AT11C_MOUSE
ID AT11C_MOUSE Reviewed; 1129 AA.
AC Q9QZW0; Q3KQR4;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Phospholipid-transporting ATPase 11C;
DE EC=7.6.2.1 {ECO:0000269|PubMed:21423173, ECO:0000269|PubMed:24898253, ECO:0000269|PubMed:24904167, ECO:0000269|PubMed:26799398, ECO:0000269|PubMed:30018401};
DE AltName: Full=ATPase class VI type 11C;
DE AltName: Full=P4-ATPase flippase complex alpha subunit ATP11C;
GN Name=Atp11c {ECO:0000303|PubMed:26799398, ECO:0000312|MGI:MGI:1859661};
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 [LARGE SCALE MRNA].
RC TISSUE=Thyroid;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 767-1129 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, 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 [4]
RP FUNCTION.
RX PubMed=21423172; DOI=10.1038/ni.2012;
RA Siggs O.M., Arnold C.N., Huber C., Pirie E., Xia Y., Lin P., Nemazee D.,
RA Beutler B.;
RT "The P4-type ATPase ATP11C is essential for B lymphopoiesis in adult bone
RT marrow.";
RL Nat. Immunol. 12:434-440(2011).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND INVOLVEMENT IN DEFECTIVE LYMPHOPOIESIS.
RX PubMed=21423173; DOI=10.1038/ni.2011;
RA Yabas M., Teh C.E., Frankenreiter S., Lal D., Roots C.M., Whittle B.,
RA Andrews D.T., Zhang Y., Teoh N.C., Sprent J., Tze L.E., Kucharska E.M.,
RA Kofler J., Farell G.C., Broer S., Goodnow C.C., Enders A.;
RT "ATP11C is critical for the internalization of phosphatidylserine and
RT differentiation of B lymphocytes.";
RL Nat. Immunol. 12:441-449(2011).
RN [6]
RP FUNCTION, AND INVOLVEMENT IN CHOLESTASIS.
RX PubMed=21518881; DOI=10.1073/pnas.1104631108;
RA Siggs O.M., Schnabl B., Webb B., Beutler B.;
RT "X-linked cholestasis in mouse due to mutations of the P4-ATPase ATP11C.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:7890-7895(2011).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND INVOLVEMENT IN ANEMIA.
RX PubMed=24898253; DOI=10.1074/jbc.c114.570267;
RA Yabas M., Coupland L.A., Cromer D., Winterberg M., Teoh N.C., D'Rozario J.,
RA Kirk K., Broeer S., Parish C.R., Enders A.;
RT "Mice deficient in the putative phospholipid flippase ATP11C exhibit
RT altered erythrocyte shape, anemia, and reduced erythrocyte life span.";
RL J. Biol. Chem. 289:19531-19537(2014).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=24904167; DOI=10.1126/science.1252809;
RA Segawa K., Kurata S., Yanagihashi Y., Brummelkamp T.R., Matsuda F.,
RA Nagata S.;
RT "Caspase-mediated cleavage of phospholipid flippase for apoptotic
RT phosphatidylserine exposure.";
RL Science 344:1164-1168(2014).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26799398; DOI=10.1371/journal.pone.0146774;
RA Yabas M., Jing W., Shafik S., Broeer S., Enders A.;
RT "ATP11C Facilitates Phospholipid Translocation across the Plasma Membrane
RT of All Leukocytes.";
RL PLoS ONE 11:e0146774-e0146774(2016).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION
RP WITH TMEM30A, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLU-181.
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 the plasma membrane (PubMed:24904167, PubMed:26799398, PubMed:30018401,
CC PubMed:24898253). Major PS-flippase in immune cell subsets
CC (PubMed:30018401). In erythrocyte plasma membrane, it is required to
CC maintain PS in the inner leaflet preventing its exposure on the
CC surface. This asymmetric distribution is critical for the survival of
CC erythrocytes in circulation since externalized PS is a phagocytic
CC signal for erythrocyte clearance by splenic macrophages
CC (PubMed:24898253). Required for B cell differentiation past the pro-B
CC cell stage (PubMed:21423173). Seems to mediate PS flipping in pro-B
CC cells (PubMed:21423172, PubMed:26799398). May be involved in the
CC transport of cholestatic bile acids (PubMed:21518881).
CC {ECO:0000269|PubMed:21423172, ECO:0000269|PubMed:21423173,
CC ECO:0000269|PubMed:21518881, ECO:0000269|PubMed:24898253,
CC ECO:0000269|PubMed:24904167, ECO:0000269|PubMed:26799398,
CC 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:21423173, ECO:0000269|PubMed:24898253,
CC ECO:0000269|PubMed:24904167, ECO:0000269|PubMed:26799398,
CC 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:21423173, ECO:0000269|PubMed:24898253,
CC ECO:0000269|PubMed:24904167, ECO:0000269|PubMed:26799398,
CC ECO:0000269|PubMed:30018401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568;
CC Evidence={ECO:0000305|PubMed:21423173, ECO:0000305|PubMed:24898253,
CC ECO:0000305|PubMed:24904167, ECO:0000305|PubMed:26799398,
CC 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:24904167, ECO:0000269|PubMed:26799398,
CC ECO:0000269|PubMed:30018401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000305|PubMed:24904167, ECO:0000305|PubMed:26799398,
CC ECO:0000305|PubMed:30018401};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1440 uM for ATP {ECO:0000269|PubMed:30018401};
CC Vmax=48.3 umol/min/mg enzyme toward ATP
CC {ECO:0000269|PubMed:30018401};
CC -!- SUBUNIT: Component of a P4-ATPase flippase complex which consists of a
CC catalytic alpha subunit ATP11C and an accessory beta subunit TMEM30A.
CC {ECO:0000269|PubMed:30018401}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NB49};
CC Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:Q8NB49}; Multi-pass membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q8NB49};
CC Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q8NB49}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Efficient exit from the endoplasmic reticulum
CC requires the presence of TMEM30A. Internalized via clathrin-dependent
CC endocytosis in response to ca(2+) signaling induced by G-protein
CC coupled serotonin and histamine receptors, HTR2A and HRH1 respectively.
CC {ECO:0000250|UniProtKB:Q8NB49}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QZW0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QZW0-2; Sequence=VSP_022222, VSP_022223;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in retina, brain, liver
CC and testes (at protein level) (PubMed:30018401). Expressed in lung,
CC bone marrow, lymph nodes, prostate, ovary and uterus (PubMed:24904167).
CC Expressed in fetus (PubMed:24904167). {ECO:0000269|PubMed:24904167,
CC ECO:0000269|PubMed:30018401}.
CC -!- DOMAIN: The di-leucine motif is required for sorting to clathrin-coated
CC endosomes upon ca(2+)-dependent PRKCA activation.
CC {ECO:0000250|UniProtKB:Q8NB49}.
CC -!- PTM: Proteolytically cleaved by CASP3, CASP6 and CASP7.
CC {ECO:0000250|UniProtKB:Q8NB49}.
CC -!- PTM: Phosphorylated at Ser-1113 likely by PRKCA; this creates a
CC functional di-leucine motif that is sufficient for endocytosis.
CC {ECO:0000250|UniProtKB:Q8NB49}.
CC -!- DISEASE: Note=Mice defective in Atp11c show defective B lymphopoiesis,
CC specifically in mature bone marrow, pronounced stomatocytosis
CC associated with anemia, hyperbilirubinemia linked to mild cholestasis
CC and hepatocellular carcinoma. {ECO:0000269|PubMed:21423173,
CC ECO:0000269|PubMed:21518881, ECO:0000269|PubMed:24898253}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC106087; AAI06088.1; -; mRNA.
DR EMBL; AF156547; AAF09445.1; -; mRNA.
DR CCDS; CCDS40988.1; -. [Q9QZW0-1]
DR RefSeq; NP_001032952.1; NM_001037863.1. [Q9QZW0-1]
DR RefSeq; XP_006528153.1; XM_006528090.3. [Q9QZW0-1]
DR RefSeq; XP_006528154.1; XM_006528091.3. [Q9QZW0-1]
DR RefSeq; XP_011245917.1; XM_011247615.2. [Q9QZW0-1]
DR RefSeq; XP_011245918.1; XM_011247616.1. [Q9QZW0-1]
DR AlphaFoldDB; Q9QZW0; -.
DR SMR; Q9QZW0; -.
DR BioGRID; 236409; 1.
DR STRING; 10090.ENSMUSP00000099066; -.
DR iPTMnet; Q9QZW0; -.
DR PhosphoSitePlus; Q9QZW0; -.
DR SwissPalm; Q9QZW0; -.
DR EPD; Q9QZW0; -.
DR jPOST; Q9QZW0; -.
DR MaxQB; Q9QZW0; -.
DR PaxDb; Q9QZW0; -.
DR PRIDE; Q9QZW0; -.
DR ProteomicsDB; 281929; -. [Q9QZW0-1]
DR ProteomicsDB; 281930; -. [Q9QZW0-2]
DR Antibodypedia; 30516; 103 antibodies from 22 providers.
DR DNASU; 320940; -.
DR Ensembl; ENSMUST00000101527; ENSMUSP00000099066; ENSMUSG00000062949. [Q9QZW0-1]
DR GeneID; 320940; -.
DR KEGG; mmu:320940; -.
DR UCSC; uc009tia.1; mouse. [Q9QZW0-1]
DR CTD; 286410; -.
DR MGI; MGI:1859661; Atp11c.
DR VEuPathDB; HostDB:ENSMUSG00000062949; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000158878; -.
DR InParanoid; Q9QZW0; -.
DR OMA; HGHTAYQ; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; Q9QZW0; -.
DR BRENDA; 7.6.2.1; 3474.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 320940; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Atp11c; mouse.
DR PRO; PR:Q9QZW0; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9QZW0; protein.
DR Bgee; ENSMUSG00000062949; Expressed in liver and 67 other tissues.
DR ExpressionAtlas; Q9QZW0; baseline and differential.
DR Genevisible; Q9QZW0; MM.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
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:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; ISO:MGI.
DR GO; GO:0140346; F:phosphatidylserine flippase activity; ISO:MGI.
DR GO; GO:0090556; F:phosphatidylserine floppase activity; IEA:RHEA.
DR GO; GO:0045332; P:phospholipid translocation; IMP:UniProtKB.
DR GO; GO:0045579; P:positive regulation of B cell differentiation; IMP:UniProtKB.
DR GO; GO:0002329; P:pre-B cell differentiation; IMP:UniProtKB.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030363; ATP11C.
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:SF38; PTHR24092:SF38; 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 Alternative splicing; ATP-binding; Cell membrane; Coiled coil;
KW Endoplasmic reticulum; Endosome; Lipid transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1129
FT /note="Phospholipid-transporting ATPase 11C"
FT /id="PRO_0000046374"
FT TOPO_DOM 1..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..876
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 877..897
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 898..905
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 906..926
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 927..952
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 953..973
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 974..988
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 989..1009
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1010..1023
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1024..1044
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1045..1066
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1067..1087
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1088..1129
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT COILED 607..643
FT /evidence="ECO:0000255"
FT COILED 695..726
FT /evidence="ECO:0000255"
FT MOTIF 1113..1118
FT /note="Di-leucine motif"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT ACT_SITE 409
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 816
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT BINDING 820
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT SITE 439..440
FT /note="Cleavage; by CASP3, CASP6 and CASP7"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT SITE 445..446
FT /note="Cleavage; by CASP3"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT SITE 481..482
FT /note="Cleavage; by CASP3 and CASP7"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT MOD_RES 1105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT MOD_RES 1113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT MOD_RES 1123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT VAR_SEQ 833..835
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11015572"
FT /id="VSP_022222"
FT VAR_SEQ 1097..1129
FT /note="RNLSCRRASDSLSARPSVRPLLLRTFSDESNIL -> NPNLELPMLLSYKHI
FT DRGCS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11015572"
FT /id="VSP_022223"
FT MUTAGEN 181
FT /note="E->Q: Impairs ATPase activity."
FT /evidence="ECO:0000269|PubMed:30018401"
FT CONFLICT 786..791
FT /note="LCCRMA -> VCCADQ (in Ref. 2; AAF09445)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1129 AA; 129240 MW; EE82DFD1F0669294 CRC64;
MFRRTLNRLC AGEEKRVGTR TVFVGNHPIS GTEPYIAQRF CDNRIVSSKY TLWNFLPKNL
FEQFRRIANF YFLIIFLVQV TVDTPTSPVT SGLPLFFVIT VTAIKQGYED WLRHRADNEV
NKSAVYIIEN AKRVRKESEK IKVGDVVEVQ ANETFPCDLI LLSSCTTDGT CYVTTASLDG
ESNCKTHYAV RDTIALCTAE SIDNLRATIE CEQPQPDLYR FVGRISIYSN SIEAVARSLG
PENLLLKGAT LKNTKKIYGV AVYTGMETKM ALNYQGKSQK CSAVEKSINA FLIVYLFILL
TKAAVCTTLK YVWQSSPYND EPWYNQKTQK ERETFQVLKM FTDFLSFMVL FNFIIPVSMY
VTVEMQKFLG SFFISWDKDF FDEEINEGAL VNTSDLNEEL GQVDYVFTDK TGTLTENSME
FIECCIDGHK YKGTTQEVDG LSQTDGPLAY FDKADKNREA LFLRALCLCH TVEMKTNDDV
DGPVEGAGFT YISSSPDEIA LVKGAKRFGF TFLGNQNGYI RVENQRKEIE EYELLHTLNF
DSVRRRMSVI VRTQKGDILL FCKGADSSIF PRVHSHQIEL TKDHVERNAM DGYRTLCVAF
KEIPPDDFER INAQLVEAKM ALQDREEKLE KVFDEIETNM NLIGATAVED KLQDQAAETI
EALHAAGLKV WVLTGDKMET AKSTCYACRL FQTNTELLEL TTKTIEESER KEDRLHELLI
EYRKKLLHEF PKSTRSLKKA WTEHQEYGLI IDGSTLSLIL NSSQDCSSNN YKSIFLQICM
KCTAVLCCRM APLQKAQIVR MVKNLKGSPI TLSIGDGAND VSMILESHVG IGIKGKEGRQ
AARNSDYSVP KFKHLKKLLL VHGHLYYVRI AHLVQYFFYK NLCFILPQFL YQFFCGFSQQ
PLYDAAYLTM YNICFTSLPI LAYSLLEQHI NIDTLTADPR LYMKITGNAM LQLGPFLHWT
FLAAFEGTVF FFGTYFLFQT SSLEDNGKIY GNWTFGTIVF TVLVFTVTLK LALDTRFWTW
INHFVIWGSL AFYVFFSFFW GGIIWPFLKQ QRMYFVFAQM LCSVSTWLAI ILLIFISLFP
EILLIVVKNV RRRSARRNLS CRRASDSLSA RPSVRPLLLR TFSDESNIL
