ID PLCH2_HUMAN Reviewed; 1416 AA. AC O75038; A2VCM3; B9DI80; Q3LUA8; Q86XJ2; Q86XU1; Q86YU7; Q8TEH5; Q8WUS6; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 3. DT 24-JAN-2024, entry version 185. DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-2 {ECO:0000305}; DE EC=3.1.4.11 {ECO:0000269|PubMed:18361507}; 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|HGNC:HGNC:29037}; Synonyms=KIAA0450, PLCL4; 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 1), AND TISSUE SPECIFICITY. 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 MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 556-1403 (ISOFORM 4). RC TISSUE=Spleen; RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.; RT "The nucleotide sequence of a long cDNA clone isolated from human spleen."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=9455484; DOI=10.1093/dnares/4.5.345; RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., RA Nomura N., Ohara O.; RT "Characterization of cDNA clones in size-fractionated cDNA libraries from RT human brain."; RL DNA Res. 4:345-349(1997). RN [4] RP SEQUENCE REVISION. RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., RA Nomura N., Ohara O.; RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 116-1416 (ISOFORM 1), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 143-1416 (ISOFORM 3). RC TISSUE=Brain, Pancreas, and Skin; 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 [7] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY RP REGULATION. RX PubMed=18361507; DOI=10.1021/bi800044n; RA Zhou Y., Sondek J., Harden T.K.; RT "Activation of human phospholipase C-eta2 by Gbetagamma."; RL Biochemistry 47:4410-4417(2008). 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 (PubMed:18361507). This phospholipase activity is very sensitive to CC calcium. May be important for formation and maintenance of the neuronal CC network in the postnatal brain (By similarity). CC {ECO:0000250|UniProtKB:A2AP18, ECO:0000269|PubMed:18361507}. 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:18361507}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180; CC Evidence={ECO:0000305|PubMed:18361507}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00041}; CC -!- ACTIVITY REGULATION: Activity is stimulated by GNB1:GNG2. CC {ECO:0000269|PubMed:18361507}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=14.4 uM for CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) CC {ECO:0000269|PubMed:18361507}; CC Vmax=12.6 umol/min/mg enzyme {ECO:0000269|PubMed:18361507}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2AP18}. Cell CC membrane {ECO:0000250|UniProtKB:A2AP18}. Note=Localized predominantly CC at the plasma membrane. {ECO:0000250|UniProtKB:A2AP18}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=O75038-1; Sequence=Displayed; CC Name=2; CC IsoId=O75038-2; Sequence=VSP_029068, VSP_029072, VSP_029073; CC Name=3; CC IsoId=O75038-3; Sequence=VSP_029070; CC Name=4; CC IsoId=O75038-4; Sequence=VSP_029071, VSP_029074; CC Name=5; CC IsoId=O75038-5; Sequence=VSP_029067, VSP_029069, VSP_029071, CC VSP_029074; CC -!- TISSUE SPECIFICITY: Expressed in retina and kidney. CC {ECO:0000269|PubMed:16107206}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH43358.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA32295.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC56932.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; DQ176850; ABA12209.1; -; mRNA. DR EMBL; AK074149; BAB84975.1; -; mRNA. DR EMBL; AK122591; BAC56932.2; ALT_INIT; mRNA. DR EMBL; AB007919; BAA32295.3; ALT_INIT; mRNA. DR EMBL; AL139246; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC019679; AAH19679.1; -; mRNA. DR EMBL; BC043358; AAH43358.1; ALT_FRAME; mRNA. DR EMBL; BC050037; AAH50037.1; -; mRNA. DR EMBL; BC128207; AAI28208.1; -; mRNA. DR CCDS; CCDS59959.1; -. [O75038-1] DR RefSeq; NP_001289941.1; NM_001303012.1. [O75038-2] DR RefSeq; NP_001289942.1; NM_001303013.1. DR RefSeq; NP_055453.2; NM_014638.3. [O75038-1] DR AlphaFoldDB; O75038; -. DR SMR; O75038; -. DR BioGRID; 115009; 7. DR IntAct; O75038; 3. DR MINT; O75038; -. DR STRING; 9606.ENSP00000367747; -. DR SwissLipids; SLP:000001755; -. DR GlyGen; O75038; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O75038; -. DR PhosphoSitePlus; O75038; -. DR BioMuta; PLCH2; -. DR EPD; O75038; -. DR jPOST; O75038; -. DR MassIVE; O75038; -. DR PaxDb; 9606-ENSP00000367747; -. DR PeptideAtlas; O75038; -. DR ProteomicsDB; 49717; -. [O75038-1] DR ProteomicsDB; 49718; -. [O75038-2] DR ProteomicsDB; 49719; -. [O75038-3] DR ProteomicsDB; 49720; -. [O75038-4] DR ProteomicsDB; 49721; -. [O75038-5] DR TopDownProteomics; O75038-1; -. [O75038-1] DR Antibodypedia; 1163; 26 antibodies from 14 providers. DR DNASU; 9651; -. DR Ensembl; ENST00000378486.8; ENSP00000367747.3; ENSG00000149527.18. [O75038-1] DR Ensembl; ENST00000419816.6; ENSP00000389803.2; ENSG00000149527.18. [O75038-1] DR Ensembl; ENST00000449969.5; ENSP00000397289.1; ENSG00000149527.18. [O75038-2] DR Ensembl; ENST00000620687.1; ENSP00000481938.1; ENSG00000276429.3. [O75038-1] DR Ensembl; ENST00000626246.2; ENSP00000486186.1; ENSG00000276429.3. [O75038-1] DR Ensembl; ENST00000627854.2; ENSP00000487140.1; ENSG00000276429.3. [O75038-2] DR GeneID; 9651; -. DR KEGG; hsa:9651; -. DR MANE-Select; ENST00000378486.8; ENSP00000367747.3; NM_014638.4; NP_055453.2. DR UCSC; uc001ajj.2; human. [O75038-1] DR AGR; HGNC:29037; -. DR CTD; 9651; -. DR DisGeNET; 9651; -. DR GeneCards; PLCH2; -. DR HGNC; HGNC:29037; PLCH2. DR HPA; ENSG00000149527; Tissue enhanced (brain, retina, skin). DR MIM; 612836; gene. DR neXtProt; NX_O75038; -. DR OpenTargets; ENSG00000149527; -. DR PharmGKB; PA134914471; -. DR VEuPathDB; HostDB:ENSG00000149527; -. DR eggNOG; KOG0169; Eukaryota. DR GeneTree; ENSGT00940000158374; -. DR HOGENOM; CLU_002738_0_0_1; -. DR InParanoid; O75038; -. DR OMA; NCITCVI; -. DR OrthoDB; 2900494at2759; -. DR PhylomeDB; O75038; -. DR TreeFam; TF313216; -. DR PathwayCommons; O75038; -. DR Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol. DR SignaLink; O75038; -. DR BioGRID-ORCS; 9651; 14 hits in 1126 CRISPR screens. DR ChiTaRS; PLCH2; human. DR GenomeRNAi; 9651; -. DR Pharos; O75038; Tbio. DR PRO; PR:O75038; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; O75038; Protein. DR Bgee; ENSG00000149527; Expressed in right hemisphere of cerebellum and 98 other cell types or tissues. DR ExpressionAtlas; O75038; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:UniProtKB. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:Ensembl. 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:UniProtKB. DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central. DR CDD; cd00275; C2_PLC_like; 1. DR CDD; cd16221; EFh_PI-PLCeta2; 1. DR CDD; cd13364; PH_PLC_eta; 1. DR CDD; cd08633; PI-PLCc_eta2; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 1.10.238.10; EF-hand; 2. DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 2. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. 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_cat. DR InterPro; IPR046971; PLC-eta2_EFh. 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:SF166; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE ETA-2; 1. DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 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; 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; 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. DR Genevisible; O75038; HS. 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..1416 FT /note="1-phosphatidylinositol 4,5-bisphosphate FT phosphodiesterase eta-2" FT /id="PRO_0000088507" FT DOMAIN 47..155 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 169..204 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 205..241 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 326..471 FT /note="PI-PLC X-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270" FT DOMAIN 626..740 FT /note="PI-PLC Y-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271" FT DOMAIN 740..869 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT REGION 1..155 FT /note="Necessary for plasma membrane localization" FT /evidence="ECO:0000250" FT REGION 535..620 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 905..1109 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1121..1222 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1315..1405 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 535..549 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 551..568 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1010..1025 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1139..1158 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 341 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270" FT ACT_SITE 385 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270" FT BINDING 182 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 184 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 186 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 188 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 193 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 342 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 371 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 373 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 420 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 469 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 471 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 653 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 680 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 784 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 786 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 810 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 839 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250" FT BINDING 840 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250" FT BINDING 841 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000250" FT MOD_RES 487 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AP18" FT MOD_RES 491 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AP18" FT MOD_RES 595 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AP18" FT MOD_RES 605 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AP18" FT VAR_SEQ 1..45 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_029067" FT VAR_SEQ 1..41 FT /note="MSGPWPSPDSRTKGTVAWLAEVLLWVGGSVVLSSEWQLGPL -> MEEPGPP FT GGLSQDQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9455484" FT /id="VSP_029068" FT VAR_SEQ 117..785 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_029069" FT VAR_SEQ 706..741 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_029070" FT VAR_SEQ 987..1211 FT /note="DTRPLSTQRPLPPLCSLETIAEEPAPGPGPPPPAAVPTSSSQGRPPYPTGPG FT ANVASPLEDTEEPRDSRPRPCNGEGAGGAYERAPGSQTDGRSQPRTLGHLPVIRRVKSE FT GQVPTEPLGGWRPLAAPFPAPAVYSDATGSDPLWQRLEPCGHRDSVSSSSSMSSSDTVI FT DLSLPSLGLGRSRENLAGAHMGRLPPRPHSASAARPDLPPVTKSKSNPNLRATGQ -> FT GKAPAAVAEKSPVRVRPPRVLDGPGPAGMAATCMKCVVGSCAGVNTGGLQRERPPSPGP FT ASRQAAIRQQPRARADSLGAPCCGLDPHAIPGRSREAPKGPGAWRQGPGGSGSMSSDSS FT SPDSPGIPERSPRWPEGACRQPGALQGEMSALFAQKLEEIRSKSPMFSAGKPLLPCVVL FT PHAPGMAGPGSPAAASAWTVSPRVLVLVALYPWHCLRGTLLPWLACGP (in FT isoform 4 and isoform 5)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_029071" FT VAR_SEQ 987..1156 FT /note="DTRPLSTQRPLPPLCSLETIAEEPAPGPGPPPPAAVPTSSSQGRPPYPTGPG FT ANVASPLEDTEEPRDSRPRPCNGEGAGGAYERAPGSQTDGRSQPRTLGHLPVIRRVKSE FT GQVPTEPLGGWRPLAAPFPAPAVYSDATGSDPLWQRLEPCGHRDSVSSSSSMSSSDTVI FT -> GKAPAAVAEKSPVRVRPPRVLDGPGPAGMAATCMKCVVGSCAGVNTGGLQRERPPS FT PGPASRQAAIRQQPRARADSLGAPCCGLDPHAIPGRSREAPKGPGAWRQGPGGSGSMSS FT DSSSPDSPGIPERSPRWPEGACRQPGALQGEMSALFAQKLEEIRSKSPMFSAVRN (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:9455484" FT /id="VSP_029072" FT VAR_SEQ 1157..1416 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9455484" FT /id="VSP_029073" FT VAR_SEQ 1212..1416 FT /note="Missing (in isoform 4 and isoform 5)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_029074" FT CONFLICT 559 FT /note="D -> E (in Ref. 2; BAB84975)" FT /evidence="ECO:0000305" FT CONFLICT 560 FT /note="V -> M (in Ref. 2; BAB84975)" FT /evidence="ECO:0000305" FT CONFLICT O75038-4:1004 FT /note="P -> L (in Ref. 2; BAB84975)" FT /evidence="ECO:0000305" FT CONFLICT O75038-5:209 FT /note="Q -> L (in Ref. 2; BAC56932)" FT /evidence="ECO:0000305" SQ SEQUENCE 1416 AA; 154668 MW; 05088ACD9C45AE87 CRC64; MSGPWPSPDS RTKGTVAWLA EVLLWVGGSV VLSSEWQLGP LVERCMGAMQ EGMQMVKLRG GSKGLVRFYY LDEHRSCIRW RPSRKNEKAK ISIDSIQEVS EGRQSEVFQR YPDGSFDPNC CFSIYHGSHR ESLDLVSTSS EVARTWVTGL RYLMAGISDE DSLARRQRTR DQWLKQTFDE ADKNGDGSLS IGEVLQLLHK LNVNLPRQRV KQMFREADTD DHQGTLGFEE FCAFYKMMST RRDLYLLMLT YSNHKDHLDA ASLQRFLQVE QKMAGVTLES CQDIIEQFEP CPENKSKGLL GIDGFTNYTR SPAGDIFNPE HHHVHQDMTQ PLSHYFITSS HNTYLVGDQL MSQSRVDMYA WVLQAGCRCV EVDCWDGPDG EPIVHHGYTL TSKILFKDVI ETINKYAFIK NEYPVILSIE NHCSVIQQKK MAQYLTDILG DKLDLSSVSS EDATTLPSPQ MLKGKILVKG KKLPANISED AEEGEVSDED SADEIDDDCK LLNGDASTNR KRVENTAKRK LDSLIKESKI RDCEDPNNFS VSTLSPSGKL GRKSKAEEDV ESGEDAGASR RNGRLVVGSF SRRKKKGSKL KKAASVEEGD EGQDSPGGQS RGATRQKKTM KLSRALSDLV KYTKSVATHD IEMEAASSWQ VSSFSETKAH QILQQKPAQY LRFNQQQLSR IYPSSYRVDS SNYNPQPFWN AGCQMVALNY QSEGRMLQLN RAKFSANGGC GYVLKPGCMC QGVFNPNSED PLPGQLKKQL VLRIISGQQL PKPRDSMLGD RGEIIDPFVE VEIIGLPVDC SREQTRVVDD NGFNPTWEET LVFMVHMPEI ALVRFLVWDH DPIGRDFIGQ RTLAFSSMMP GYRHVYLEGM EEASIFVHVA VSDISGKVKQ ALGLKGLFLR GPKPGSLDSH AAGRPPARPS VSQRILRRTA SAPTKSQKPG RRGFPELVLG TRDTGSKGVA DDVVPPGPGP APEAPAQEGP GSGSPRDTRP LSTQRPLPPL CSLETIAEEP APGPGPPPPA AVPTSSSQGR PPYPTGPGAN VASPLEDTEE PRDSRPRPCN GEGAGGAYER APGSQTDGRS QPRTLGHLPV IRRVKSEGQV PTEPLGGWRP LAAPFPAPAV YSDATGSDPL WQRLEPCGHR DSVSSSSSMS SSDTVIDLSL PSLGLGRSRE NLAGAHMGRL PPRPHSASAA RPDLPPVTKS KSNPNLRATG QRPPIPDELQ PRSLAPRMAG LPFRPPWGCL SLVGVQDCPV AAKSKSLGDL TADDFAPSFE GGSRRLSHSL GLPGGTRRVS GPGVRRDTLT EQLRWLTVFQ QAGDITSPTS LGPAGEGVAG GPGFVRRSSS RSHSRVRAIA SRARQAQERQ QRLQGLGRQG PPEEERGTPE GACSVGHEGS VDAPAPSKGA LGPASAAAEN LVLLRL //