ID   PLCD4_RAT               Reviewed;         772 AA.
AC   Q62711; Q63693;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 159.
DE   RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4 {ECO:0000305};
DE            EC=3.1.4.11 {ECO:0000269|PubMed:8550586};
DE   AltName: Full=Phosphoinositide phospholipase C-delta-4;
DE   AltName: Full=Phospholipase C-delta-4;
DE            Short=PLC-delta-4;
GN   Name=Plcd4 {ECO:0000312|RGD:621025};
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] (ISOFORMS 1; 2 AND 3), FUNCTION, ENZYME
RP   ACTIVITY, COFACTOR, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=8550568; DOI=10.1074/jbc.271.1.25;
RA   Lee S.B., Rhee S.-G.;
RT   "Molecular cloning, splice variants, expression, and purification of
RT   phospholipase C-delta 4.";
RL   J. Biol. Chem. 271:25-31(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND CATALYTIC
RP   ACTIVITY.
RC   STRAIN=Donryu;
RX   PubMed=8550586; DOI=10.1074/jbc.271.1.355;
RA   Liu N., Fukami K., Yu H., Takenawa T.;
RT   "A new phospholipase C delta 4 is induced at S-phase of the cell cycle and
RT   appears in the nucleus.";
RL   J. Biol. Chem. 271:355-360(1996).
RN   [3]
RP   ALTERNATIVE SPLICING (ISOFORM 4), FUNCTION (ISOFORM 4), AND MUTAGENESIS OF
RP   ARG-36.
RX   PubMed=9915823; DOI=10.1074/jbc.274.5.2872;
RA   Nagano K., Fukami K., Minagawa T., Watanabe Y., Ozaki C., Takenawa T.;
RT   "A novel phospholipase C delta4 (PLCdelta4) splice variant as a negative
RT   regulator of PLC.";
RL   J. Biol. Chem. 274:2872-2879(1999).
RN   [4]
RP   DOMAIN C2, AND MUTAGENESIS OF LYS-714; SER-717 AND ARG-718.
RX   PubMed=11706040; DOI=10.1074/jbc.m109705200;
RA   Ananthanarayanan B., Das S., Rhee S.-G., Murray D., Cho W.;
RT   "Membrane targeting of C2 domains of phospholipase C-delta isoforms.";
RL   J. Biol. Chem. 277:3568-3575(2002).
RN   [5]
RP   DOMAIN PH, AND SUBCELLULAR LOCATION.
RX   PubMed=15037625; DOI=10.1074/jbc.m312772200;
RA   Lee S.B., Varnai P., Balla A., Jalink K., Rhee S.G., Balla T.;
RT   "The pleckstrin homology domain of phosphoinositide-specific phospholipase
RT   Cdelta4 is not a critical determinant of the membrane localization of the
RT   enzyme.";
RL   J. Biol. Chem. 279:24362-24371(2004).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17063484; DOI=10.1002/jcb.21048;
RA   Lo Vasco V.R., Fabrizi C., Artico M., Cocco L., Billi A.M., Fumagalli L.,
RA   Manzoli F.A.;
RT   "Expression of phosphoinositide-specific phospholipase C isoenzymes in
RT   cultured astrocytes.";
RL   J. Cell. Biochem. 100:952-959(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445 AND SER-458, AND
RP   IDENTIFICATION BY MASS 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: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2)
CC       to generate 2 second messenger molecules diacylglycerol (DAG) and
CC       inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of
CC       protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular
CC       stores. Required for acrosome reaction in sperm during fertilization,
CC       probably by acting as an important enzyme for intracellular Ca(2+)
CC       mobilization in the zona pellucida-induced acrosome reaction. May play
CC       a role in cell growth. Modulates the liver regeneration in cooperation
CC       with nuclear PKC. Overexpression up-regulates the Erk signaling pathway
CC       and proliferation. {ECO:0000269|PubMed:8550568}.
CC   -!- FUNCTION: [Isoform 4]: Has no enzyme activity and acts as a negative
CC       regulator of phospholipase C, with a preference for thePLC-delta
CC       family. {ECO:0000269|PubMed:9915823}.
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:8550586};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC         Evidence={ECO:0000305|PubMed:8550586};
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:Q9BRC7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC         Evidence={ECO:0000250|UniProtKB:Q9BRC7};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000305|PubMed:8550568};
CC       Note=Binds 3 Ca(2+) ions per subunit. Two of the Ca(2+) ions are bound
CC       to the C2 domain. {ECO:0000305|PubMed:8550568};
CC   -!- SUBUNIT: Interacts with GRIP1 (By similarity). Interacts (via GBA
CC       motif) with guanine nucleotide-binding protein G(i) alpha subunit GNAI3
CC       (inactive GDP-bound form); low-affinity interaction (By similarity).
CC       {ECO:0000250|UniProtKB:Q8K3R3, ECO:0000250|UniProtKB:Q9BRC7}.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein.
CC       Nucleus. Cytoplasm. Endoplasmic reticulum. Note=Localizes primarily to
CC       intracellular membranes mostly to the endoplasmic reticulum.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q62711-1; Sequence=Displayed;
CC       Name=2; Synonyms=ALT I;
CC         IsoId=Q62711-2; Sequence=VSP_028508;
CC       Name=3; Synonyms=ALT II;
CC         IsoId=Q62711-3; Sequence=VSP_028509;
CC       Name=4; Synonyms=ALT III;
CC         IsoId=Q62711-4; Sequence=VSP_028507;
CC   -!- TISSUE SPECIFICITY: Present at high level in testis. Also present in
CC       brain > skeletal muscle > thyroid gland > stomach > thymus > aorta >
CC       heart (at protein level). Highly expressed in regenerating liver.
CC       Isoform 4 is weakly expressed compared to other isoforms but is
CC       expressed at high level in some neural cells.
CC       {ECO:0000269|PubMed:8550568, ECO:0000269|PubMed:8550586}.
CC   -!- DEVELOPMENTAL STAGE: Increases at the transition from G1- to S-phase,
CC       and the continues to the end of M-phase. Almost disappears when cells
CC       reenter the next G1-phase. {ECO:0000269|PubMed:8550586}.
CC   -!- INDUCTION: By serum treatment. {ECO:0000269|PubMed:8550586}.
CC   -!- DOMAIN: The PDZ-binding motif mediates the interaction with GRIP1.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The C2 domain mediates pre-localization to the membrane prior
CC       to Ca(2+) import and non-selective Ca(2+)-mediated targeting to various
CC       cellular membranes.
CC   -!- DOMAIN: The PH domain is not a critical determinant of the membrane
CC       localization. The PH domain of isoform 4 is necessary and sufficient to
CC       inhibit enzyme activity of other PLC-delta enzymes.
CC   -!- DOMAIN: The GBA (G-alpha binding and activating) motif mediates binding
CC       to the alpha subunits of guanine nucleotide-binding proteins (G
CC       proteins). {ECO:0000250|UniProtKB:Q9BRC7}.
CC   -!- MISCELLANEOUS: [Isoform 4]: Inactive. {ECO:0000305}.
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DR   EMBL; U16655; AAC52346.1; -; mRNA.
DR   EMBL; D50455; BAA09046.1; -; mRNA.
DR   RefSeq; NP_542419.1; NM_080688.1. [Q62711-1]
DR   AlphaFoldDB; Q62711; -.
DR   SMR; Q62711; -.
DR   STRING; 10116.ENSRNOP00000022234; -.
DR   BindingDB; Q62711; -.
DR   SwissLipids; SLP:000001069; -.
DR   iPTMnet; Q62711; -.
DR   PhosphoSitePlus; Q62711; -.
DR   PaxDb; 10116-ENSRNOP00000022234; -.
DR   GeneID; 140693; -.
DR   KEGG; rno:140693; -.
DR   UCSC; RGD:621025; rat. [Q62711-1]
DR   AGR; RGD:621025; -.
DR   CTD; 84812; -.
DR   RGD; 621025; Plcd4.
DR   VEuPathDB; HostDB:ENSRNOG00000016361; -.
DR   eggNOG; KOG0169; Eukaryota.
DR   HOGENOM; CLU_002738_0_2_1; -.
DR   InParanoid; Q62711; -.
DR   OrthoDB; 2900494at2759; -.
DR   PhylomeDB; Q62711; -.
DR   BRENDA; 3.1.4.11; 5301.
DR   Reactome; R-RNO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR   PRO; PR:Q62711; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000016361; Expressed in skeletal muscle tissue and 19 other cell types or tissues.
DR   ExpressionAtlas; Q62711; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:RGD.
DR   GO; GO:0007340; P:acrosome reaction; ISO:RGD.
DR   GO; GO:0035556; P:intracellular signal transduction; TAS:RGD.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00275; C2_PLC_like; 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; 1.
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; 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:SF31; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA-4; 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; PF00169; PH; 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; 3.
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; 3.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR   Genevisible; Q62711; RN.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cytoplasm; Endoplasmic reticulum; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Membrane; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transducer.
FT   CHAIN           1..772
FT                   /note="1-phosphatidylinositol 4,5-bisphosphate
FT                   phosphodiesterase delta-4"
FT                   /id="PRO_0000306829"
FT   DOMAIN          16..124
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          134..169
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          170..205
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          203..237
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          290..435
FT                   /note="PI-PLC X-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   DOMAIN          503..619
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT   DOMAIN          619..746
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          26..53
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          445..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           213..243
FT                   /note="GBA"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRC7"
FT   MOTIF           741..744
FT                   /note="PDZ-binding"
FT   COMPBIAS        468..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   ACT_SITE        350
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   BINDING         147
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         149
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         151
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         153
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         158
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         183
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         185
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         187
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         189
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         194
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         306
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         335
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         337
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         433
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         435
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         532
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         559
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         662
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         686
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         715
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250"
FT   BINDING         716
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         445
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         458
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   VAR_SEQ         424..487
FT                   /note="EQLRGKILVKGKKLRTIEVVESDKEEEELEKDEGSDLDPASAELDMQSQPES
FT                   QEQASGNKSKNK -> VMKCPMSCLLICVHVLAQAPNSIPESILLPKR (in
FT                   isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_028507"
FT   VAR_SEQ         487
FT                   /note="K -> KVMKCPMSCLLICVHVLAQAPNSIPESILLP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8550568"
FT                   /id="VSP_028508"
FT   VAR_SEQ         487
FT                   /note="K -> KAPNSIPESILLP (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:8550568"
FT                   /id="VSP_028509"
FT   MUTAGEN         36
FT                   /note="R->G: Only retains weak enzyme activity and
FT                   abolishes the ability of isoform 4 to act as a negative
FT                   regulator."
FT                   /evidence="ECO:0000269|PubMed:9915823"
FT   MUTAGEN         714
FT                   /note="K->E: Abolishes affinity for POPC/POPS in the
FT                   absence of Ca(2+); when associated with E-718."
FT                   /evidence="ECO:0000269|PubMed:11706040"
FT   MUTAGEN         717
FT                   /note="S->D: Induces a larger Ca(2+)-dependence."
FT                   /evidence="ECO:0000269|PubMed:11706040"
FT   MUTAGEN         718
FT                   /note="R->E: Abolishes affinity for POPC/POPS in the
FT                   absence of Ca(2+); when associated with E-714."
FT                   /evidence="ECO:0000269|PubMed:11706040"
FT   CONFLICT        395
FT                   /note="M -> ML (in Ref. 2; BAA09046)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416
FT                   /note="Missing (in Ref. 2; BAA09046)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        425
FT                   /note="Missing (in Ref. 2; BAA09046)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        757
FT                   /note="I -> H (in Ref. 2; BAA09046)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   772 AA;  88967 MW;  5DD56D1D4AA21356 CRC64;
     MASQIQKLLT TNQDLLLMQK GTMMRKVRTK SWKKLRYFRL QDDGMTVWHG RHLESISKPT
     FSISDVERIR KGQDSELLRY LVEEFPLEQG FTIVFNGRRP NLDLVANSVE EAQTWMRGLQ
     LLVDLVARMN YQEQLDQMLR EWFQQADRNQ DSRMSFREAQ RLLLLMNVEM DEEYAFSLFQ
     EADVSQSNTL DSEEFVQFYK ALTKRTEIEE LFENFSSDKQ KLTLLEFVDF LREEQKESDH
     SSDLALKLID RYEPSENGRL LRVLSKDGFL SYLCSADGNI FNPDCLPIYQ DMTQPLSHYY
     INSSHNTYLL GDQFCGQSSV EGYIRALKRG CRCVEVDTWD GPDGEPVVYH GRTLTSRILF
     KDVLATLAQY AFQSSDYPLI LSLDNHCTWE QQKTMAHHLI AILGEQLLST TLEEQLIDIM
     PSPEQLRGKI LVKGKKLRTI EVVESDKEEE ELEKDEGSDL DPASAELDMQ SQPESQEQAS
     GNKSKNKKKF LLQSSTTILC PDLSALVVYL RTAPFCSFTH SKENYHIYDI SSFSESKAKN
     LIREAGNEFV QHNARQLCRV YPSGLRTDSS NYNPQEHWNV GCQMVAMNMQ TAGSAMDICD
     GLFRQNGGSG YVLKPEFLRD TQSSFNPMKP VSLYKAQILV VQVISGQRLP KVDKTKETTV
     VDPLVRVELY GVPEDTKQQE TSYVENNGIN PYWGETFYFQ IQVPELAMLR FVVKDYSRTS
     RNNFIGQYTL PWTCMKHGYR HVSLLSKDGT SLHPASIFVY TCMQEDLDMD EP
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