AT11B_HUMAN
ID AT11B_HUMAN Reviewed; 1177 AA.
AC Q9Y2G3; Q96FN1; Q9UKK7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Phospholipid-transporting ATPase IF;
DE EC=7.6.2.1 {ECO:0000269|PubMed:30018401};
DE AltName: Full=ATPase IR;
DE AltName: Full=ATPase class VI type 11B;
DE AltName: Full=P4-ATPase flippase complex alpha subunit ATP11B;
GN Name=ATP11B; Synonyms=ATPIF, ATPIR, KIAA0956;
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] OF 1-248.
RC TISSUE=Colon;
RX PubMed=11015572; DOI=10.1152/physiolgenomics.1999.1.3.139;
RA Halleck M.S., Lawler J.F. Jr., Blackshaw S., Gao L., Nagarajan P.,
RA Hacker C., Pyle S., Newman J.T., Nakanishi Y., Ando H., Weinstock D.,
RA Williamson P.L., Schlegel R.A.;
RT "Differential expression of putative transbilayer amphipath transporters.";
RL Physiol. Genomics 1:139-150(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-195 AND 540-1177.
RC TISSUE=Colon, and Mammary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 111-450.
RX PubMed=11790799; DOI=10.1074/jbc.m200240200;
RA Halleck M.S., Schlegel R.A., Williamson P.L.;
RT "Reanalysis of ATP11B, a Type IV P-type ATPase.";
RL J. Biol. Chem. 277:9736-9740(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 440-1111.
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 688-1111.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1154, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP INTERACTION WITH TMEM30A, AND 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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=23585472; DOI=10.1172/jci65425;
RA Moreno-Smith M., Halder J.B., Meltzer P.S., Gonda T.A., Mangala L.S.,
RA Rupaimoole R., Lu C., Nagaraja A.S., Gharpure K.M., Kang Y.,
RA Rodriguez-Aguayo C., Vivas-Mejia P.E., Zand B., Schmandt R., Wang H.,
RA Langley R.R., Jennings N.B., Ivan C., Coffin J.E., Armaiz G.N.,
RA Bottsford-Miller J., Kim S.B., Halleck M.S., Hendrix M.J., Bornman W.,
RA Bar-Eli M., Lee J.S., Siddik Z.H., Lopez-Berestein G., Sood A.K.;
RT "ATP11B mediates platinum resistance in ovarian cancer.";
RL J. Clin. Invest. 123:2119-2130(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1154, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1154, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, INTERACTION WITH TMEM30A, AND MUTAGENESIS OF GLU-180.
RX PubMed=30018401; DOI=10.1038/s41598-018-29108-z;
RA Wang J., Molday L.L., Hii T., Coleman J.A., Wen T., Andersen J.P.,
RA Molday R.S.;
RT "Proteomic Analysis and Functional Characterization of P4-ATPase
RT Phospholipid Flippases from Murine Tissues.";
RL Sci. Rep. 8:10795-10795(2018).
CC -!- FUNCTION: Catalytic component of a P4-ATPase flippase complex which
CC catalyzes the hydrolysis of ATP coupled to the transport of
CC aminophospholipids, phosphatidylserines (PS) and
CC phosphatidylethanolamines (PE), from the outer to the inner leaflet of
CC intracellular membranes (PubMed:30018401). May contribute to the
CC maintenance of membrane lipid asymmetry in endosome compartment
CC (PubMed:30018401). {ECO:0000269|PubMed:30018401}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000269|PubMed:30018401};
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:30018401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568;
CC Evidence={ECO:0000305|PubMed:30018401};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:30018401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000305|PubMed:30018401};
CC -!- ACTIVITY REGULATION: The ATPase activity is up-regulated by
CC aminophospholipids PS and PE. {ECO:0000269|PubMed:30018401}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=730 uM for ATP {ECO:0000269|PubMed:30018401};
CC Vmax=9.5 umol/min/mg enzyme toward ATP {ECO:0000269|PubMed:30018401};
CC Vmax=17.3 umol/min/mg enzyme toward ATP (in the presence of PS)
CC {ECO:0000269|PubMed:30018401};
CC Vmax=25.2 umol/min/mg enzyme toward ATP (in the presence of PE)
CC {ECO:0000269|PubMed:30018401};
CC -!- SUBUNIT: Component of a P4-ATPase flippase complex which consists of a
CC catalytic alpha subunit ATP11B and an accessory beta subunit TMEM30A.
CC {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:30018401}.
CC -!- INTERACTION:
CC Q9Y2G3; Q9NV96: TMEM30A; NbExp=2; IntAct=EBI-20857228, EBI-2836942;
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000269|PubMed:21914794}; Multi-pass membrane protein. Early
CC endosome {ECO:0000269|PubMed:23585472}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:21914794}. Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:23585472}. Note=Exit from the endoplasmic reticulum
CC requires the presence of TMEM30A, but not TMEM30B (PubMed:21914794). In
CC the presence of TMEM30A, mainly located in recycling endosomes
CC (PubMed:21914794). {ECO:0000269|PubMed:21914794}.
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=AAH10630.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH42180.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF156548; AAF09446.1; -; mRNA.
DR EMBL; AC069431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042180; AAH42180.1; ALT_SEQ; mRNA.
DR EMBL; BC010630; AAH10630.1; ALT_FRAME; mRNA.
DR EMBL; AB023173; BAA76800.1; -; mRNA.
DR EMBL; AL133061; CAB61385.1; -; mRNA.
DR CCDS; CCDS33896.1; -.
DR PIR; T42662; T42662.
DR RefSeq; NP_055431.1; NM_014616.2.
DR AlphaFoldDB; Q9Y2G3; -.
DR SMR; Q9Y2G3; -.
DR BioGRID; 116809; 7.
DR ComplexPortal; CPX-6311; ATP11B-CDC50A P4-ATPase complex.
DR IntAct; Q9Y2G3; 3.
DR STRING; 9606.ENSP00000321195; -.
DR TCDB; 3.A.3.8.12; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; Q9Y2G3; -.
DR PhosphoSitePlus; Q9Y2G3; -.
DR SwissPalm; Q9Y2G3; -.
DR BioMuta; ATP11B; -.
DR DMDM; 30316395; -.
DR EPD; Q9Y2G3; -.
DR jPOST; Q9Y2G3; -.
DR MassIVE; Q9Y2G3; -.
DR MaxQB; Q9Y2G3; -.
DR PaxDb; Q9Y2G3; -.
DR PeptideAtlas; Q9Y2G3; -.
DR PRIDE; Q9Y2G3; -.
DR ProteomicsDB; 85764; -.
DR Antibodypedia; 33765; 135 antibodies from 30 providers.
DR DNASU; 23200; -.
DR Ensembl; ENST00000323116.10; ENSP00000321195.5; ENSG00000058063.16.
DR GeneID; 23200; -.
DR KEGG; hsa:23200; -.
DR MANE-Select; ENST00000323116.10; ENSP00000321195.5; NM_014616.3; NP_055431.1.
DR UCSC; uc003fla.3; human.
DR CTD; 23200; -.
DR DisGeNET; 23200; -.
DR GeneCards; ATP11B; -.
DR HGNC; HGNC:13553; ATP11B.
DR HPA; ENSG00000058063; Low tissue specificity.
DR MIM; 605869; gene.
DR neXtProt; NX_Q9Y2G3; -.
DR OpenTargets; ENSG00000058063; -.
DR PharmGKB; PA25102; -.
DR VEuPathDB; HostDB:ENSG00000058063; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000156162; -.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; Q9Y2G3; -.
DR OMA; TMWWESH; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; Q9Y2G3; -.
DR TreeFam; TF326897; -.
DR PathwayCommons; Q9Y2G3; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR SignaLink; Q9Y2G3; -.
DR BioGRID-ORCS; 23200; 15 hits in 1073 CRISPR screens.
DR ChiTaRS; ATP11B; human.
DR GeneWiki; ATP11B; -.
DR GenomeRNAi; 23200; -.
DR Pharos; Q9Y2G3; Tbio.
DR PRO; PR:Q9Y2G3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y2G3; protein.
DR Bgee; ENSG00000058063; Expressed in calcaneal tendon and 206 other tissues.
DR ExpressionAtlas; Q9Y2G3; baseline and differential.
DR Genevisible; Q9Y2G3; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0031901; C:early endosome membrane; IDA:ComplexPortal.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IPI:ComplexPortal.
DR GO; GO:0005637; C:nuclear inner membrane; NAS:UniProtKB.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
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:0015075; F:ion transmembrane transporter activity; NAS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:RHEA.
DR GO; GO:0090556; F:phosphatidylserine floppase activity; IEA:RHEA.
DR GO; GO:0015917; P:aminophospholipid transport; TAS:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0006811; P:ion transport; NAS:UniProtKB.
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; IPR030362; ATP11B.
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:SF57; PTHR24092:SF57; 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; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Endoplasmic reticulum; Endosome; Golgi apparatus;
KW Lipid transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1177
FT /note="Phospholipid-transporting ATPase IF"
FT /id="PRO_0000046371"
FT TOPO_DOM 1..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..82
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..341
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..876
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 877..898
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 899..910
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 911..930
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 931..960
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 961..982
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 983..997
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 998..1020
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1021..1025
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1026..1047
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1048..1065
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1066..1090
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1091..1177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 407
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD20"
FT BINDING 821
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT BINDING 825
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT MOD_RES 1154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MUTAGEN 180
FT /note="E->Q: Impairs ATPase activity."
FT /evidence="ECO:0000269|PubMed:30018401"
SQ SEQUENCE 1177 AA; 134190 MW; 665110145457B220 CRC64;
MWRWIRQQLG FDPPHQSDTR TIYVANRFPQ NGLYTPQKFI DNRIISSKYT VWNFVPKNLF
EQFRRVANFY FLIIFLVQLM IDTPTSPVTS GLPLFFVITV TAIKQGYEDW LRHNSDNEVN
GAPVYVVRSG GLVKTRSKNI RVGDIVRIAK DEIFPADLVL LSSDRLDGSC HVTTASLDGE
TNLKTHVAVP ETALLQTVAN LDTLVAVIEC QQPEADLYRF MGRMIITQQM EEIVRPLGPE
SLLLRGARLK NTKEIFGVAV YTGMETKMAL NYKSKSQKRS AVEKSMNTFL IIYLVILISE
AVISTILKYT WQAEEKWDEP WYNQKTEHQR NSSKILRFIS DFLAFLVLYN FIIPISLYVT
VEMQKFLGSF FIGWDLDLYH EESDQKAQVN TSDLNEELGQ VEYVFTDKTG TLTENEMQFR
ECSINGMKYQ EINGRLVPEG PTPDSSEGNL SYLSSLSHLN NLSHLTTSSS FRTSPENETE
LIKEHDLFFK AVSLCHTVQI SNVQTDCTGD GPWQSNLAPS QLEYYASSPD EKALVEAAAR
IGIVFIGNSE ETMEVKTLGK LERYKLLHIL EFDSDRRRMS VIVQAPSGEK LLFAKGAESS
ILPKCIGGEI EKTRIHVDEF ALKGLRTLCI AYRKFTSKEY EEIDKRIFEA RTALQQREEK
LAAVFQFIEK DLILLGATAV EDRLQDKVRE TIEALRMAGI KVWVLTGDKH ETAVSVSLSC
GHFHRTMNIL ELINQKSDSE CAEQLRQLAR RITEDHVIQH GLVVDGTSLS LALREHEKLF
MEVCRNCSAV LCCRMAPLQK AKVIRLIKIS PEKPITLAVG DGANDVSMIQ EAHVGIGIMG
KEGRQAARNS DYAIARFKFL SKLLFVHGHF YYIRIATLVQ YFFYKNVCFI TPQFLYQFYC
LFSQQTLYDS VYLTLYNICF TSLPILIYSL LEQHVDPHVL QNKPTLYRDI SKNRLLSIKT
FLYWTILGFS HAFIFFFGSY LLIGKDTSLL GNGQMFGNWT FGTLVFTVMV ITVTVKMALE
THFWTWINHL VTWGSIIFYF VFSLFYGGIL WPFLGSQNMY FVFIQLLSSG SAWFAIILMV
VTCLFLDIIK KVFDRHLHPT STEKAQLTET NAGIKCLDSM CCFPEGEAAC ASVGRMLERV
IGRCSPTHIS RSWSASDPFY TNDRSILTLS TMDSSTC
