ID AT2B2_RAT Reviewed; 1243 AA. AC P11506; Q63443; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 27-MAR-2024, entry version 209. DE RecName: Full=Plasma membrane calcium-transporting ATPase 2; DE Short=PMCA2; DE EC=7.2.2.10 {ECO:0000250|UniProtKB:Q01814, ECO:0000250|UniProtKB:Q9R0K7}; DE AltName: Full=Plasma membrane calcium ATPase isoform 2; DE AltName: Full=Plasma membrane calcium pump isoform 2; GN Name=Atp2b2; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC STRAIN=Sprague-Dawley; TISSUE=Brain; RX PubMed=2837461; DOI=10.1016/s0021-9258(18)68354-1; RA Shull G.E., Greeb J.; RT "Molecular cloning of two isoforms of the plasma membrane Ca2+-transporting RT ATPase from rat brain. Structural and functional domains exhibit similarity RT to Na+,K+- and other cation transport ATPases."; RL J. Biol. Chem. 263:8646-8657(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1083-1243 (ISOFORMS WB/XB/YB/ZB), AND RP ALTERNATIVE SPLICING. RX PubMed=1315513; DOI=10.1042/bj2830355; RA Adamo H.P., Penniston J.T.; RT "New Ca2+ pump isoforms generated by alternative splicing of rPMCA2 mRNA."; RL Biochem. J. 283:355-359(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1083-1243 (ISOFORMS WB/XB/YB/ZB), AND RP ALTERNATIVE SPLICING. RC STRAIN=Sprague-Dawley; RX PubMed=8428948; DOI=10.1016/s0021-9258(18)53836-9; RA Keeton T.P., Burk S.E., Shull G.E.; RT "Alternative splicing of exons encoding the calmodulin-binding domains and RT C termini of plasma membrane Ca(2+)-ATPase isoforms 1, 2, 3, and 4."; RL J. Biol. Chem. 268:2740-2748(1993). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND THR-1188, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1152 (ISOFORMS WA; WB AND RP WC), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1162 AND SER-1175 RP (ISOFORM WB), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1161 (ISOFORMS RP WB AND YB), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1121 (ISOFORMS RP XA; XB AND XC), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1131 AND RP SER-1144 (ISOFORM XB), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1130 RP (ISOFORMS XB AND ZB), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1138 RP (ISOFORMS YA; YB AND YC), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT RP SER-1147 AND SER-1148 (ISOFORM YB), PHOSPHORYLATION [LARGE SCALE ANALYSIS] RP AT SER-1107 (ISOFORMS ZA; ZB AND ZC), PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-1116 AND SER-1117 (ISOFORM ZB), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). 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. Uses ATP as an energy CC source to transport cytosolic Ca(2+) ions across the plasma membrane to CC the extracellular compartment (By similarity). Has fast activation and CC Ca(2+) clearance rate suited to control fast neuronal Ca(2+) dynamics. CC At parallel fiber to Purkinje neuron synapse, mediates presynaptic CC Ca(2+) efflux in response to climbing fiber-induced Ca(2+) rise. CC Provides for fast return of Ca(2+) concentrations back to their resting CC levels, ultimately contributing to long-term depression induction and CC motor learning (By similarity). Plays an essential role in hearing and CC balance. In cochlear hair cells, shuttles Ca(2+) ions from stereocilia CC to the endolymph and dissipates Ca(2+) transients generated by the CC opening of the mechanoelectrical transduction channels. Regulates CC Ca(2+) levels in the vestibular system, where it contributes to the CC formation of otoconia (By similarity). In non-excitable cells, CC regulates Ca(2+) signaling through spatial control of Ca(2+) ions CC extrusion and dissipation of Ca(2+) transients generated by store- CC operated channels (By similarity). In lactating mammary gland, allows CC for the high content of Ca(2+) ions in the milk (By similarity). CC {ECO:0000250|UniProtKB:Q01814, ECO:0000250|UniProtKB:Q9R0K7}. 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:0000250|UniProtKB:Q01814, CC ECO:0000250|UniProtKB:Q9R0K7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106; CC Evidence={ECO:0000250|UniProtKB:Q01814, CC ECO:0000250|UniProtKB:Q9R0K7}; 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}. Synapse CC {ECO:0000250|UniProtKB:Q9R0K7}. 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}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=14; CC Comment=There is a combination of two alternatively spliced domains CC at N-terminal site A (W, X, Y and Z) and at C-terminal site C (A, B CC and C). So far the splice sites have only been studied independently. CC Experimental confirmation may be lacking for some isoforms.; CC Name=1; CC IsoId=P11506-13; Sequence=Displayed; CC Name=WB; Synonyms=AIIICI; CC IsoId=P11506-1; Sequence=VSP_038681, VSP_038682; CC Name=WA; Synonyms=AIIICII; CC IsoId=P11506-2; Sequence=VSP_000390; CC Name=XA; Synonyms=AIICII; CC IsoId=P11506-3; Sequence=VSP_000387, VSP_000390; CC Name=YA; Synonyms=AIIICII; CC IsoId=P11506-4; Sequence=VSP_000389, VSP_000390; CC Name=ZA; Synonyms=AICII; CC IsoId=P11506-5; Sequence=VSP_000388, VSP_000390; CC Name=XB; Synonyms=AIICI; CC IsoId=P11506-6; Sequence=VSP_000387, VSP_038681, VSP_038682; CC Name=YB; Synonyms=AIIICI; CC IsoId=P11506-7; Sequence=VSP_000389, VSP_038681, VSP_038682; CC Name=ZB; Synonyms=AICI; CC IsoId=P11506-8; Sequence=VSP_000388, VSP_038681, VSP_038682; CC Name=WC; Synonyms=AIIICIII; CC IsoId=P11506-9; Sequence=VSP_000391; CC Name=XC; Synonyms=AIICIII; CC IsoId=P11506-10; Sequence=VSP_000387, VSP_000391; CC Name=YC; Synonyms=AIIICIII; CC IsoId=P11506-11; Sequence=VSP_000389, VSP_000391; CC Name=ZC; Synonyms=AICIII; CC IsoId=P11506-12; Sequence=VSP_000388, VSP_000391; CC Name=2; CC IsoId=P11506-14; Sequence=VSP_000388; CC -!- TISSUE SPECIFICITY: Isoforms containing segment B are found in brain, CC uterus, liver and kidney and in low levels in other tissues. Isoforms CC containing segment W are found in kidney, uterus, and pancreas. CC Isoforms containing segment Y are found in pancreas and in low levels CC in brain and heart. Isoforms containing segment Z are found in brain CC and heart and isoforms containing segment X are found in low levels in CC brain. Isoforms containing segment A are found in low levels in heart CC and small intestine while isoforms containing segment C are found in CC testis and in low levels in other tissues. CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) CC family. Type IIB 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; J03754; AAA74219.1; -; mRNA. DR EMBL; AH005430; AAB60703.1; -; Genomic_DNA. DR PIR; B28065; B28065. DR RefSeq; NP_036640.1; NM_012508.5. [P11506-14] DR AlphaFoldDB; P11506; -. DR SMR; P11506; -. DR BioGRID; 246403; 2. DR IntAct; P11506; 2. DR MINT; P11506; -. DR STRING; 10116.ENSRNOP00000045983; -. DR iPTMnet; P11506; -. DR PhosphoSitePlus; P11506; -. DR PaxDb; 10116-ENSRNOP00000063572; -. DR Ensembl; ENSRNOT00000095628.1; ENSRNOP00000090928.1; ENSRNOG00000030269.7. [P11506-13] DR Ensembl; ENSRNOT00065049048; ENSRNOP00065040228; ENSRNOG00065028357. [P11506-13] DR GeneID; 24215; -. DR KEGG; rno:24215; -. DR UCSC; RGD:2176; rat. [P11506-13] DR AGR; RGD:2176; -. DR CTD; 491; -. DR RGD; 2176; Atp2b2. DR eggNOG; KOG0204; Eukaryota. DR GeneTree; ENSGT00940000161461; -. DR InParanoid; P11506; -. DR OMA; IQHCKRA; -. DR OrthoDB; 847at2759; -. DR PhylomeDB; P11506; -. DR BRENDA; 7.2.2.10; 5301. DR Reactome; R-RNO-418359; Reduction of cytosolic Ca++ levels. DR Reactome; R-RNO-5578775; Ion homeostasis. DR Reactome; R-RNO-936837; Ion transport by P-type ATPases. DR PRO; PR:P11506; -. DR Proteomes; UP000002494; Chromosome 4. DR Bgee; ENSRNOG00000030269; Expressed in frontal cortex and 9 other cell types or tissues. DR ExpressionAtlas; P11506; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005929; C:cilium; ISO:RGD. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0030425; C:dendrite; IDA:RGD. DR GO; GO:0032591; C:dendritic spine membrane; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD. DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0043005; C:neuron projection; ISO:RGD. DR GO; GO:0043025; C:neuronal cell body; IDA:RGD. DR GO; GO:0032809; C:neuronal cell body membrane; IDA:RGD. DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO. DR GO; GO:0098684; C:photoreceptor ribbon synapse; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO. DR GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO. DR GO; GO:0048787; C:presynaptic active zone membrane; IDA:SynGO. DR GO; GO:0042734; C:presynaptic membrane; ISO:RGD. DR GO; GO:0005524; F:ATP binding; IDA:RGD. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0030899; F:calcium-dependent ATPase activity; ISO:RGD. DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB. DR GO; GO:0035254; F:glutamate receptor binding; IPI:RGD. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005388; F:P-type calcium transporter activity; IDA:RGD. DR GO; GO:1905059; F:P-type calcium transporter activity involved in regulation of postsynaptic cytosolic calcium ion concentration; ISO:RGD. DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD. DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISO:RGD. DR GO; GO:0006816; P:calcium ion transport; ISO:RGD. DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD. DR GO; GO:0021707; P:cerebellar granule cell differentiation; ISO:RGD. DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; ISO:RGD. DR GO; GO:0021692; P:cerebellar Purkinje cell layer morphogenesis; ISO:RGD. DR GO; GO:0021549; P:cerebellum development; ISO:RGD. DR GO; GO:0046068; P:cGMP metabolic process; ISO:RGD. DR GO; GO:0090102; P:cochlea development; ISO:RGD. DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISO:RGD. DR GO; GO:0051649; P:establishment of localization in cell; ISO:RGD. DR GO; GO:0048839; P:inner ear development; ISO:RGD. DR GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD. DR GO; GO:0060113; P:inner ear receptor cell differentiation; ISO:RGD. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; ISO:RGD. DR GO; GO:0007595; P:lactation; ISO:RGD. DR GO; GO:0040011; P:locomotion; ISO:RGD. DR GO; GO:0007626; P:locomotory behavior; ISO:RGD. DR GO; GO:0003407; P:neural retina development; IEP:RGD. DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD. DR GO; GO:0070050; P:neuron cellular homeostasis; ISO:RGD. DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB. DR GO; GO:0006996; P:organelle organization; ISO:RGD. DR GO; GO:0045299; P:otolith mineralization; ISO:RGD. DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:RGD. DR GO; GO:0008361; P:regulation of cell size; ISO:RGD. DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:RGD. DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD. DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB. DR GO; GO:0042428; P:serotonin metabolic process; ISO:RGD. DR GO; GO:0050808; P:synapse organization; ISO:RGD. DR CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1. DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1. DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1. DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 3. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. 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 NCBIfam; TIGR01517; ATPase-IIB_Ca; 1. DR NCBIfam; TIGR01494; ATPase_P-type; 3. DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1. DR PANTHER; PTHR24093:SF377; PLASMA MEMBRANE CALCIUM-TRANSPORTING ATPASE 2; 1. DR Pfam; PF12424; ATP_Ca_trans_C; 1. DR Pfam; PF13246; Cation_ATPase; 1. DR Pfam; PF00689; Cation_ATPase_C; 1. DR Pfam; PF00690; Cation_ATPase_N; 1. DR Pfam; PF00122; E1-E2_ATPase; 2. DR Pfam; PF00702; Hydrolase; 1. DR PRINTS; PR00119; CATATPASE. DR PRINTS; PR00121; NAKATPASE. DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1. DR SFLD; SFLDF00027; p-type_atpase; 1. DR SMART; SM00831; Cation_ATPase_N; 1. DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1. DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1. 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 membrane; Ion transport; Magnesium; Membrane; KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; KW Synapse; Translocase; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..1243 FT /note="Plasma membrane calcium-transporting ATPase 2" FT /id="PRO_0000046216" 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 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 296..382 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 REGION 1194..1243 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 326..351 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 365..382 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1195..1243 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 499 FT /note="4-aspartylphosphate intermediate" FT BINDING 820 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 824 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT MOD_RES 18 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9R0K7" FT MOD_RES 27 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" 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:0007744|PubMed:22673903" 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:0000250|UniProtKB:Q01814" FT VAR_SEQ 303..347 FT /note="Missing (in isoform 2, isoform ZA, isoform ZB and FT isoform ZC)" FT /evidence="ECO:0000303|PubMed:2837461" FT /id="VSP_000388" FT VAR_SEQ 303..333 FT /note="Missing (in isoform XA, isoform XB and isoform XC)" FT /evidence="ECO:0000305" FT /id="VSP_000387" FT VAR_SEQ 334..347 FT /note="Missing (in isoform YA, isoform YB and isoform YC)" FT /evidence="ECO:0000305" FT /id="VSP_000389" 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_000390" FT VAR_SEQ 1141..1243 FT /note="IRVVKAFRSSLYEGLEKPESRTSIHNFMAHPEFRIEDSQPHIPLIDDTDLEE FT DAALKQNSSPPSSLNKNNSAIDSGINLTTDTSKSATSSSPGSPIHSLETSL -> IEVV FT NTFKSGASFQGALRRQSSVTSQSQDVANLSSPSRVSLSNALSSPTSLPPAAAGHPRREG FT VP (in isoform WC, isoform XC, isoform YC and isoform ZC)" FT /evidence="ECO:0000305" FT /id="VSP_000391" FT VAR_SEQ 1141 FT /note="I -> IEVVNTFKSGASFQGALRRQSSVTSQSQDVASLSSPSRVSLSNALSS FT PTSLPPAAAGI (in isoform WB, isoform XB, isoform YB and FT isoform ZB)" FT /evidence="ECO:0000305" FT /id="VSP_038681" FT VAR_SEQ 1201..1243 FT /note="Missing (in isoform WB, isoform XB, isoform YB and FT isoform ZB)" FT /evidence="ECO:0000305" FT /id="VSP_038682" FT MOD_RES P11506-1:1152 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-1:1161 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-1:1162 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-1:1175 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-2:1152 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-3:1121 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-4:1138 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-5:1107 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-6:1121 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-6:1130 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-6:1131 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-6:1144 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-7:1138 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-7:1147 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-7:1148 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-7:1161 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-8:1107 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-8:1116 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-8:1117 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-8:1130 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-9:1152 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-10:1121 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-11:1138 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES P11506-12:1107 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" SQ SEQUENCE 1243 AA; 136811 MW; 1DC324836BFD5D59 CRC64; MGDMTNSDFY SKNQRNESSH GGEFGCSMEE LRSLMELRGT EAVVKIKETY GDTESICRRL KTSPVEGLPG TAPDLEKRKQ IFGQNFIPPK KPKTFLQLVW EALQDVTLII LEIAAIISLG LSFYHPPGES NEGCATAQGG AEDEGEAEAG WIEGAAILLS VICVVLVTAF NDWSKEKQFR GLQSRIEQEQ KFTVVRAGQV VQIPVAEIVV GDIAQIKYGD LLPADGLFIQ GNDLKIDESS LTGESDQVRK SVDKDPMLLS GTHVMEGSGR MVVTAVGVNS QTGIIFTLLG AGGEEEEKKD KKGVKKGDGL QLPAADGAAP ANAAGSANAS LVNGKMQDGS ADSSQSKAKQ QDGAAAMEMQ PLKSAEGGDA DDKKKANMHK KEKSVLQGKL TKLAVQIGKA GLVMSAITVI ILVLYFTVDT FVVNKKPWLT ECTPVYVQYF VKFFIIGVTV LVVAVPEGLP LAVTISLAYS VKKMMKDNNL VRHLDACETM GNATAICSDK TGTLTTNRMT VVQAYVGDVH YKEIPDPSSI NAKTLELLVN AIAINSAYTT KILPPEKEGA LPRQVGNKTE CGLLGFVLDL RQDYEPVRSQ MPEEKLYKVY TFNSVRKSMS TVIKMPDESF RMYSKGASEI VLKKCCKILS 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 YQLTLIFTLL 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 //