AT10A_HUMAN
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 03-AUG-2022, entry version 204.
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 -!- 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.ENSP00000349325; -.
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; O60312; -.
DR PeptideAtlas; O60312; -.
DR PRIDE; O60312; -.
DR ProteomicsDB; 49339; -. [O60312-1]
DR ProteomicsDB; 62126; -.
DR Antibodypedia; 58541; 22 antibodies from 12 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 CTD; 57194; -.
DR DisGeNET; 57194; -.
DR GeneCards; ATP10A; -.
DR GeneReviews; ATP10A; -.
DR HGNC; HGNC:13542; ATP10A.
DR HPA; ENSG00000206190; Tissue enhanced (brain).
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; 587717at2759; -.
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; 22 hits in 1071 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 160 other tissues.
DR ExpressionAtlas; O60312; baseline and differential.
DR Genevisible; O60312; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
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: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 Gene3D; 3.40.1110.10; -; 2.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR030357; ATP10A.
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 PANTHER; PTHR24092:SF81; PTHR24092:SF81; 1.
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; 2.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
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 1031
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
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; unknown pathological 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
