PLCB4_HUMAN
ID PLCB4_HUMAN Reviewed; 1175 AA.
AC Q15147; B7ZLK6; E2QRH8; Q17R56; Q5JYS8; Q5JYS9; Q5JYT0; Q5JYT3; Q5JYT4;
AC Q9BQW5; Q9BQW6; Q9BQW8; Q9UJQ2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 3.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000250|UniProtKB:Q07722};
DE AltName: Full=Phosphoinositide phospholipase C-beta-4;
DE AltName: Full=Phospholipase C-beta-4;
DE Short=PLC-beta-4;
GN Name=PLCB4 {ECO:0000312|HGNC:HGNC:9059};
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).
RC TISSUE=Retina;
RX PubMed=8530101; DOI=10.1006/geno.1995.1214;
RA Alvarez R.A., Ghalayini A.J., Xu P., Hardcastle A., Bhattacharya S.,
RA Rao P.N., Pettenati M.J., Anderson R.E., Baehr W.;
RT "cDNA sequence and gene locus of the human retinal phosphoinositide-
RT specific phospholipase-C beta 4 (PLCB4).";
RL Genomics 29:53-61(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-21.
RC TISSUE=Brain;
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 [4]
RP PROTEIN SEQUENCE OF 2-11; 79-88; 154-163; 181-195; 220-227; 255-266;
RP 366-377; 435-455; 516-528; 577-586; 606-717; 762-780; 786-797; 822-847;
RP 854-871; 883-908; 910-918; 1023-1039 AND 1139-1149, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-886, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [6]
RP VARIANTS ARCND2 THR-329; HIS-621; CYS-621; CYS-623 AND HIS-650.
RX PubMed=22560091; DOI=10.1016/j.ajhg.2012.04.002;
RA Rieder M.J., Green G.E., Park S.S., Stamper B.D., Gordon C.T.,
RA Johnson J.M., Cunniff C.M., Smith J.D., Emery S.B., Lyonnet S., Amiel J.,
RA Holder M., Heggie A.A., Bamshad M.J., Nickerson D.A., Cox T.C., Hing A.V.,
RA Horst J.A., Cunningham M.L.;
RT "A human homeotic transformation resulting from mutations in PLCB4 and
RT GNAI3 causes auriculocondylar syndrome.";
RL Am. J. Hum. Genet. 90:907-914(2012).
RN [7]
RP ERRATUM OF PUBMED:22560091.
RA Rieder M.J., Green G.E., Park S.S., Stamper B.D., Gordon C.T.,
RA Johnson J.M., Cunniff C.M., Smith J.D., Emery S.B., Lyonnet S., Amiel J.,
RA Holder M., Heggie A.A., Bamshad M.J., Nickerson D.A., Cox T.C., Hing A.V.,
RA Horst J.A., Cunningham M.L.;
RL Am. J. Hum. Genet. 90:1116-1116(2012).
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 form has a role in retina signal transduction.
CC {ECO:0000250|UniProtKB:Q07722}.
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:Q07722};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000250|UniProtKB:Q07722};
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:Q07722};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000250|UniProtKB:Q07722};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC -!- INTERACTION:
CC Q15147; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-998637, EBI-16439278;
CC Q15147; Q04864: REL; NbExp=3; IntAct=EBI-998637, EBI-307352;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=2;
CC IsoId=Q15147-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q15147-2; Sequence=VSP_004721, VSP_004722;
CC Name=3;
CC IsoId=Q15147-4; Sequence=VSP_037818;
CC Name=4;
CC IsoId=Q15147-5; Sequence=VSP_055182;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in the retina.
CC -!- DISEASE: Auriculocondylar syndrome 2 (ARCND2) [MIM:614669]: A
CC craniofacial malformation syndrome characterized by variable mandibular
CC anomalies, including mild to severe micrognathia, temporomandibular
CC joint ankylosis, cleft palate, and a characteristic ear malformation
CC that consists of separation of the lobule from the external ear, giving
CC the appearance of a question mark (question-mark ear). Other frequently
CC described features include prominent cheeks, cupped and posteriorly
CC rotated ears, preauricular tags, and microstomia.
CC {ECO:0000269|PubMed:22560091}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; L41349; AAB02027.1; -; mRNA.
DR EMBL; AL121898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL023805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117458; AAI17459.1; -; mRNA.
DR EMBL; BC143868; AAI43869.1; -; mRNA.
DR CCDS; CCDS13104.1; -. [Q15147-4]
DR CCDS; CCDS13105.1; -. [Q15147-1]
DR CCDS; CCDS54447.1; -. [Q15147-5]
DR RefSeq; NP_000924.3; NM_000933.3. [Q15147-4]
DR RefSeq; NP_001166117.1; NM_001172646.1. [Q15147-5]
DR RefSeq; NP_877949.2; NM_182797.2. [Q15147-1]
DR RefSeq; XP_016883369.1; XM_017027880.1. [Q15147-4]
DR RefSeq; XP_016883370.1; XM_017027881.1.
DR AlphaFoldDB; Q15147; -.
DR SMR; Q15147; -.
DR BioGRID; 111348; 22.
DR DIP; DIP-36735N; -.
DR IntAct; Q15147; 5.
DR STRING; 9606.ENSP00000367762; -.
DR iPTMnet; Q15147; -.
DR PhosphoSitePlus; Q15147; -.
DR SwissPalm; Q15147; -.
DR BioMuta; PLCB4; -.
DR EPD; Q15147; -.
DR jPOST; Q15147; -.
DR MassIVE; Q15147; -.
DR MaxQB; Q15147; -.
DR PaxDb; Q15147; -.
DR PeptideAtlas; Q15147; -.
DR PRIDE; Q15147; -.
DR ProteomicsDB; 15257; -.
DR ProteomicsDB; 60459; -. [Q15147-1]
DR ProteomicsDB; 60460; -. [Q15147-2]
DR ProteomicsDB; 60461; -. [Q15147-4]
DR ProteomicsDB; 63514; -.
DR Antibodypedia; 24070; 39 antibodies from 17 providers.
DR DNASU; 5332; -.
DR Ensembl; ENST00000378493.6; ENSP00000367754.1; ENSG00000101333.19. [Q15147-1]
DR Ensembl; ENST00000378501.3; ENSP00000367762.2; ENSG00000101333.19. [Q15147-4]
DR Ensembl; ENST00000685110.1; ENSP00000510632.1; ENSG00000101333.19. [Q15147-1]
DR Ensembl; ENST00000685310.1; ENSP00000510124.1; ENSG00000101333.19. [Q15147-1]
DR Ensembl; ENST00000685823.1; ENSP00000508676.1; ENSG00000101333.19. [Q15147-5]
DR Ensembl; ENST00000685859.1; ENSP00000510302.1; ENSG00000101333.19. [Q15147-1]
DR Ensembl; ENST00000686313.1; ENSP00000508595.1; ENSG00000101333.19. [Q15147-4]
DR Ensembl; ENST00000686871.1; ENSP00000510118.1; ENSG00000101333.19. [Q15147-4]
DR Ensembl; ENST00000686976.1; ENSP00000508600.1; ENSG00000101333.19. [Q15147-4]
DR Ensembl; ENST00000688656.1; ENSP00000509912.1; ENSG00000101333.19. [Q15147-1]
DR Ensembl; ENST00000689910.1; ENSP00000508650.1; ENSG00000101333.19. [Q15147-1]
DR Ensembl; ENST00000693005.1; ENSP00000509597.1; ENSG00000101333.19. [Q15147-1]
DR Ensembl; ENST00000693752.1; ENSP00000508677.1; ENSG00000101333.19. [Q15147-4]
DR GeneID; 5332; -.
DR KEGG; hsa:5332; -.
DR UCSC; uc010gbx.4; human. [Q15147-1]
DR CTD; 5332; -.
DR DisGeNET; 5332; -.
DR GeneCards; PLCB4; -.
DR HGNC; HGNC:9059; PLCB4.
DR HPA; ENSG00000101333; Tissue enhanced (brain, salivary gland).
DR MalaCards; PLCB4; -.
DR MIM; 600810; gene.
DR MIM; 614669; phenotype.
DR neXtProt; NX_Q15147; -.
DR OpenTargets; ENSG00000101333; -.
DR Orphanet; 137888; Auriculocondylar syndrome.
DR PharmGKB; PA33387; -.
DR VEuPathDB; HostDB:ENSG00000101333; -.
DR eggNOG; KOG1265; Eukaryota.
DR GeneTree; ENSGT00940000156426; -.
DR HOGENOM; CLU_002738_2_1_1; -.
DR InParanoid; Q15147; -.
DR OMA; FKICPRN; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q15147; -.
DR TreeFam; TF352235; -.
DR BRENDA; 3.1.4.11; 2681.
DR PathwayCommons; Q15147; -.
DR Reactome; R-HSA-112043; PLC beta mediated events.
DR Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; Q15147; -.
DR BioGRID-ORCS; 5332; 6 hits in 1070 CRISPR screens.
DR ChiTaRS; PLCB4; human.
DR GeneWiki; PLCB4; -.
DR GenomeRNAi; 5332; -.
DR Pharos; Q15147; Tbio.
DR PRO; PR:Q15147; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q15147; protein.
DR Bgee; ENSG00000101333; Expressed in parotid gland and 194 other tissues.
DR ExpressionAtlas; Q15147; baseline and differential.
DR Genevisible; Q15147; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0004629; F:phospholipase C activity; TAS:Reactome.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR CDD; cd13361; PH_PLC_beta; 1.
DR Gene3D; 1.20.1230.10; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 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; IPR042531; PLC-beta_C_sf.
DR InterPro; IPR009535; PLC-beta_CS.
DR InterPro; IPR037862; PLC-beta_PH.
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 Pfam; PF00168; C2; 1.
DR Pfam; PF06631; DUF1154; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF17787; PH_14; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 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; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 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; Alternative splicing; Calcium; Direct protein sequencing;
KW Disease variant; Hydrolase; Lipid degradation; Lipid metabolism;
KW Phosphoprotein; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..1175
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase beta-4"
FT /id="PRO_0000088495"
FT DOMAIN 313..463
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 565..681
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 684..809
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 482..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..507
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 886
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..153
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:8530101"
FT /id="VSP_004721"
FT VAR_SEQ 154..167
FT /note="LAFMTNTNGKIPVR -> MNNNWNVCFFLFCP (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:8530101"
FT /id="VSP_004722"
FT VAR_SEQ 535
FT /note="V -> VKKASDDLEHENN (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_055182"
FT VAR_SEQ 1154..1175
FT /note="AKEMQQMVKLEAEMDRRPATVV -> LLKSCHAVSQTQGEGDAADGEIGSRD
FT GPQTSNSSMKLQNAN (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_037818"
FT VARIANT 21
FT /note="A -> T (in dbSNP:rs6077510)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_056694"
FT VARIANT 329
FT /note="N -> T (in ARCND2; dbSNP:rs387907179)"
FT /evidence="ECO:0000269|PubMed:22560091"
FT /id="VAR_068559"
FT VARIANT 621
FT /note="R -> C (in ARCND2; dbSNP:rs397514482)"
FT /evidence="ECO:0000269|PubMed:22560091"
FT /id="VAR_068560"
FT VARIANT 621
FT /note="R -> H (in ARCND2; dbSNP:rs397514481)"
FT /evidence="ECO:0000269|PubMed:22560091"
FT /id="VAR_068561"
FT VARIANT 623
FT /note="Y -> C (in ARCND2; dbSNP:rs397514480)"
FT /evidence="ECO:0000269|PubMed:22560091"
FT /id="VAR_068562"
FT VARIANT 650
FT /note="N -> H (in ARCND2; dbSNP:rs397514483)"
FT /evidence="ECO:0000269|PubMed:22560091"
FT /id="VAR_068563"
FT VARIANT 710
FT /note="G -> S (in dbSNP:rs6118603)"
FT /id="VAR_056695"
FT CONFLICT 447
FT /note="A -> P (in Ref. 1; AAB02027)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="F -> L (in Ref. 1; AAB02027)"
FT /evidence="ECO:0000305"
FT CONFLICT 787
FT /note="L -> P (in Ref. 1; AAB02027)"
FT /evidence="ECO:0000305"
FT CONFLICT 840
FT /note="K -> T (in Ref. 1; AAB02027)"
FT /evidence="ECO:0000305"
FT CONFLICT 902
FT /note="A -> P (in Ref. 1; AAB02027)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1175 AA; 134464 MW; AB2C8EB99EF57357 CRC64;
MAKPYEFNWQ KEVPSFLQEG AVFDRYEEES FVFEPNCLFK VDEFGFFLTW RSEGKEGQVL
ECSLINSIRS GAIPKDPKIL AALEAVGKSE NDLEGRIVCV CSGTDLVNIS FTYMVAENPE
VTKQWVEGLR SIIHNFRANN VSPMTCLKKH WMKLAFMTNT NGKIPVRSIT RTFASGKTEK
VIFQALKELG LPSGKNDEIE PTAFSYEKFY ELTQKICPRT DIEDLFKKIN GDKTDYLTVD
QLVSFLNEHQ RDPRLNEILF PFYDAKRAMQ IIEMYEPDED LKKKGLISSD GFCRYLMSDE
NAPVFLDRLE LYQEMDHPLA HYFISSSHNT YLTGRQFGGK SSVEMYRQVL LAGCRCVELD
CWDGKGEDQE PIITHGKAMC TDILFKDVIQ AIKETAFVTS EYPVILSFEN HCSKYQQYKM
SKYCEDLFGD LLLKQALESH PLEPGRALPS PNDLKRKILI KNKRLKPEVE KKQLEALRSM
MEAGESASPA NILEDDNEEE IESADQEEEA HPEFKFGNEL SADDLGHKEA VANSVKKGLV
TVEDEQAWMA SYKYVGATTN IHPYLSTMIN YAQPVKFQGF HVAEERNIHY NMSSFNESVG
LGYLKTHAIE FVNYNKRQMS RIYPKGGRVD SSNYMPQIFW NAGCQMVSLN YQTPDLAMQL
NQGKFEYNGS CGYLLKPDFM RRPDRTFDPF SETPVDGVIA ATCSVQVISG QFLSDKKIGT
YVEVDMYGLP TDTIRKEFRT RMVMNNGLNP VYNEESFVFR KVILPDLAVL RIAVYDDNNK
LIGQRILPLD GLQAGYRHIS LRNEGNKPLS LPTIFCNIVL KTYVPDGFGD IVDALSDPKK
FLSITEKRAD QMRAMGIETS DIADVPSDTS KNDKKGKANT AKANVTPQSS SELRPTTTAA
LASGVEAKKG IELIPQVRIE DLKQMKAYLK HLKKQQKELN SLKKKHAKEH STMQKLHCTQ
VDKIVAQYDK EKSTHEKILE KAMKKKGGSN CLEMKKETEI KIQTLTSDHK SKVKEIVAQH
TKEWSEMINT HSAEEQEIRD LHLSQQCELL KKLLINAHEQ QTQQLKLSHD RESKEMRAHQ
AKISMENSKA ISQDKSIKNK AERERRVREL NSSNTKKFLE ERKRLAMKQS KEMDQLKKVQ
LEHLEFLEKQ NEQAKEMQQM VKLEAEMDRR PATVV
