PLCH2_HUMAN
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 03-AUG-2022, entry version 177.
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;
CC Evidence={ECO:0000255|PROSITE-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 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) {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};
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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; 6.
DR IntAct; O75038; 4.
DR MINT; O75038; -.
DR STRING; 9606.ENSP00000367747; -.
DR SwissLipids; SLP:000001755; -.
DR iPTMnet; O75038; -.
DR PhosphoSitePlus; O75038; -.
DR BioMuta; PLCH2; -.
DR EPD; O75038; -.
DR jPOST; O75038; -.
DR MassIVE; O75038; -.
DR PaxDb; O75038; -.
DR PeptideAtlas; O75038; -.
DR PRIDE; 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; 25 antibodies from 13 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 CTD; 9651; -.
DR DisGeNET; 9651; -.
DR GeneCards; PLCH2; -.
DR HGNC; HGNC:29037; PLCH2.
DR HPA; ENSG00000149527; Tissue enhanced (retina, skin).
DR MalaCards; PLCH2; -.
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; CSIVQQK; -.
DR OrthoDB; 368239at2759; -.
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; 12 hits in 1047 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 96 other tissues.
DR ExpressionAtlas; O75038; baseline and differential.
DR Genevisible; O75038; HS.
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; IDA: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..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
