AT2B2_MOUSE
ID AT2B2_MOUSE Reviewed; 1198 AA.
AC Q9R0K7; O88863;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Plasma membrane calcium-transporting ATPase 2;
DE Short=PMCA2;
DE EC=7.2.2.10 {ECO:0000269|PubMed:17234811};
DE AltName: Full=Plasma membrane calcium ATPase isoform 2;
DE AltName: Full=Plasma membrane calcium pump isoform 2;
GN Name=Atp2b2 {ECO:0000312|MGI:MGI:105368};
GN Synonyms=Pmca2 {ECO:0000303|PubMed:20083513};
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], TISSUE SPECIFICITY, INVOLVEMENT IN DEAFNESS,
RP AND VARIANT DFW SER-283.
RC STRAIN=C3H/HeJ;
RX PubMed=9697703; DOI=10.1038/1284;
RA Street V.A., McKee-Johnson J.W., Fonseca R.C., Tempel B.L.,
RA Noben-Trauth K.;
RT "Mutations in a plasma membrane Ca2+-ATPase gene cause deafness in
RT deafwaddler mice.";
RL Nat. Genet. 19:390-394(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-412.
RC STRAIN=BALB/C WMS;
RX PubMed=11985881; DOI=10.1016/s0168-0102(02)00008-1;
RA Ueno T., Kameyama K., Hirata M., Ogawa M., Hatsuse H., Takagaki Y.,
RA Ohmura M., Osawa N., Kudo Y.;
RT "A mouse with a point mutation in plasma membrane Ca2+-ATPase isoform 2
RT gene showed the reduced Ca2+ influx in cerebellar neurons.";
RL Neurosci. Res. 42:287-297(2002).
RN [3]
RP PROTEIN SEQUENCE OF 16-32; 46-58; 62-77; 80-90; 197-249; 251-270; 305-318;
RP 438-455; 464-477; 489-506; 537-543; 554-561; 570-576; 581-588; 593-601;
RP 626-632; 684-694; 757-767; 785-818; 825-832; 931-938; 976-983; 1104-1116;
RP 1130-1152 AND 1164-1180.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9668038; DOI=10.1074/jbc.273.30.18693;
RA Kozel P.J., Friedman R.A., Erway L.C., Yamoah E.N., Liu L.H., Riddle T.,
RA Duffy J.J., Doetschman T., Miller M.L., Cardell E.L., Shull G.E.;
RT "Balance and hearing deficits in mice with a null mutation in the gene
RT encoding plasma membrane Ca2+-ATPase isoform 2.";
RL J. Biol. Chem. 273:18693-18696(1998).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12209837; DOI=10.1002/cne.10281;
RA Krizaj D., Demarco S.J., Johnson J., Strehler E.E., Copenhagen D.R.;
RT "Cell-specific expression of plasma membrane calcium ATPase isoforms in
RT retinal neurons.";
RL J. Comp. Neurol. 451:1-21(2002).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15302868; DOI=10.1074/jbc.m407788200;
RA Reinhardt T.A., Lippolis J.D., Shull G.E., Horst R.L.;
RT "Null mutation in the gene encoding plasma membrane Ca2+-ATPase isoform 2
RT impairs calcium transport into milk.";
RL J. Biol. Chem. 279:42369-42373(2004).
RN [7]
RP FUNCTION.
RX PubMed=17409239; DOI=10.1523/jneurosci.0069-07.2007;
RA Empson R.M., Garside M.L., Knoepfel T.;
RT "Plasma membrane Ca2+ ATPase 2 contributes to short-term synapse plasticity
RT at the parallel fiber to Purkinje neuron synapse.";
RL J. Neurosci. 27:3753-3758(2007).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, INVOLVEMENT IN DEAFNESS, AND CHARACTERIZATION
RP OF VARIANT DFW SER-293.
RX PubMed=17234811; DOI=10.1073/pnas.0609775104;
RA Ficarella R., Di Leva F., Bortolozzi M., Ortolano S., Donaudy F.,
RA Petrillo M., Melchionda S., Lelli A., Domi T., Fedrizzi L., Lim D.,
RA Shull G.E., Gasparini P., Brini M., Mammano F., Carafoli E.;
RT "A functional study of plasma-membrane calcium-pump isoform 2 mutants
RT causing digenic deafness.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1516-1521(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-1133; THR-1143 AND
RP SER-1156, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Brown adipose tissue;
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 TISSUE SPECIFICITY.
RX PubMed=20083513; DOI=10.1113/jphysiol.2009.182196;
RA Empson R.M., Turner P.R., Nagaraja R.Y., Beesley P.W., Knoepfel T.;
RT "Reduced expression of the Ca(2+) transporter protein PMCA2 slows Ca(2+)
RT dynamics in mouse cerebellar Purkinje neurones and alters the precision of
RT motor coordination.";
RL J. Physiol. (Lond.) 588:907-922(2010).
CC -!- FUNCTION: ATP-driven Ca(2+) ion pump involved in the maintenance of
CC basal intracellular Ca(2+) levels in specialized cells of cerebellar
CC circuit and vestibular and cochlear systems (PubMed:17234811,
CC PubMed:9668038). Uses ATP as an energy source to transport cytosolic
CC Ca(2+) ions across the plasma membrane to the extracellular
CC compartment. Has fast activation and Ca(2+) clearance rate suited to
CC control fast neuronal Ca(2+) dynamics (PubMed:17409239,
CC PubMed:20083513). At parallel fiber to Purkinje neuron synapse,
CC mediates presynaptic Ca(2+) efflux in response to climbing fiber-
CC induced Ca(2+) rise. Provides for fast return of Ca(2+) concentrations
CC back to their resting levels, ultimately contributing to long-term
CC depression induction and motor learning (PubMed:17409239,
CC PubMed:20083513). Plays an essential role in hearing and balance. In
CC cochlear hair cells, shuttles Ca(2+) ions from stereocilia to the
CC endolymph and dissipates Ca(2+) transients generated by the opening of
CC the mechanoelectrical transduction channels. Regulates Ca(2+) levels in
CC the vestibular system, where it contributes to the formation of
CC otoconia (PubMed:9668038) (By similarity). Regulates Ca(2+) signaling
CC through dissipation of Ca(2+) transients generated by store-operated
CC channels (By similarity). In lactating mammary gland, allows for the
CC high content of Ca(2+) ions in the milk (PubMed:15302868).
CC {ECO:0000250|UniProtKB:Q01814, ECO:0000269|PubMed:15302868,
CC ECO:0000269|PubMed:17234811, ECO:0000269|PubMed:17409239,
CC ECO:0000269|PubMed:20083513, ECO:0000269|PubMed:9668038}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000269|PubMed:17234811};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC Evidence={ECO:0000305|PubMed:17234811};
CC -!- SUBUNIT: Interacts with PDZD11. {ECO:0000250|UniProtKB:Q01814}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q01814};
CC Multi-pass membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q01814}; Multi-pass membrane protein
CC {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q01814}; Multi-pass membrane protein
CC {ECO:0000255}. Synapse {ECO:0000269|PubMed:12209837}.
CC -!- TISSUE SPECIFICITY: Expressed in the retina, with strongest levels in
CC the inner plexiform layer, weaker levels in the outer plexiform layer,
CC and very low levels in the proximal inner nuclear layer
CC (PubMed:12209837). Specifically expressed in the following retinal cell
CC types: rod bipolar cells, horizontal cells, amacrine cells and ganglion
CC cells (PubMed:12209837). Also found in the cochlea (stereocilia and
CC outer wall of hair cells) (at protein level) (PubMed:9697703). Strongly
CC expressed in brain cortex and cerebellum. Found at low levels in heart,
CC liver, lung and testis during late gestation (PubMed:9697703,
CC PubMed:20083513). Expressed in lactating mammary gland (at protein
CC level). {ECO:0000269|PubMed:12209837, ECO:0000269|PubMed:15302868,
CC ECO:0000269|PubMed:20083513, ECO:0000269|PubMed:9697703}.
CC -!- DISEASE: Note=Defects in Atp2b2 are associated with early onset
CC profound hearing loss and severe vestibular dysfunction.
CC {ECO:0000269|PubMed:17234811, ECO:0000269|PubMed:9697703}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice, born at the expected Mendelian rate,
CC show balance impairment and hearing loss. They develop severe ataxia
CC before 2 weeks of age associated with the absence of otoconia in the
CC vestibular inner ear. {ECO:0000269|PubMed:9668038}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIB subfamily. {ECO:0000305}.
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DR EMBL; AF053471; AAC61255.1; -; mRNA.
DR EMBL; AB030737; BAA83104.1; -; mRNA.
DR EMBL; AB030738; BAA83105.1; -; mRNA.
DR CCDS; CCDS20433.1; -.
DR RefSeq; NP_001031761.1; NM_001036684.3.
DR RefSeq; NP_033853.1; NM_009723.6.
DR RefSeq; XP_017176842.1; XM_017321353.1.
DR AlphaFoldDB; Q9R0K7; -.
DR SMR; Q9R0K7; -.
DR BioGRID; 198250; 11.
DR IntAct; Q9R0K7; 4.
DR MINT; Q9R0K7; -.
DR STRING; 10090.ENSMUSP00000086398; -.
DR iPTMnet; Q9R0K7; -.
DR PhosphoSitePlus; Q9R0K7; -.
DR SwissPalm; Q9R0K7; -.
DR EPD; Q9R0K7; -.
DR jPOST; Q9R0K7; -.
DR MaxQB; Q9R0K7; -.
DR PaxDb; Q9R0K7; -.
DR PRIDE; Q9R0K7; -.
DR ProteomicsDB; 277122; -.
DR ABCD; Q9R0K7; 1 sequenced antibody.
DR Antibodypedia; 26012; 129 antibodies from 24 providers.
DR DNASU; 11941; -.
DR Ensembl; ENSMUST00000089003; ENSMUSP00000086398; ENSMUSG00000030302.
DR Ensembl; ENSMUST00000101045; ENSMUSP00000098606; ENSMUSG00000030302.
DR GeneID; 11941; -.
DR KEGG; mmu:11941; -.
DR UCSC; uc009dhn.1; mouse.
DR CTD; 491; -.
DR MGI; MGI:105368; Atp2b2.
DR VEuPathDB; HostDB:ENSMUSG00000030302; -.
DR eggNOG; KOG0204; Eukaryota.
DR GeneTree; ENSGT00940000161461; -.
DR HOGENOM; CLU_002360_9_0_1; -.
DR InParanoid; Q9R0K7; -.
DR TreeFam; TF300330; -.
DR BRENDA; 7.2.2.10; 3474.
DR Reactome; R-MMU-418359; Reduction of cytosolic Ca++ levels.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 11941; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Atp2b2; mouse.
DR PRO; PR:Q9R0K7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9R0K7; protein.
DR Bgee; ENSMUSG00000030302; Expressed in olfactory tubercle and 132 other tissues.
DR ExpressionAtlas; Q9R0K7; baseline and differential.
DR Genevisible; Q9R0K7; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0032591; C:dendritic spine membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0032809; C:neuronal cell body membrane; ISO:MGI.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0030899; F:calcium-dependent ATPase activity; IMP:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0035254; F:glutamate receptor binding; ISO:MGI.
DR GO; GO:0005388; F:P-type calcium transporter activity; ISS:UniProtKB.
DR GO; GO:1905059; F:P-type calcium transporter activity involved in regulation of postsynaptic cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:1905056; F:P-type calcium transporter activity involved in regulation of presynaptic cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI.
DR GO; GO:0006816; P:calcium ion transport; IMP:DFLAT.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR GO; GO:0021707; P:cerebellar granule cell differentiation; IMP:MGI.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:MGI.
DR GO; GO:0021692; P:cerebellar Purkinje cell layer morphogenesis; IMP:MGI.
DR GO; GO:0021549; P:cerebellum development; IMP:MGI.
DR GO; GO:0046068; P:cGMP metabolic process; IMP:MGI.
DR GO; GO:0090102; P:cochlea development; IMP:DFLAT.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0048839; P:inner ear development; IMP:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR GO; GO:0060113; P:inner ear receptor cell differentiation; IMP:MGI.
DR GO; GO:0007595; P:lactation; IMP:MGI.
DR GO; GO:0040011; P:locomotion; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0006996; P:organelle organization; IMP:MGI.
DR GO; GO:0045299; P:otolith mineralization; IMP:MGI.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IMP:MGI.
DR GO; GO:0008361; P:regulation of cell size; IMP:MGI.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IMP:DFLAT.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0042428; P:serotonin metabolic process; IMP:MGI.
DR GO; GO:0050808; P:synapse organization; IMP:MGI.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030322; ATP2B2.
DR InterPro; IPR022141; ATP_Ca_trans_C.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR PANTHER; PTHR24093:SF377; PTHR24093:SF377; 2.
DR Pfam; PF12424; ATP_Ca_trans_C; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Calcium transport; Calmodulin-binding; Cell membrane;
KW Direct protein sequencing; Disease variant; Ion transport; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Synapse; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1198
FT /note="Plasma membrane calcium-transporting ATPase 2"
FT /id="PRO_0000046215"
FT TOPO_DOM 1..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..152
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..398
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..830
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 831..850
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 851..860
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 861..881
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 882..901
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 902..924
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 925..942
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 943..964
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 965..983
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 984..1005
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1006..1015
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1016..1037
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1038..1198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1095
FT /note="Calmodulin-binding subdomain A"
FT /evidence="ECO:0000250"
FT REGION 1096..1105
FT /note="Calmodulin-binding subdomain B"
FT /evidence="ECO:0000250"
FT REGION 1149..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 454
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 775
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 779
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1094
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT MOD_RES 1133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1143
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01814"
FT VARIANT 283
FT /note="G -> S (in dfw; results in impaired long-term Ca2+
FT export at stereocilia)"
FT /evidence="ECO:0000269|PubMed:17234811,
FT ECO:0000269|PubMed:9697703"
FT VARIANT 412
FT /note="E -> K"
FT /evidence="ECO:0000269|PubMed:11985881"
SQ SEQUENCE 1198 AA; 132588 MW; BAA8CC28620D994B CRC64;
MGDMTNSDFY SKNQRNESSH GGEFGCTMEE LRSLMELRGT EAVVKIKETY GDTEAICRRL
KTSPVEGLPG TAPDLEKRKQ IFGQNFIPPK KPKTFLQLVW EALQDVTLII LEIAAIISLG
LSFYHPPGES NEGCATAQGG AEDEGEAEAG WIEGAAILLS VICVVLVTAF NDWSKEKQFR
GLQSRIEQEQ KFTVVRAGQV VQIPVAEIVV GDIAQIKYGD LLPADGLFIQ GNDLKIDESS
LTGESDQVRK SVDKDPMLLS GTHVMEGSGR MVVTAVGVNS QTGIIFTLLG AGGEEEEKKD
KKAKQQDGAA AMEMQPLKSA EGGDADDKKK ANMHKKEKSV LQGKLTKLAV QIGKAGLVMS
AITVIILVLY FTVDTFVVNK KPWLTECTPV YVQYFVKFFI IGVTVLVVAV PEGLPLAVTI
SLAYSVKKMM KDNNLVRHLD ACETMGNATA ICSDKTGTLT TNRMTVVQAY VGDVHYKEIP
DPSSINAKTL ELLVNAIAIN SAYTTKILPP EKEGALPRQV GNKTECGLLG FVLDLRQDYE
PVRSQMPEEK LYKVYTFNSV RKSMSTVIKM PDESFRMYSK GASEIVLKKC CKILSGAGEA
RVFRPRDRDE MVKKVIEPMA CDGLRTICVA YRDFPSSPEP DWDNENDILN ELTCICVVGI
EDPVRPEVPE AIRKCQRAGI TVRMVTGDNI NTARAIAIKC GIIHPGEDFL CLEGKEFNRR
IRNEKGEIEQ ERIDKIWPKL RVLARSSPTD KHTLVKGIID STHTEQRQVV AVTGDGTNDG
PALKKADVGF AMGIAGTDVA KEASDIILTD DNFSSIVKAV MWGRNVYDSI SKFLQFQLTV
NVVAVIVAFT GACITQDSPL KAVQMLWVNL IMDTFASLAL ATEPPTETLL LRKPYGRNKP
LISRTMMKNI LGHAVYQLTL IFTLLFVGEK MFQIDSGRNA PLHSPPSEHY TIIFNTFVMM
QLFNEINARK IHGERNVFDG IFRNPIFCTI VLGTFAIQIV IVQFGGKPFS CSPLQLDQWM
WCIFIGLGEL VWGQVIATIP TSRLKFLKEA GRLTQKEEIP EEELNEDVEE IDHAERELRR
GQILWFRGLN RIQTQIRVVK AFRSSLYEGL EKPESRTSIH NFMAHPEFRI EDSQPHIPLI
DDTDLEEDAA LKQNSSPPSS LNKNNSAIDS GINLTTDTSK SATSSSPGSP IHSLETSL
