ID   AT2B2_HUMAN             Reviewed;        1243 AA.
AC   Q01814; O00766; Q12994; Q16818;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   07-OCT-2020, entry version 215.
DE   RecName: Full=Plasma membrane calcium-transporting ATPase 2;
DE            Short=PMCA2;
DE            EC=7.2.2.10;
DE   AltName: Full=Plasma membrane calcium ATPase isoform 2;
DE   AltName: Full=Plasma membrane calcium pump isoform 2;
GN   Name=ATP2B2; Synonyms=PMCA2;
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 ZB).
RC   TISSUE=Brain;
RX   PubMed=1427863; DOI=10.1016/s0888-7543(05)80246-0;
RA   Brandt P., Ibrahim E., Bruns G.A.P., Neve R.L.;
RT   "Determination of the nucleotide sequence and chromosomal localization of
RT   the ATP2B2 gene encoding human Ca(2+)-pumping ATPase isoform PMCA2.";
RL   Genomics 14:484-487(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZB), AND ALTERNATIVE SPLICING.
RX   PubMed=8428366;
RA   Latif F., Duh F.-M., Gnarra J., Tory K., Kuzmin I., Yao M., Stackhouse T.,
RA   Modi W., Geil L., Schmidt L., Li H., Orcutt M.L., Maher E., Richards F.,
RA   Phipps M., Ferguson-Smith M., le Paslier D., Linehan W.M., Zbar B.,
RA   Lerman M.I.;
RT   "von Hippel-Lindau syndrome: cloning and identification of the plasma
RT   membrane Ca(++)-transporting ATPase isoform 2 gene that resides in the von
RT   Hippel-Lindau gene region.";
RL   Cancer Res. 53:861-867(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM WB), AND ALTERNATIVE SPLICING.
RC   TISSUE=Brain, and Skeletal muscle;
RX   PubMed=1313367; DOI=10.1111/j.1432-1033.1992.tb16784.x;
RA   Heim R., Hug M., Iwata T., Strehler E.E., Carafoli E.;
RT   "Microdiversity of human-plasma-membrane calcium-pump isoform 2 generated
RT   by alternative RNA splicing in the N-terminal coding region.";
RL   Eur. J. Biochem. 205:333-340(1992).
RN   [4]
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   [5]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS WA/YA/ZA).
RC   TISSUE=Brain cortex;
RX   PubMed=8245032;
RA   Stauffer T.P., Hilfiker H., Carafoli E., Strehler E.E.;
RT   "Quantitative analysis of alternative splicing options of human plasma
RT   membrane calcium pump genes.";
RL   J. Biol. Chem. 268:25993-26003(1993).
RN   [6]
RP   ERRATUM OF PUBMED:8245032.
RX   PubMed=7989379;
RA   Stauffer T.P., Hilfiker H., Carafoli E., Strehler E.E.;
RL   J. Biol. Chem. 269:32022-32022(1994).
RN   [7]
RP   INTERACTION WITH PDZD11.
RX   PubMed=12763866; DOI=10.1111/j.1749-6632.2003.tb07230.x;
RA   Goellner G.M., DeMarco S.J., Strehler E.E.;
RT   "Characterization of PISP, a novel single-PDZ protein that binds to all
RT   plasma membrane Ca2+-ATPase b-splice variants.";
RL   Ann. N. Y. Acad. Sci. 986:461-471(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1177 (ISOFORM WA),
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1146 (ISOFORM XA),
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1163 (ISOFORM YA),
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1132 (ISOFORM ZA), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1211, PHOSPHORYLATION [LARGE
RP   SCALE ANALYSIS] AT SER-1165 (ISOFORM WA), PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-1134 (ISOFORM XA), PHOSPHORYLATION [LARGE SCALE ANALYSIS]
RP   AT SER-1151 (ISOFORM YA), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP   SER-1120 (ISOFORM ZA), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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).
CC   -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC       ATP coupled with the transport of calcium out of the cell.
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   -!- SUBUNIT: Interacts with PDZD11. {ECO:0000269|PubMed:12763866}.
CC   -!- INTERACTION:
CC       Q01814; P01258: CALCA; NbExp=2; IntAct=EBI-1174243, EBI-1018474;
CC       Q01814; Q14160: SCRIB; NbExp=2; IntAct=EBI-1174243, EBI-357345;
CC       Q01814-1; Q63622: Dlg2; Xeno; NbExp=2; IntAct=EBI-1174262, EBI-396947;
CC       Q01814-1; Q8SQG9: SLC9A3R2; Xeno; NbExp=3; IntAct=EBI-1174262, EBI-1174758;
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse
CC       {ECO:0000250|UniProtKB:Q9R0K7}. Cell membrane {ECO:0000255}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC         Comment=There is a combination of two alternative spliced domains at
CC         N-terminal site A (Z, X, Y and W) and at C-terminal site C (A and B).
CC         So far the splice sites have only been studied independently.
CC         Experimental confirmation may be lacking for some isoforms.;
CC       Name=WB; Synonyms=AIIICI;
CC         IsoId=Q01814-1; Sequence=Displayed;
CC       Name=WA; Synonyms=AIIICII;
CC         IsoId=Q01814-2; Sequence=VSP_000386;
CC       Name=YA; Synonyms=AIICII;
CC         IsoId=Q01814-3; Sequence=VSP_000385, VSP_000386;
CC       Name=ZA; Synonyms=AICII;
CC         IsoId=Q01814-4; Sequence=VSP_000384, VSP_000386;
CC       Name=YB; Synonyms=AIICI;
CC         IsoId=Q01814-5; Sequence=VSP_000385;
CC       Name=ZB; Synonyms=AICI;
CC         IsoId=Q01814-6; Sequence=VSP_000384;
CC       Name=XA;
CC         IsoId=Q01814-7; Sequence=VSP_040837, VSP_000386;
CC       Name=XB;
CC         IsoId=Q01814-8; Sequence=VSP_040837;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in brain cortex. Found in low
CC       levels in skeletal muscle, heart muscle, stomach, liver, kidney and
CC       lung. Isoforms containing segment B are found in brain cortex and at
CC       low levels in other tissues. Isoforms containing segments X and W are
CC       found at low levels in all tissues. Isoforms containing segment A and
CC       segment Z are found at low levels in skeletal muscle and heart muscle.
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; M97260; AAA36456.1; -; mRNA.
DR   EMBL; L20977; AAA50877.1; -; mRNA.
DR   EMBL; L00620; AAA51893.1; -; mRNA.
DR   EMBL; X63575; CAA45131.1; -; mRNA.
DR   EMBL; AC018839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U15688; AAA60985.1; -; mRNA.
DR   CCDS; CCDS2601.1; -. [Q01814-6]
DR   CCDS; CCDS33701.1; -. [Q01814-1]
DR   CCDS; CCDS82733.1; -. [Q01814-4]
DR   PIR; S22393; S22393.
DR   RefSeq; NP_001001331.1; NM_001001331.2. [Q01814-1]
DR   RefSeq; NP_001317540.1; NM_001330611.1. [Q01814-4]
DR   RefSeq; XP_005265236.1; XM_005265179.4. [Q01814-1]
DR   RefSeq; XP_006713238.1; XM_006713175.3. [Q01814-1]
DR   RefSeq; XP_011532054.1; XM_011533752.2. [Q01814-1]
DR   RefSeq; XP_016861970.1; XM_017006481.1. [Q01814-1]
DR   RefSeq; XP_016861971.1; XM_017006482.1. [Q01814-1]
DR   RefSeq; XP_016861972.1; XM_017006483.1. [Q01814-8]
DR   RefSeq; XP_016861973.1; XM_017006484.1. [Q01814-8]
DR   RefSeq; XP_016861975.1; XM_017006486.1. [Q01814-2]
DR   RefSeq; XP_016861978.1; XM_017006489.1. [Q01814-7]
DR   BioGRID; 106981; 143.
DR   ELM; Q01814; -.
DR   IntAct; Q01814; 111.
DR   MINT; Q01814; -.
DR   STRING; 9606.ENSP00000353414; -.
DR   TCDB; 3.A.3.2.40; the p-type atpase (p-atpase) superfamily.
DR   iPTMnet; Q01814; -.
DR   PhosphoSitePlus; Q01814; -.
DR   SwissPalm; Q01814; -.
DR   BioMuta; ATP2B2; -.
DR   DMDM; 14286115; -.
DR   jPOST; Q01814; -.
DR   MassIVE; Q01814; -.
DR   MaxQB; Q01814; -.
DR   PaxDb; Q01814; -.
DR   PeptideAtlas; Q01814; -.
DR   PRIDE; Q01814; -.
DR   ProteomicsDB; 57993; -. [Q01814-1]
DR   ProteomicsDB; 57994; -. [Q01814-2]
DR   ProteomicsDB; 57995; -. [Q01814-3]
DR   ProteomicsDB; 57996; -. [Q01814-4]
DR   ProteomicsDB; 57997; -. [Q01814-5]
DR   ProteomicsDB; 57998; -. [Q01814-6]
DR   ProteomicsDB; 57999; -. [Q01814-7]
DR   ProteomicsDB; 58000; -. [Q01814-8]
DR   Antibodypedia; 26012; 120 antibodies.
DR   Ensembl; ENST00000360273; ENSP00000353414; ENSG00000157087. [Q01814-1]
DR   Ensembl; ENST00000397077; ENSP00000380267; ENSG00000157087. [Q01814-6]
DR   Ensembl; ENST00000452124; ENSP00000414854; ENSG00000157087. [Q01814-8]
DR   Ensembl; ENST00000460129; ENSP00000424494; ENSG00000157087. [Q01814-4]
DR   Ensembl; ENST00000643662; ENSP00000495924; ENSG00000157087. [Q01814-7]
DR   Ensembl; ENST00000644807; ENSP00000495228; ENSG00000157087. [Q01814-4]
DR   Ensembl; ENST00000645850; ENSP00000494716; ENSG00000157087. [Q01814-1]
DR   Ensembl; ENST00000646379; ENSP00000494381; ENSG00000157087. [Q01814-6]
DR   GeneID; 491; -.
DR   KEGG; hsa:491; -.
DR   UCSC; uc003bvt.3; human. [Q01814-1]
DR   CTD; 491; -.
DR   DisGeNET; 491; -.
DR   EuPathDB; HostDB:ENSG00000157087.16; -.
DR   GeneCards; ATP2B2; -.
DR   HGNC; HGNC:815; ATP2B2.
DR   HPA; ENSG00000157087; Group enriched (brain, liver, salivary gland, skeletal muscle).
DR   MalaCards; ATP2B2; -.
DR   MIM; 108733; gene.
DR   neXtProt; NX_Q01814; -.
DR   OpenTargets; ENSG00000157087; -.
DR   Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR   PharmGKB; PA25108; -.
DR   eggNOG; KOG0204; Eukaryota.
DR   GeneTree; ENSGT00940000161461; -.
DR   HOGENOM; CLU_002360_9_0_1; -.
DR   InParanoid; Q01814; -.
DR   KO; K05850; -.
DR   OMA; NCIMVGG; -.
DR   OrthoDB; 115892at2759; -.
DR   PhylomeDB; Q01814; -.
DR   TreeFam; TF300330; -.
DR   BRENDA; 3.6.3.8; 2681.
DR   PathwayCommons; Q01814; -.
DR   Reactome; R-HSA-418359; Reduction of cytosolic Ca++ levels.
DR   Reactome; R-HSA-5578775; Ion homeostasis.
DR   Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR   BioGRID-ORCS; 491; 1 hit in 866 CRISPR screens.
DR   ChiTaRS; ATP2B2; human.
DR   GeneWiki; ATP2B2; -.
DR   GenomeRNAi; 491; -.
DR   Pharos; Q01814; Tbio.
DR   PRO; PR:Q01814; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q01814; protein.
DR   Bgee; ENSG00000157087; Expressed in frontal cortex and 160 other tissues.
DR   ExpressionAtlas; Q01814; baseline and differential.
DR   Genevisible; Q01814; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0098982; C:GABA-ergic synapse; IMP:SynGO.
DR   GO; GO:0098978; C:glutamatergic synapse; IMP:SynGO.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0005388; F:calcium transmembrane transporter activity, phosphorylative mechanism; IDA:UniProtKB.
DR   GO; GO:1905056; F:calcium-transporting ATPase activity involved in regulation of presynaptic cytosolic calcium ion concentration; IMP:SynGO.
DR   GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030165; F:PDZ domain binding; IDA:UniProtKB.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0006816; P:calcium ion transport; IMP:DFLAT.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR   GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR   GO; GO:0030182; P:neuron differentiation; IDA:UniProtKB.
DR   GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
DR   GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IMP:DFLAT.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
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   PANTHER; PTHR24093:SF377; PTHR24093:SF377; 1.
DR   Pfam; PF12424; ATP_Ca_trans_C; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 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   Alternative splicing; ATP-binding; Calcium; Calcium transport;
KW   Calmodulin-binding; Cell junction; Cell membrane; Ion transport; Magnesium;
KW   Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Synapse; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1243
FT                   /note="Plasma membrane calcium-transporting ATPase 2"
FT                   /id="PRO_0000046214"
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..390
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        391..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        411..443
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        444..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        462..875
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        876..895
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        896..905
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        906..926
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        927..946
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        947..969
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        970..987
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        988..1009
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1010..1028
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1029..1050
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1051..1060
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1061..1082
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1083..1243
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1123..1140
FT                   /note="Calmodulin-binding subdomain A"
FT                   /evidence="ECO:0000250"
FT   REGION          1141..1150
FT                   /note="Calmodulin-binding subdomain B"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        294..297
FT                   /note="Poly-Glu"
FT   ACT_SITE        499
FT                   /note="4-aspartylphosphate intermediate"
FT   METAL           820
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           824
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R0K7"
FT   MOD_RES         1139
FT                   /note="Phosphothreonine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:P20020"
FT   MOD_RES         1178
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R0K7"
FT   MOD_RES         1188
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R0K7"
FT   MOD_RES         1201
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R0K7"
FT   MOD_RES         1211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   VAR_SEQ         303..347
FT                   /note="Missing (in isoform ZA and isoform ZB)"
FT                   /evidence="ECO:0000303|PubMed:1427863,
FT                   ECO:0000303|PubMed:8428366"
FT                   /id="VSP_000384"
FT   VAR_SEQ         304..334
FT                   /note="Missing (in isoform XA and isoform XB)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_040837"
FT   VAR_SEQ         334..347
FT                   /note="Missing (in isoform YA and isoform YB)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000385"
FT   VAR_SEQ         1141..1243
FT                   /note="IRVVKAFRSSLYEGLEKPESRTSIHNFMAHPEFRIEDSQPHIPLIDDTDLEE
FT                   DAALKQNSSPPSSLNKNNSAIDSGINLTTDTSKSATSSSPGSPIHSLETSL -> IEVV
FT                   NTFKSGASFQGALRRQSSVTSQSQDVANLSSPSRVSLSNALSSPTSLPPAAAGQG (in
FT                   isoform WA, isoform XA, isoform YA and isoform ZA)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000386"
FT   CONFLICT        92..94
FT                   /note="PKT -> AKP (in Ref. 1; AAA36456)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="P -> R (in Ref. 2; AAA50877/AAA51893)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        517
FT                   /note="G -> D (in Ref. 2; AAA50877/AAA51893)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        667..668
FT                   /note="DG -> EW (in Ref. 1; AAA36456)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1212
FT                   /note="A -> S (in Ref. 1; AAA36456)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         Q01814-2:1165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         Q01814-2:1177
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         Q01814-3:1151
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         Q01814-3:1163
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         Q01814-4:1120
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         Q01814-4:1132
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         Q01814-7:1134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         Q01814-7:1146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
SQ   SEQUENCE   1243 AA;  136876 MW;  7F10221B7B9AC3A2 CRC64;
     MGDMTNSDFY SKNQRNESSH GGEFGCTMEE LRSLMELRGT EAVVKIKETY GDTEAICRRL
     KTSPVEGLPG TAPDLEKRKQ IFGQNFIPPK KPKTFLQLVW EALQDVTLII LEIAAIISLG
     LSFYHPPGEG NEGCATAQGG AEDEGEAEAG WIEGAAILLS VICVVLVTAF NDWSKEKQFR
     GLQSRIEQEQ KFTVVRAGQV VQIPVAEIVV GDIAQVKYGD LLPADGLFIQ GNDLKIDESS
     LTGESDQVRK SVDKDPMLLS GTHVMEGSGR MLVTAVGVNS QTGIIFTLLG AGGEEEEKKD
     KKGVKKGDGL QLPAADGAAA SNAADSANAS LVNGKMQDGN VDASQSKAKQ QDGAAAMEMQ
     PLKSAEGGDA DDRKKASMHK KEKSVLQGKL TKLAVQIGKA GLVMSAITVI ILVLYFTVDT
     FVVNKKPWLP ECTPVYVQYF VKFFIIGVTV LVVAVPEGLP LAVTISLAYS VKKMMKDNNL
     VRHLDACETM GNATAICSDK TGTLTTNRMT VVQAYVGDVH YKEIPDPSSI NTKTMELLIN
     AIAINSAYTT KILPPEKEGA LPRQVGNKTE CGLLGFVLDL KQDYEPVRSQ MPEEKLYKVY
     TFNSVRKSMS TVIKLPDESF RMYSKGASEI VLKKCCKILN GAGEPRVFRP RDRDEMVKKV
     IEPMACDGLR TICVAYRDFP SSPEPDWDNE NDILNELTCI CVVGIEDPVR PEVPEAIRKC
     QRAGITVRMV TGDNINTARA IAIKCGIIHP GEDFLCLEGK EFNRRIRNEK GEIEQERIDK
     IWPKLRVLAR SSPTDKHTLV KGIIDSTHTE QRQVVAVTGD GTNDGPALKK ADVGFAMGIA
     GTDVAKEASD IILTDDNFSS IVKAVMWGRN VYDSISKFLQ FQLTVNVVAV IVAFTGACIT
     QDSPLKAVQM LWVNLIMDTF ASLALATEPP TETLLLRKPY GRNKPLISRT MMKNILGHAV
     YQLALIFTLL FVGEKMFQID SGRNAPLHSP PSEHYTIIFN TFVMMQLFNE INARKIHGER
     NVFDGIFRNP IFCTIVLGTF AIQIVIVQFG GKPFSCSPLQ LDQWMWCIFI GLGELVWGQV
     IATIPTSRLK FLKEAGRLTQ KEEIPEEELN EDVEEIDHAE RELRRGQILW FRGLNRIQTQ
     IRVVKAFRSS LYEGLEKPES RTSIHNFMAH PEFRIEDSQP HIPLIDDTDL EEDAALKQNS
     SPPSSLNKNN SAIDSGINLT TDTSKSATSS SPGSPIHSLE TSL
//