNA.
DR   EMBL; AY029493; AAK33100.1; JOINED; Genomic_DNA.
DR   EMBL; AY029494; AAK33100.1; JOINED; Genomic_DNA.
DR   EMBL; AY029495; AAK33100.1; JOINED; Genomic_DNA.
DR   EMBL; AY029496; AAK33100.1; JOINED; Genomic_DNA.
DR   EMBL; AY029497; AAK33100.1; JOINED; Genomic_DNA.
DR   EMBL; AY029498; AAK33100.1; JOINED; Genomic_DNA.
DR   EMBL; AY029499; AAK33100.1; JOINED; Genomic_DNA.
DR   EMBL; AY029500; AAK33100.1; JOINED; Genomic_DNA.
DR   EMBL; AY029501; AAK33100.1; JOINED; Genomic_DNA.
DR   EMBL; AY029502; AAK33100.1; JOINED; Genomic_DNA.
DR   EMBL; AY029503; AAK33100.1; JOINED; Genomic_DNA.
DR   EMBL; AC016266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC023449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC109512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC052251; AAH52251.1; -; mRNA.
DR   EMBL; BC038712; AAH38712.1; -; mRNA.
DR   EMBL; AB011138; BAA25492.1; -; mRNA.
DR   CCDS; CCDS32178.1; -. [O60312-1]
DR   RefSeq; NP_077816.1; NM_024490.3. [O60312-1]
DR   RefSeq; XP_005268318.1; XM_005268261.4. [O60312-1]
DR   RefSeq; XP_011520128.1; XM_011521826.2. [O60312-1]
DR   AlphaFoldDB; O60312; -.
DR   SMR; O60312; -.
DR   BioGRID; 121443; 8.
DR   ComplexPortal; CPX-6307; ATP10A-CDC50A P4-ATPase complex.
DR   IntAct; O60312; 1.
DR   STRING; 9606.ENSP00000450480; -.
DR   TCDB; 3.A.3.8.26; the p-type atpase (p-atpase) superfamily.
DR   iPTMnet; O60312; -.
DR   PhosphoSitePlus; O60312; -.
DR   BioMuta; ATP10A; -.
DR   jPOST; O60312; -.
DR   MassIVE; O60312; -.
DR   PaxDb; 9606-ENSP00000349325; -.
DR   PeptideAtlas; O60312; -.
DR   ProteomicsDB; 49339; -. [O60312-1]
DR   ProteomicsDB; 62126; -.
DR   Antibodypedia; 58541; 29 antibodies from 13 providers.
DR   DNASU; 57194; -.
DR   Ensembl; ENST00000356865.11; ENSP00000349325.6; ENSG00000206190.13. [O60312-1]
DR   Ensembl; ENST00000389967.9; ENSP00000374617.4; ENSG00000206190.13. [O60312-2]
DR   Ensembl; ENST00000555815.7; ENSP00000450480.2; ENSG00000206190.13. [O60312-1]
DR   Ensembl; ENST00000619904.1; ENSP00000480665.1; ENSG00000206190.13. [O60312-2]
DR   GeneID; 57194; -.
DR   KEGG; hsa:57194; -.
DR   MANE-Select; ENST00000555815.7; ENSP00000450480.2; NM_024490.4; NP_077816.1.
DR   UCSC; uc001zax.4; human. [O60312-1]
DR   AGR; HGNC:13542; -.
DR   CTD; 57194; -.
DR   DisGeNET; 57194; -.
DR   GeneCards; ATP10A; -.
DR   GeneReviews; ATP10A; -.
DR   HGNC; HGNC:13542; ATP10A.
DR   HPA; ENSG00000206190; Low tissue specificity.
DR   MalaCards; ATP10A; -.
DR   MIM; 605855; gene.
DR   neXtProt; NX_O60312; -.
DR   OpenTargets; ENSG00000206190; -.
DR   Orphanet; 411515; Angelman syndrome due to imprinting defect in 15q11-q13.
DR   PharmGKB; PA25097; -.
DR   VEuPathDB; HostDB:ENSG00000206190; -.
DR   eggNOG; KOG0206; Eukaryota.
DR   GeneTree; ENSGT00940000157895; -.
DR   HOGENOM; CLU_000846_3_4_1; -.
DR   InParanoid; O60312; -.
DR   OMA; QALRCGR; -.
DR   OrthoDB; 275833at2759; -.
DR   PhylomeDB; O60312; -.
DR   TreeFam; TF354252; -.
DR   BRENDA; 7.6.2.1; 2681.
DR   PathwayCommons; O60312; -.
DR   Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR   SignaLink; O60312; -.
DR   BioGRID-ORCS; 57194; 23 hits in 1149 CRISPR screens.
DR   ChiTaRS; ATP10A; human.
DR   GeneWiki; ATP10A; -.
DR   GenomeRNAi; 57194; -.
DR   Pharos; O60312; Tbio.
DR   PRO; PR:O60312; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; O60312; Protein.
DR   Bgee; ENSG00000206190; Expressed in endothelial cell and 162 other cell types or tissues.
DR   ExpressionAtlas; O60312; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:1990531; C:phospholipid-translocating ATPase complex; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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:0140351; F:glycosylceramide flippase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0140345; F:phosphatidylcholine flippase activity; IDA:UniProtKB.
DR   GO; GO:0090554; F:phosphatidylcholine floppase activity; IEA:RHEA.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; TAS:Reactome.
DR   GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR   GO; GO:1903527; P:positive regulation of membrane tubulation; IDA:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; NAS:UniProtKB.
DR   CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; 2.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR24092:SF81; PHOSPHOLIPID-TRANSPORTING ATPASE VA; 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.
DR   Genevisible; O60312; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell membrane; Endoplasmic reticulum;
KW   Lipid transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1499
FT                   /note="Phospholipid-transporting ATPase VA"
FT                   /id="PRO_0000046379"
FT   TOPO_DOM        1..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        107..110
FT                   /note="Exoplasmic loop"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..309
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..362
FT                   /note="Exoplasmic loop"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        385..1087
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1088..1108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1109..1119
FT                   /note="Exoplasmic loop"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1120..1140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1141..1170
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1171..1192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1193..1199
FT                   /note="Exoplasmic loop"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1200..1222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1223..1228
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1229..1249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1250..1267
FT                   /note="Exoplasmic loop"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1268..1292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1293..1499
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          464..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1311..1356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1464..1499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1340..1356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        427
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HD20"
FT   BINDING         427
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         427
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         428
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         429
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         429
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         700
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         742
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         766
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         809
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         889
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         890
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         891
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         1005
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         1011
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         1031
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT   BINDING         1034
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         1035
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         1035
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT   MOD_RES         466
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O54827"
FT   VAR_SEQ         150..155
FT                   /note="REEKKY -> SRSHLK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056604"
FT   VAR_SEQ         156..1499
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056605"
FT   VARIANT         208
FT                   /note="R -> W (found in a patient with autism and
FT                   Parkinson's disease; uncertain significance;
FT                   dbSNP:rs763246380)"
FT                   /evidence="ECO:0000269|PubMed:26637798"
FT                   /id="VAR_078700"
FT   VARIANT         353
FT                   /note="S -> Y (in dbSNP:rs17116056)"
FT                   /id="VAR_048380"
FT   VARIANT         504
FT                   /note="R -> H (in dbSNP:rs56724944)"
FT                   /id="VAR_061038"
FT   VARIANT         532
FT                   /note="T -> M (in dbSNP:rs2066703)"
FT                   /id="VAR_022004"
FT   VARIANT         784
FT                   /note="A -> T (in dbSNP:rs2066704)"
FT                   /id="VAR_022005"
FT   VARIANT         834
FT                   /note="E -> K (in dbSNP:rs17555920)"
FT                   /id="VAR_048381"
FT   VARIANT         1172
FT                   /note="W -> C (in dbSNP:rs2076742)"
FT                   /id="VAR_022006"
FT   VARIANT         1179
FT                   /note="A -> T (in dbSNP:rs2076744)"
FT                   /id="VAR_022007"
FT   VARIANT         1188
FT                   /note="I -> V (in dbSNP:rs2076745)"
FT                   /id="VAR_022008"
FT   VARIANT         1198
FT                   /note="V -> M (in dbSNP:rs2076746)"
FT                   /id="VAR_048382"
FT   VARIANT         1298
FT                   /note="R -> S (in dbSNP:rs3816800)"
FT                   /id="VAR_022009"
FT   VARIANT         1397
FT                   /note="A -> V (in dbSNP:rs9324127)"
FT                   /id="VAR_048383"
FT   MUTAGEN         98..99
FT                   /note="NF->QA: Decreases PC-flipping activity."
FT                   /evidence="ECO:0000269|PubMed:30530492"
FT   MUTAGEN         203
FT                   /note="E->Q: Impairs PC-flipping activity."
FT                   /evidence="ECO:0000269|PubMed:25947375,
FT                   ECO:0000269|PubMed:29599178, ECO:0000269|PubMed:30530492"
FT   CONFLICT        388
FT                   /note="Q -> R (in Ref. 5; BAA25492)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1499 AA;  167688 MW;  D4996A4D0635A68D CRC64;
     MEREPAGTEE PGPPGRRRRR EGRTRTVRSN LLPPPGAEDP AAGAAKGERR RRRGCAQHLA
     DNRLKTTKYT LLSFLPKNLF EQFHRPANVY FVFIALLNFV PAVNAFQPGL ALAPVLFILA
     ITAFRDLWED YSRHRSDHKI NHLGCLVFSR EEKKYVNRFW KEIHVGDFVR LRCNEIFPAD
     ILLLSSSDPD GLCHIETANL DGETNLKRRQ VVRGFSELVS EFNPLTFTSV IECEKPNNDL
     SRFRGCIIHD NGKKAGLYKE NLLLRGCTLR NTDAVVGIVI YAGHETKALL NNSGPRYKRS
     KLERQMNCDV LWCVLLLVCM SLFSAVGHGL WIWRYQEKKS LFYVPKSDGS SLSPVTAAVY
     SFLTMIIVLQ VLIPISLYVS IEIVKACQVY FINQDMQLYD EETDSQLQCR ALNITEDLGQ
     IQYIFSDKTG TLTENKMVFR RCTVSGVEYS HDANAQRLAR YQEADSEEEE VVPRGGSVSQ
     RGSIGSHQSV RVVHRTQSTK SHRRTGSRAE AKRASMLSKH TAFSSPMEKD ITPDPKLLEK
     VSECDKSLAV ARHQEHLLAH LSPELSDVFD FFIALTICNT VVVTSPDQPR TKVRVRFELK
     SPVKTIEDFL RRFTPSCLTS GCSSIGSLAA NKSSHKLGSS FPSTPSSDGM LLRLEERLGQ
     PTSAIASNGY SSQADNWASE LAQEQESERE LRYEAESPDE AALVYAARAY NCVLVERLHD
     QVSVELPHLG RLTFELLHTL GFDSVRKRMS VVIRHPLTDE INVYTKGADS VVMDLLQPCS
     SVDARGRHQK KIRSKTQNYL NVYAAEGLRT LCIAKRVLSK EEYACWLQSH LEAESSLENS
     EELLFQSAIR LETNLHLLGA TGIEDRLQDG VPETISKLRQ AGLQIWVLTG DKQETAVNIA
     YACKLLDHDE EVITLNATSQ EACAALLDQC LCYVQSRGLQ RAPEKTKGKV SMRFSSLCPP
     STSTASGRRP SLVIDGRSLA YALEKNLEDK FLFLAKQCRS VLCCRSTPLQ KSMVVKLVRS
     KLKAMTLAIG DGANDVSMIQ VADVGVGISG QEGMQAVMAS DFAVPKFRYL ERLLILHGHW
     CYSRLANMVL YFFYKNTMFV GLLFWFQFFC GFSASTMIDQ WYLIFFNLLF SSLPPLVTGV
     LDRDVPANVL LTNPQLYKSG QNMEEYRPRT FWFNMADAAF QSLVCFSIPY LAYYDSNVDL
     FTWGTPIVTI ALLTFLLHLG IETKTWTWLN WITCGFSVLL FFTVALIYNA SCATCYPPSN
     PYWTMQALLG DPVFYLTCLM TPVAALLPRL FFRSLQGRVF PTQLQLARQL TRKSPRRCSA
     PKETFAQGRL PKDSGTEHSS GRTVKTSVPL SQPSWHTQQP VCSLEASGEP STVDMSMPVR
     EHTLLEGLSA PAPMSSAPGE AVLRSPGGCP EESKVRAAST GRVTPLSSLF SLPTFSLLNW
     ISSWSLVSRL GSVLQFSRTE QLADGQAGRG LPVQPHSGRS GLQGPDHRLL IGASSRRSQ
//