ID   PLCB3_MOUSE             Reviewed;        1234 AA.
AC   P51432; Q3UIS0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   02-SEP-2026, entry version 205.
DE   RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 {ECO:0000305};
DE            EC=3.1.4.11 {ECO:0000250|UniProtKB:Q99JE6};
DE   AltName: Full=Phosphoinositide phospholipase C-beta-3;
DE   AltName: Full=Phospholipase C-beta-3;
DE            Short=PLC-beta-3;
GN   Name=Plcb3 {ECO:0000312|MGI:MGI:104778};
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=Kidney;
RX   PubMed=9714794; DOI=10.1016/s0005-2760(98)00074-5;
RA   Wang S., Zhou Y., Lukinius A., Oberg K., Skogseid B., Gobl A.;
RT   "Molecular cloning and characterization of a cDNA encoding mouse
RT   phospholipase C-beta3.";
RL   Biochim. Biophys. Acta 1393:173-178(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
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   [5]
RP   FUNCTION.
RX   PubMed=22728827; DOI=10.1038/emboj.2012.167;
RA   Suire S., Lecureuil C., Anderson K.E., Damoulakis G., Niewczas I.,
RA   Davidson K., Guillou H., Pan D., Clark J., Hawkins P.T., Stephens L.;
RT   "GPCR activation of Ras and PI3Kc in neutrophils depends on PLCb2/b3 and
RT   the RasGEF RasGRP4.";
RL   EMBO J. 31:3118-3129(2012).
CC   -!- FUNCTION: Catalyzes the production of the second messenger molecules
CC       diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (By
CC       similarity). Key transducer of G protein-coupled receptor signaling:
CC       activated by G(q)/G(11) G alpha proteins downstream of G protein-
CC       coupled receptors activation (PubMed:22728827). In neutrophils,
CC       participates in a phospholipase C-activating N-formyl peptide-activated
CC       GPCR (G protein-coupled receptor) signaling pathway by promoting
CC       RASGRP4 activation by DAG, to promote neutrophil functional responses
CC       (PubMed:22728827). In conjunction with OSBPL2, it may contribute to the
CC       control of keratinocyte proliferation and differentiation, probably
CC       through the regulation of the ERK pathway and the cell cycle (By
CC       similarity). {ECO:0000250|UniProtKB:Q01970,
CC       ECO:0000269|PubMed:22728827}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC         bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC         diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC         ChEBI:CHEBI:203600; EC=3.1.4.11;
CC         Evidence={ECO:0000250|UniProtKB:Q99JE6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC         Evidence={ECO:0000250|UniProtKB:Q99JE6};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O =
CC         1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+);
CC         Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433;
CC         Evidence={ECO:0000250|UniProtKB:Q99JE6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC         Evidence={ECO:0000250|UniProtKB:Q99JE6};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by G(q)/G(11) G alpha proteins in
CC       response to ligand-binding to G protein-coupled receptors.
CC       {ECO:0000250|UniProtKB:Q01970}.
CC   -!- SUBUNIT: Interacts with SHANK2 (By similarity). Interacts with LPAR2
CC       (By similarity). Interacts with OSBPL2; the interaction inhibits PLCB3
CC       ubiquitination and degradation (By similarity).
CC       {ECO:0000250|UniProtKB:Q01970, ECO:0000250|UniProtKB:Q99JE6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q01970}.
CC       Membrane {ECO:0000250|UniProtKB:Q01970}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q01970}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q01970}. Nucleus {ECO:0000269|PubMed:9714794}.
CC       Note=An heterotetramer composed of GNG2 and GNB1 increases the
CC       concentration of PLCB3 on the membrane surface, where its substrate
CC       PIP2 resides, by orienting its catalytic site.
CC       {ECO:0000250|UniProtKB:Q01970}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in kidney, skeletal muscle, liver,
CC       lung, heart and brain. {ECO:0000269|PubMed:9714794}.
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DR   EMBL; U43144; AAA85199.1; -; mRNA.
DR   EMBL; AK146793; BAE27436.1; -; mRNA.
DR   EMBL; CH466612; EDL33267.1; -; Genomic_DNA.
DR   CCDS; CCDS70925.1; -.
DR   RefSeq; NP_001277278.1; NM_001290349.1.
DR   RefSeq; NP_032900.2; NM_008874.4.
DR   AlphaFoldDB; P51432; -.
DR   SMR; P51432; -.
DR   BioGRID; 202234; 5.
DR   FunCoup; P51432; 1273.
DR   IntAct; P51432; 1.
DR   MINT; P51432; -.
DR   STRING; 10090.ENSMUSP00000025912; -.
DR   GlyGen; P51432; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P51432; -.
DR   PhosphoSitePlus; P51432; -.
DR   SwissPalm; P51432; -.
DR   jPOST; P51432; -.
DR   PaxDb; 10090-ENSMUSP00000025912; -.
DR   PeptideAtlas; P51432; -.
DR   ProteomicsDB; 289672; -.
DR   Pumba; P51432; -.
DR   Antibodypedia; 3983; 415 antibodies from 39 providers.
DR   DNASU; 18797; -.
DR   Ensembl; ENSMUST00000025912.10; ENSMUSP00000025912.9; ENSMUSG00000024960.10.
DR   GeneID; 18797; -.
DR   KEGG; mmu:18797; -.
DR   UCSC; uc008gjr.2; mouse.
DR   AGR; MGI:104778; -.
DR   CTD; 5331; -.
DR   MGI; MGI:104778; Plcb3.
DR   VEuPathDB; HostDB:ENSMUSG00000024960; -.
DR   eggNOG; KOG1265; Eukaryota.
DR   GeneTree; ENSGT00940000160539; -.
DR   HOGENOM; CLU_002738_2_0_1; -.
DR   InParanoid; P51432; -.
DR   OMA; IWSEELF; -.
DR   OrthoDB; 269822at2759; -.
DR   PhylomeDB; P51432; -.
DR   Reactome; R-MMU-112043; PLC beta mediated events.
DR   Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR   Reactome; R-MMU-399997; Acetylcholine regulates insulin secretion.
DR   Reactome; R-MMU-4086398; Ca2+ pathway.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   Reactome; R-MMU-418217; G beta:gamma signalling through PLC beta.
DR   Reactome; R-MMU-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR   Reactome; R-MMU-500657; Presynaptic function of Kainate receptors.
DR   BioGRID-ORCS; 18797; 4 hits in 75 CRISPR screens.
DR   PRO; PR:P51432; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; P51432; protein.
DR   Bgee; ENSMUSG00000024960; Expressed in crypt of Lieberkuhn of small intestine and 218 other cell types or tissues.
DR   ExpressionAtlas; P51432; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0098562; C:cytoplasmic side of membrane; ISO:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:GO_Central.
DR   GO; GO:0005634; C:nucleus; EXP:UniProtKB.
DR   GO; GO:0099524; C:postsynaptic cytosol; IDA:UniProt.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0042383; C:sarcolemma; ISO:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; ISO:GO_Central.
DR   GO; GO:0031681; F:G-protein beta-subunit binding; ISO:GO_Central.
DR   GO; GO:0031682; F:G-protein gamma-subunit binding; ISO:GO_Central.
DR   GO; GO:0060090; F:molecular adaptor activity; ISO:GO_Central.
DR   GO; GO:0140677; F:molecular function activator activity; ISO:GO_Central.
DR   GO; GO:0120548; F:phosphatidylinositol phospholipase C activity; ISS:UniProtKB.
DR   GO; GO:0004435; F:phosphatidylinositol-4,5-bisphosphate phospholipase C activity; IDA:UniProt.
DR   GO; GO:0140582; P:adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:0032957; P:inositol trisphosphate metabolic process; ISO:GO_Central.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR   GO; GO:0031161; P:phosphatidylinositol catabolic process; ISO:GO_Central.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:UniProt.
DR   GO; GO:0007208; P:phospholipase C-activating serotonin receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:0006892; P:post-Golgi vesicle-mediated transport; ISO:GO_Central.
DR   GO; GO:0003073; P:regulation of systemic arterial blood pressure; ISO:MGI.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR   CDD; cd00275; C2_PLC_like; 1.
DR   CDD; cd16210; EFh_PI-PLCbeta3; 1.
DR   CDD; cd13361; PH_PLC_beta; 1.
DR   CDD; cd08591; PI-PLCc_beta; 1.
DR   FunFam; 1.10.238.10:FF:000048; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase; 1.
DR   FunFam; 1.20.1230.10:FF:000003; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase; 1.
DR   FunFam; 2.30.29.240:FF:000005; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase; 1.
DR   FunFam; 2.60.40.150:FF:000008; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase; 1.
DR   Gene3D; 2.30.29.240; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   Gene3D; 1.20.1230.10; Phospholipase C beta, distal C-terminal domain; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR001192; PI-PLC_fam.
DR   InterPro; IPR016280; PLC-beta.
DR   InterPro; IPR014815; PLC-beta_C.
DR   InterPro; IPR042531; PLC-beta_C_sf.
DR   InterPro; IPR037862; PLC-beta_PH.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR053945; PLCB1-4-like_EFh.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR   PANTHER; PTHR10336:SF11; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-3; 1.
DR   PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF17787; PH_14; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   Pfam; PF08703; PLC-beta_C; 1.
DR   Pfam; PF22631; PLCB1-4-like_EFh; 1.
DR   PIRSF; PIRSF000956; PLC-beta; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF69989; C-terminal domain of PLC-beta; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Calcium; Cytoplasm; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Membrane; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transducer.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   CHAIN           2..1234
FT                   /note="1-phosphatidylinositol 4,5-bisphosphate
FT                   phosphodiesterase beta-3"
FT                   /id="PRO_0000088492"
FT   DOMAIN          318..468
FT                   /note="PI-PLC X-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   DOMAIN          591..707
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT   DOMAIN          708..836
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          466..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          888..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1001..1026
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1207..1234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1231..1234
FT                   /note="Interaction with SHANK2"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        488..515
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..568
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..588
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        888..907
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        925..936
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1222..1234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        332
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   ACT_SITE        379
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   BINDING         333
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   BINDING         362
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   BINDING         364
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   BINDING         413
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   MOD_RES         474
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   MOD_RES         490
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   MOD_RES         495
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   MOD_RES         537
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         927
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   MOD_RES         1105
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01970"
FT   CONFLICT        16
FT                   /note="P -> S (in Ref. 1; AAA85199)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        20
FT                   /note="E -> K (in Ref. 1; AAA85199)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        609
FT                   /note="A -> S (in Ref. 1; AAA85199)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1234 AA;  139487 MW;  E055744A33C5F6B0 CRC64;
     MAGARPGVHA LQLEPPTVVE TLRRGSKFIK WDEEASSRNL VTLRVDPNGF FLYWTGPNME
     VDTLDISSIR DTRTGRYARL PKDPKIREVL GFGGPDTRLE EKLMTVVAGP DPVNTTFLNF
     MAVQDDTVKV WSEELFKLAM NILAQNASRN TFLRKAYTKL KLQVNQDGRI PVKNILKMFS
     ADKKRVETAL ESCGLNFNRS ESIRPDEFPL EIFERFLNKL CLRPDIDKIL LEIGAKGKPY
     LTLEQLMDFI NQKQRDPRLN EVLYPPLRSS QARLLIEKYE TNKQFLERDQ MSMEGFSRYL
     GGEENGILPL EALDLSMDMT QPLSAYFINS SHNTYLTAGQ LAGPSSVEMY RQALLWGCRC
     VELDVWKGRP PEEEPFITHG FTMTTEVPLR DVLEAIAEAA FKTSPYPVIL SFENHVDSAK
     QQAKMAEYCR SIFGDALLID PLDKYPLSAG IPLPSPQDLM GRILVKNKKR HRPSTGVPDS
     SVRKRPLEQS NSALSESSAA TEPSSPQLGS PSSDSCPGLS NGEEVGLEKT SLEPQKSLGE
     ESLSREPNVP MPDRDREDEE EDEEEEETTD PKKPTTDEGT ASSEVNATEE MSTLVNYVEP
     VKFKSFEAAR KRNKCFEMSS FVETKAMEQL TKSPMEFVEY NKQQLSRIYP KGTRVDSSNY
     MPQLFWNVGC QLVALNFQTL DLPMQLNAGV FEYNGRSGYL LKPEFMRRPD KSFDPFTEVI
     VDGIVANALR VKVISGQFLS DKKVGIYVEV DMFGLPVDTR RKYRTRTSQG NSFNPVWDEE
     PFDFPKVVLP TLASLRIAAF EEGGKFVGHR ILPVSAIRSG YHYVCLRNEA NQPLCLPALL
     IYTEASDYIP DDHQDYAEAL INPIKHVSLM DQRAKQLAAL IGESEAQAST ETYQETPCQQ
     PGSQLPSNPT PNPLDASPRW PPGPTTSSTS SSLSSPGQRD DLIASILSEV TPTPLEELRS
     HKAMVKLRSR QDRDLRELHK KHQRKAVALT RRLLDGLAQA RAEGKCRPSP SALGKATNSE
     DVKEEEEAKQ YREFQNRQVQ SLLELREAQA DVETKRKLEH LRQAHQRLKE VVLDTHTTQF
     KRLKELNERE KKELQKILDR KRNNSISEAK TREKHKKEVE LTEINRRHIT ESVNSIRRLE
     EAQKQRHERL VAGQQQVLQQ LEEEEPKLLA QLTQECQEQR ERLPQEIRRC LLGETAEGLG
     DGPLVACASN GHAPGSGGHL SSADSESQEE NTQL
//