AT2B2_RAT
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 03-AUG-2022, entry version 200.
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}.
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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.ENSRNOP00000063572; -.
DR iPTMnet; P11506; -.
DR PhosphoSitePlus; P11506; -.
DR PRIDE; P11506; -.
DR Ensembl; ENSRNOT00000095628; ENSRNOP00000090928; ENSRNOG00000030269. [P11506-13]
DR GeneID; 24215; -.
DR KEGG; rno:24215; -.
DR UCSC; RGD:2176; rat. [P11506-13]
DR CTD; 491; -.
DR RGD; 2176; Atp2b2.
DR eggNOG; KOG0204; Eukaryota.
DR GeneTree; ENSGT00940000161461; -.
DR InParanoid; P11506; -.
DR OrthoDB; 115892at2759; -.
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 tissues.
DR ExpressionAtlas; P11506; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IDA: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:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
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; 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:1905056; F:P-type calcium transporter activity involved in regulation of presynaptic cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; 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: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: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: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 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; 1.
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 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
