ID PLCL2_HUMAN Reviewed; 1127 AA.
AC Q9UPR0; A8K5V4; Q8N498; Q9H8L0; Q9UFP9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 24-JAN-2024, entry version 186.
DE RecName: Full=Inactive phospholipase C-like protein 2;
DE Short=PLC-L(2);
DE Short=PLC-L2;
DE Short=Phospholipase C-L2;
DE AltName: Full=Phospholipase C-epsilon-2;
DE Short=PLC-epsilon-2;
GN Name=PLCL2; Synonyms=KIAA1092, PLCE2;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 384-1127 (ISOFORM 2).
RC TISSUE=Brain, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS ARG-211;
RP MET-635; VAL-742; HIS-809 AND ARG-890.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 918-1127.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-584 AND SER-1113, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; THR-584 AND SER-1113, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1113, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-584, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May play an role in the regulation of Ins(1,4,5)P3 around the
CC endoplasmic reticulum. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UPR0; P22607: FGFR3; NbExp=3; IntAct=EBI-311059, EBI-348399;
CC Q9UPR0; P06396: GSN; NbExp=3; IntAct=EBI-311059, EBI-351506;
CC Q9UPR0; P01112: HRAS; NbExp=3; IntAct=EBI-311059, EBI-350145;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Predominantly localized to
CC perinuclear areas in both myoblast and myotube C2C12 cells.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UPR0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPR0-2; Sequence=VSP_025790, VSP_025791, VSP_025792;
CC Name=3;
CC IsoId=Q9UPR0-3; Sequence=VSP_025790;
CC -!- CAUTION: In the PI-PLC X-box Thr-486 is present instead of the
CC conserved His which is one of the active site residues. It is therefore
CC expected that this protein lacks catalytic activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83044.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14606.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB029015; BAA83044.1; ALT_INIT; mRNA.
DR EMBL; AK023546; BAB14606.1; ALT_INIT; mRNA.
DR EMBL; AK291419; BAF84108.1; -; mRNA.
DR EMBL; BC036392; AAH36392.1; -; mRNA.
DR EMBL; AL117515; CAB55974.1; -; mRNA.
DR CCDS; CCDS33713.1; -. [Q9UPR0-3]
DR CCDS; CCDS74911.1; -. [Q9UPR0-1]
DR PIR; T17284; T17284.
DR RefSeq; NP_001137854.1; NM_001144382.1. [Q9UPR0-1]
DR RefSeq; NP_055999.2; NM_015184.5. [Q9UPR0-3]
DR RefSeq; XP_016861511.1; XM_017006022.1.
DR RefSeq; XP_016861512.1; XM_017006023.1.
DR RefSeq; XP_016861513.1; XM_017006024.1.
DR RefSeq; XP_016861514.1; XM_017006025.1. [Q9UPR0-3]
DR AlphaFoldDB; Q9UPR0; -.
DR SMR; Q9UPR0; -.
DR BioGRID; 116833; 15.
DR IntAct; Q9UPR0; 11.
DR MINT; Q9UPR0; -.
DR STRING; 9606.ENSP00000478458; -.
DR GlyGen; Q9UPR0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UPR0; -.
DR PhosphoSitePlus; Q9UPR0; -.
DR BioMuta; PLCL2; -.
DR DMDM; 148880116; -.
DR EPD; Q9UPR0; -.
DR jPOST; Q9UPR0; -.
DR MassIVE; Q9UPR0; -.
DR MaxQB; Q9UPR0; -.
DR PaxDb; 9606-ENSP00000478458; -.
DR PeptideAtlas; Q9UPR0; -.
DR ProteomicsDB; 85423; -. [Q9UPR0-1]
DR ProteomicsDB; 85424; -. [Q9UPR0-2]
DR ProteomicsDB; 85425; -. [Q9UPR0-3]
DR Pumba; Q9UPR0; -.
DR Antibodypedia; 26950; 179 antibodies from 29 providers.
DR DNASU; 23228; -.
DR Ensembl; ENST00000432376.5; ENSP00000412836.1; ENSG00000154822.18. [Q9UPR0-3]
DR Ensembl; ENST00000615277.5; ENSP00000478458.1; ENSG00000154822.18. [Q9UPR0-1]
DR Ensembl; ENST00000638327.1; ENSP00000491897.1; ENSG00000284017.2. [Q9UPR0-3]
DR Ensembl; ENST00000638466.2; ENSP00000492839.1; ENSG00000284017.2. [Q9UPR0-1]
DR GeneID; 23228; -.
DR KEGG; hsa:23228; -.
DR MANE-Select; ENST00000615277.5; ENSP00000478458.1; NM_001144382.2; NP_001137854.1.
DR UCSC; uc011awd.3; human. [Q9UPR0-1]
DR AGR; HGNC:9064; -.
DR CTD; 23228; -.
DR DisGeNET; 23228; -.
DR GeneCards; PLCL2; -.
DR HGNC; HGNC:9064; PLCL2.
DR HPA; ENSG00000154822; Tissue enhanced (skeletal).
DR MIM; 614276; gene.
DR neXtProt; NX_Q9UPR0; -.
DR OpenTargets; ENSG00000154822; -.
DR PharmGKB; PA33395; -.
DR VEuPathDB; HostDB:ENSG00000154822; -.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000155660; -.
DR InParanoid; Q9UPR0; -.
DR OMA; MRTSWIS; -.
DR OrthoDB; 2900494at2759; -.
DR PhylomeDB; Q9UPR0; -.
DR TreeFam; TF313216; -.
DR PathwayCommons; Q9UPR0; -.
DR SignaLink; Q9UPR0; -.
DR BioGRID-ORCS; 23228; 12 hits in 1151 CRISPR screens.
DR ChiTaRS; PLCL2; human.
DR GenomeRNAi; 23228; -.
DR Pharos; Q9UPR0; Tbio.
DR PRO; PR:Q9UPR0; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UPR0; Protein.
DR Bgee; ENSG00000154822; Expressed in cortical plate and 106 other cell types or tissues.
DR ExpressionAtlas; Q9UPR0; baseline and differential.
DR Genevisible; Q9UPR0; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050811; F:GABA receptor binding; IDA:MGI.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:InterPro.
DR GO; GO:0002322; P:B cell proliferation involved in immune response; IEA:Ensembl.
DR GO; GO:0002337; P:B-1a B cell differentiation; IEA:Ensembl.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0050859; P:negative regulation of B cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IEA:Ensembl.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd16223; EFh_PRIP2; 1.
DR CDD; cd13364; PH_PLC_eta; 1.
DR CDD; cd08597; PI-PLCc_PRIP_metazoa; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
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; 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; IPR028382; PLCL2_EFh.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF84; INACTIVE PHOSPHOLIPASE C-LIKE PROTEIN 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; 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; 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 Acetylation; Alternative splicing; Cytoplasm; Phosphoprotein;
KW Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..1127
FT /note="Inactive phospholipase C-like protein 2"
FT /id="PRO_0000288851"
FT DOMAIN 141..251
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 426..570
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 618..734
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 734..863
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K394"
FT MOD_RES 584
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 1113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..126
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025790"
FT VAR_SEQ 1069..1086
FT /note="GQADLLKYAKNETLENLK -> IRKTGRRSIFVPQTPIMV (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025791"
FT VAR_SEQ 1087..1127
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025792"
FT VARIANT 211
FT /note="Q -> R (in dbSNP:rs17853614)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032507"
FT VARIANT 635
FT /note="V -> M (in dbSNP:rs17857109)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032508"
FT VARIANT 742
FT /note="A -> V (in dbSNP:rs17857110)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032509"
FT VARIANT 809
FT /note="P -> H (in dbSNP:rs17853612)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032510"
FT VARIANT 890
FT /note="H -> R (in dbSNP:rs17853613)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032511"
SQ SEQUENCE 1127 AA; 125866 MW; F75F774DAE18EC5F CRC64;
MAECGRGGAA GGALPTSPGP ALGAKGALKA GVGEGGGGGG RLGHGRARYD SGGVSNGDCS
LGVSGDEARA SPTRGPRGVA LAPTPSAVVC TLPRESKPGG LPRRSSIIKD GTKQKRERKK
TVSFSSMPTE KKISSASDCI NSMVEGSELK KVRSNSRIYH RYFLLDADMQ SLRWEPSKKD
SEKAKIDIKS IKEVRTGKNT DIFRSNGISD QISEDCAFSV IYGENYESLD LVANSADVAN
IWVTGLRYLI SYGKHTLDML ESSQDNMRTS WVSQMFSEID VDNLGHITLC NAVQCIRNLN
PGLKTSKIEL KFKELHKSKD KAGTEVTKEE FIEVFHELCT RPEIYFLLVQ FSSNKEFLDT
KDLMMFLEAE QGVAHINEEI SLEIIHKYEP SKEGQEKGWL SIDGFTNYLM SPDCYIFDPE
HKKVCQDMKQ PLSHYFINSS HNTYLIEDQF RGPSDITGYI RALKMGCRSV ELDVWDGPDN
EPVIYTGHTM TSQIVFRSVI DIINKYAFFA SEYPLILCLE NHCSIKQQKV MVQHMKKLLG
DKLYTTSPNV EESYLPSPDV LKGKILIKAK KLSSNCSGVE GDVTDEDEGA EMSQRMGKEN
MEQPNNVPVK RFQLCKELSE LVSICKSVQF KEFQVSFQVQ KYWEVCSFNE VLASKYANEN
PGDFVNYNKR FLARVFPSPM RIDSSNMNPQ DFWKCGCQIV AMNFQTPGLM MDLNIGWFRQ
NGNCGYVLRP AIMREEVSFF SANTKDSVPG VSPQLLHIKI ISGQNFPKPK GSGAKGDVVD
PYVYVEIHGI PADCAEQRTK TVHQNGDAPI FDESFEFQIN LPELAMVRFV VLDDDYIGDE
FIGQYTIPFE CLQTGYRHVP LQSLTGEVLA HASLFVHVAI TNRRGGGKPH KRGLSVRKGK
KSREYASLRT LWIKTVDEVF KNAQPPIRDA TDLRENMQNA VVSFKELCGL SSVANLMQCM
LAVSPRFLGP DNTPLVVLNL SEQYPTMELQ GIVPEVLKKI VTTYDMMIQS LKALIENADA
VYEKIVHCQK AAMEFHEHLH SIGTKEGLKE RKLQKAVESF TWNITILKGQ ADLLKYAKNE
TLENLKQIHF AAVSCGLNKP GTENADVQKP RRSLEVIPEK ANDETGE
//
