PLCH2_MOUSE
ID PLCH2_MOUSE Reviewed; 1501 AA.
AC A2AP18; A6PWW5; Q3LUA7; Q4QSC7; Q80WP6; Q8BJV1; Q8BWU4; Q8BXN5; Q8CFR1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-2 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000269|PubMed:15899900};
DE AltName: Full=Phosphoinositide phospholipase C-eta-2;
DE AltName: Full=Phosphoinositide phospholipase C-like 4;
DE Short=PLC-L4;
DE Short=Phospholipase C-like protein 4;
DE AltName: Full=Phospholipase C-eta-2;
DE Short=PLC-eta2;
GN Name=Plch2 {ECO:0000312|MGI:MGI:2443078}; Synonyms=Plcl4;
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] (ISOFORM 1), FUNCTION, ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=16107206; DOI=10.1042/bj20050839;
RA Zhou Y., Wing M.R., Sondek J., Harden T.K.;
RT "Molecular cloning and characterization of PLC-eta2.";
RL Biochem. J. 391:667-676(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-664 (ISOFORM 4), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 2-1501 (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 2-246 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye, Hippocampus, and Retina;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-1501 (ISOFORM 2), TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, REGION, FUNCTION, DEVELOPMENTAL STAGE, MUTAGENESIS OF
RP HIS-415, AND CATALYTIC ACTIVITY.
RC STRAIN=C57BL/6J x 129; TISSUE=Brain;
RX PubMed=15899900; DOI=10.1074/jbc.m503817200;
RA Nakahara M., Shimozawa M., Nakamura Y., Irino Y., Morita M., Kudo Y.,
RA Fukami K.;
RT "A novel phospholipase C, PLC(eta)2, is a neuron-specific isozyme.";
RL J. Biol. Chem. 280:29128-29134(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 624-1501 (ISOFORM 3).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676 AND SER-686, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561; SER-565; SER-676 AND
RP SER-686, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: The production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC by activated phosphatidylinositol-specific phospholipase C enzymes.
CC This phospholipase activity is very sensitive to calcium. May be
CC important for formation and maintenance of the neuronal network in the
CC postnatal brain. {ECO:0000269|PubMed:15899900,
CC ECO:0000269|PubMed:16107206}.
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:0000269|PubMed:15899900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000305|PubMed:15899900};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- ACTIVITY REGULATION: Activity is stimulated by GNB1:GNG2.
CC {ECO:0000250|UniProtKB:O75038}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15899900}. Cell
CC membrane {ECO:0000269|PubMed:15899900}. Note=Localized predominantly at
CC the plasma membrane. {ECO:0000269|PubMed:15899900}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=A2AP18-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AP18-2; Sequence=VSP_029082, VSP_029083;
CC Name=3;
CC IsoId=A2AP18-3; Sequence=VSP_029081, VSP_029084;
CC Name=4;
CC IsoId=A2AP18-4; Sequence=VSP_029075, VSP_029077;
CC Name=5;
CC IsoId=A2AP18-5; Sequence=VSP_029076, VSP_029078, VSP_029079;
CC -!- TISSUE SPECIFICITY: Specifically detected in the brain, with higher
CC level in cerebral cortex, olfactory bulb and hippocampus (at protein
CC level). Expressed in the pyramidal cells of the hippocampus, but also
CC in eye and lung. {ECO:0000269|PubMed:15899900,
CC ECO:0000269|PubMed:16107206}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 2 weeks after birth but barely
CC detected 1 week after birth. Increased expression during brain
CC development. {ECO:0000269|PubMed:15899900}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32005.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC32005.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAC37371.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAO78007.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAO78129.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ176851; ABA12210.1; -; mRNA.
DR EMBL; AL831788; CAM16344.2; -; Genomic_DNA.
DR EMBL; BX004788; CAM16344.2; JOINED; Genomic_DNA.
DR EMBL; BX004788; CAM28037.2; -; Genomic_DNA.
DR EMBL; AL831788; CAM28037.2; JOINED; Genomic_DNA.
DR EMBL; AL831788; CAO78007.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX004788; CAO78007.1; JOINED; Genomic_DNA.
DR EMBL; BX004788; CAO78129.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL831788; CAO78129.1; JOINED; Genomic_DNA.
DR EMBL; AK044619; BAC32005.1; ALT_SEQ; mRNA.
DR EMBL; AK049970; BAC34011.1; -; mRNA.
DR EMBL; AK078731; BAC37371.1; ALT_SEQ; mRNA.
DR EMBL; AY966876; AAY33831.1; -; mRNA.
DR EMBL; BC040465; AAH40465.1; -; mRNA.
DR EMBL; BC052329; AAH52329.1; -; mRNA.
DR CCDS; CCDS38990.2; -. [A2AP18-2]
DR CCDS; CCDS71533.1; -. [A2AP18-1]
DR RefSeq; NP_001106831.1; NM_001113360.2. [A2AP18-1]
DR RefSeq; NP_780765.2; NM_175556.4.
DR AlphaFoldDB; A2AP18; -.
DR SMR; A2AP18; -.
DR STRING; 10090.ENSMUSP00000101256; -.
DR SwissLipids; SLP:000000943; -.
DR iPTMnet; A2AP18; -.
DR PhosphoSitePlus; A2AP18; -.
DR SwissPalm; A2AP18; -.
DR MaxQB; A2AP18; -.
DR PaxDb; A2AP18; -.
DR PRIDE; A2AP18; -.
DR ProteomicsDB; 289536; -. [A2AP18-1]
DR ProteomicsDB; 289537; -. [A2AP18-2]
DR ProteomicsDB; 289538; -. [A2AP18-3]
DR ProteomicsDB; 289539; -. [A2AP18-4]
DR ProteomicsDB; 289540; -. [A2AP18-5]
DR Antibodypedia; 1163; 25 antibodies from 13 providers.
DR DNASU; 269615; -.
DR Ensembl; ENSMUST00000105631; ENSMUSP00000101256; ENSMUSG00000029055. [A2AP18-1]
DR Ensembl; ENSMUST00000135665; ENSMUSP00000118292; ENSMUSG00000029055. [A2AP18-4]
DR Ensembl; ENSMUST00000145662; ENSMUSP00000119864; ENSMUSG00000029055. [A2AP18-5]
DR GeneID; 269615; -.
DR KEGG; mmu:269615; -.
DR UCSC; uc008wcq.2; mouse. [A2AP18-5]
DR UCSC; uc056zyr.1; mouse. [A2AP18-1]
DR CTD; 9651; -.
DR MGI; MGI:2443078; Plch2.
DR VEuPathDB; HostDB:ENSMUSG00000029055; -.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000158374; -.
DR HOGENOM; CLU_030679_1_0_1; -.
DR InParanoid; A2AP18; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; A2AP18; -.
DR TreeFam; TF313216; -.
DR BRENDA; 3.1.4.11; 3474.
DR Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR BioGRID-ORCS; 269615; 6 hits in 68 CRISPR screens.
DR ChiTaRS; Plch2; mouse.
DR PRO; PR:A2AP18; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AP18; protein.
DR Bgee; ENSMUSG00000029055; Expressed in habenula and 140 other tissues.
DR ExpressionAtlas; A2AP18; baseline and differential.
DR Genevisible; A2AP18; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; ISS:UniProtKB.
DR GO; GO:0004629; F:phospholipase C activity; IDA:MGI.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:MGI.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR028393; PLC-eta2.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336; PTHR10336; 1.
DR PANTHER; PTHR10336:SF166; PTHR10336:SF166; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF16457; PH_12; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cytoplasm; Hydrolase;
KW Lipid degradation; Lipid metabolism; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transducer.
FT CHAIN 1..1501
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase eta-2"
FT /id="PRO_0000308959"
FT DOMAIN 121..229
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 243..278
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 279..315
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 400..545
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 707..821
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 821..950
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 28..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..229
FT /note="Necessary for plasma membrane localization"
FT REGION 551..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..570
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1442..1461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 459
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 494
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 543
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 545
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 734
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 761
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 865
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 867
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 891
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 920
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 921
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 922
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..105
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029075"
FT VAR_SEQ 40..115
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029076"
FT VAR_SEQ 106..116
FT /note="VSPRWQLSLVV -> MDAGAAPQKHM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029077"
FT VAR_SEQ 580..675
FT /note="ASTNRKRVENIAKKKLDSLIKESKIRDCEDPNDFSVSTLSPSGKLGRKAEAK
FT KGQSKVEEDVEAGEDSGVSRQNSRLFMSSFSKRKKKGSKIKKVA -> VSGSPGSACRE
FT PGVGPQHPRPILSTKGIYLPQRERGQGVRDKDRRWRVREKGKGTREGARGICPGGRGDK
FT GLPLDREETDRQTWPIGKWWFTNVKK (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029078"
FT VAR_SEQ 676..1501
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029079"
FT VAR_SEQ 1068..1252
FT /note="DTRLFPLQRPISPLCSLEPIAEEPALGPGLPLQAAAPTGPSQEGSQCPVGLG
FT AKVTSSQQTSLGAFGTLQLRIGGGRENEEPPLRPHNGGISSGPREGTSGRQTDSKSRSR
FT VPGHLPVVRRAKSEGQVLSELSPTPAVYSDATGTDRLWQRLEPGSHRDSVSSSSSMSSN
FT DTVIDLSLPSLGLCR -> GKAPGGEATEERTLAQVRSPNAPEGPGPAGMAATCMKCVV
FT GSCAGMDVEGLQREQQPSPGPAGSHMAISHQPRARVDSLGGPCCSPSPRATPGRSKEAP
FT KGPRARRQGPGGGSVSSDSSSPDSPGSPKVAPCQPEGAHRQQGALQGEMNALFVQKLEE
FT IRSHSPMFSTGKACRSAASHALYTWHA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029081"
FT VAR_SEQ 1068..1238
FT /note="DTRLFPLQRPISPLCSLEPIAEEPALGPGLPLQAAAPTGPSQEGSQCPVGLG
FT AKVTSSQQTSLGAFGTLQLRIGGGRENEEPPLRPHNGGISSGPREGTSGRQTDSKSRSR
FT VPGHLPVVRRAKSEGQVLSELSPTPAVYSDATGTDRLWQRLEPGSHRDSVSSSSSMSSN
FT D -> GKAPGGEATEERTLAQVRSPNAPEGPGPAGMAATCMKCVVGSCAGMDVEGLRRE
FT QQPSPGPAGSHMAISHQPRARVDSLGGPCCSPSPRATPGRSKEAPKGPRARRQGPGGGS
FT VSSDSSSPDSPGSPKVAPCQPEGAHRQQGALQGEMNALFVQKLEEIRSHSPMFSTVRD
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15899900"
FT /id="VSP_029082"
FT VAR_SEQ 1239..1501
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15899900"
FT /id="VSP_029083"
FT VAR_SEQ 1253..1501
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029084"
FT MUTAGEN 415
FT /note="H->A: Inhibition of activity."
FT /evidence="ECO:0000269|PubMed:15899900"
FT CONFLICT 340
FT /note="F -> L (in Ref. 3; BAC34011)"
FT /evidence="ECO:0000305"
FT CONFLICT 664..665
FT /note="RK -> HR (in Ref. 5; AAH40465)"
FT /evidence="ECO:0000305"
FT CONFLICT 781
FT /note="N -> D (in Ref. 3; BAC32005)"
FT /evidence="ECO:0000305"
FT CONFLICT 1258
FT /note="P -> A (in Ref. 3; BAC32005)"
FT /evidence="ECO:0000305"
FT CONFLICT 1495
FT /note="G -> S (in Ref. 3; BAC32005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1501 AA; 164297 MW; 6C2CA0E2864B327B CRC64;
MGGLAWGPSR AAGSSWVNAS GTWEQPLRGF SGLQGGRRRG RGEKGIPEEP LCQLTPQLGL
SLRVPFGLGD YGLDMPGPQP SAASQTTGAV ACLAEVLLWV GGSVVVSPRW QLSLVVERCM
SAMQEGTQMV KLRGSSKGLV RFYYLDEHRS CLRWRPSRKN EKAKISIDSI QEVSEGRQSE
IFQRYPDSSF DPNCCFSIYH GSHRESLDLV SPSSEEARTW VTGLRYLMAG ISDEDSLARR
QRTRDQWLKQ TFDEADKNGD GSLSISEVLQ LLHKLNVNLP RQRVKQMFRE ADTDDHQGTL
GFEEFCAFYK MMSTRRDLYL LMLTYSNHKD HLDASDLQRF LEVEQKMNGV TLESCQNIIE
QFEPCLENKS KGMLGIDGFT NYTRSPAGDI FNPEHNRVHQ DMTQPLSHYF ITSSHNTYLV
GDQLMSQSRV DMYAWVLQAG CRCVEVDCWD GPDGEPIVHH GYTLTSKILF KDVIETINKY
AFIKNEYPVI LSIENHCSVV QQKKMAQYLT DILGDKLDLS SVSSEDATML PSPQMLKGKI
LVKGKKLPAN ISEDAEEGEV SDEDSADEME DDCKLLNGDA STNRKRVENI AKKKLDSLIK
ESKIRDCEDP NDFSVSTLSP SGKLGRKAEA KKGQSKVEED VEAGEDSGVS RQNSRLFMSS
FSKRKKKGSK IKKVASVEEG DETLDSPGSQ SRGTARQKKT MKLSRALSDL VKYTKSVGTH
DVEIEVVSSW QVSSFSETKA HQILQQKPTQ YLRFNQHQLS RIYPSSYRVD SSNYNPQPFW
NAGCQMVALN YQSEGRMLQL NRAKFSANGD CGYVLKPQCM CQGVFNPNSE DPLPGQLKKQ
LALRIISGQQ LPKPRDSVLG DRGEIIDPFV EVEVIGLPVD CSKEQTRVVD DNGFNPMWEE
TLVFTVHMPE IALVRFLVWD HDPIGRDFIG QRTLAFSSIM PGYRHVYLEG MEEASIFVHV
AVSDISGKVK QTLGLKGLFL RGTKPGSLDS HAAGQPLPRP SVSQRLLRRT ASAPTKSQKP
SRKGFPELAL GTQDAGSEGA ADDVAPSSPN PALEAPTQER SGSSSPRDTR LFPLQRPISP
LCSLEPIAEE PALGPGLPLQ AAAPTGPSQE GSQCPVGLGA KVTSSQQTSL GAFGTLQLRI
GGGRENEEPP LRPHNGGISS GPREGTSGRQ TDSKSRSRVP GHLPVVRRAK SEGQVLSELS
PTPAVYSDAT GTDRLWQRLE PGSHRDSVSS SSSMSSNDTV IDLSLPSLGL CRSRESIPGV
SLGRLTSRPC LASAARPDLP PVTKSKSNPN LRVAGGLPTA PDELQPRPLA PRLTGHHPRP
PWHHLTLVGL RDCPVSAKSK SLGDLTADDF APSFQGSTSS LSCGLGSLGV AHQVLEPGIR
RDALTEQLRW LTGFQQAGDI TSPTSLGPAG DGSVGGPSFL RRSSSRSQSR VRAIASRARQ
AQERQQRLRG QDSRGPPEEE RGTPEGACSV GHEGCVDVPM PAKGAPEQVC GAADGQLLLR
L
