CBP1_CAEEL
ID CBP1_CAEEL Reviewed; 2017 AA.
AC P34545; B0M0M3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 6.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Protein cbp-1;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q92793};
GN Name=cbp-1; ORFNames=R10E11.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, INTERACTION WITH PRMT-5 AND CEP-1, MUTAGENESIS OF ARG-234, AND
RP METHYLATION AT ARG-234.
RX PubMed=19521535; DOI=10.1371/journal.pgen.1000514;
RA Yang M., Sun J., Sun X., Shen Q., Gao Z., Yang C.;
RT "Caenorhabditis elegans protein arginine methyltransferase PRMT-5
RT negatively regulates DNA damage-induced apoptosis.";
RL PLoS Genet. 5:E1000514-E1000514(2009).
RN [4] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=24811939; DOI=10.1002/dvdy.24146;
RA Wong M.C., Kennedy W.P., Schwarzbauer J.E.;
RT "Transcriptionally regulated cell adhesion network dictates distal tip cell
RT directionality.";
RL Dev. Dyn. 243:999-1010(2014).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31118512; DOI=10.1038/s41586-019-1243-y;
RA Cabianca D.S., Munoz-Jimenez C., Kalck V., Gaidatzis D., Padeken J.,
RA Seeber A., Askjaer P., Gasser S.M.;
RT "Active chromatin marks drive spatial sequestration of heterochromatin in
RT C. elegans nuclei.";
RL Nature 569:734-739(2019).
CC -!- FUNCTION: Acetyltransferase enzyme (By similarity). Acetylates
CC histones, giving a specific tag for transcriptional activation (By
CC similarity). May prevent DNA damage-induced apoptosis by inhibiting
CC cep-1-dependent transcription activation of the programmed cell death
CC activator egl-1 (PubMed:19521535). In differentiated cells, negatively
CC regulates localization of heterochromatin to the nuclear periphery
CC (PubMed:31118512). Plays a role in migration of gonadal distal tip
CC cells, where it probably modulates expression of genes involved in
CC integrin-mediated adhesion (PubMed:24811939).
CC {ECO:0000250|UniProtKB:Q92793, ECO:0000269|PubMed:24811939,
CC ECO:0000269|PubMed:31118512, ECO:0000303|PubMed:19521535}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000250|UniProtKB:Q92793};
CC -!- SUBUNIT: Interacts (via N-terminus domain and HAT domain) with prmt-5;
CC the interaction results in methylation of cbp-1 (PubMed:19521535).
CC Interacts (via HAT domain) with cep-1; cep-1 transcriptional activity
CC may be inhibited by interaction with methylated cbp-1
CC (PubMed:19521535). Component of a complex that contains prmt-5 and cbp-
CC 1 (PubMed:19521535). {ECO:0000269|PubMed:19521535,
CC ECO:0000303|PubMed:19521535}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92793}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b;
CC IsoId=P34545-1; Sequence=Displayed;
CC Name=a;
CC IsoId=P34545-2; Sequence=VSP_000557;
CC Name=c;
CC IsoId=P34545-3; Sequence=VSP_000557, VSP_044149;
CC -!- DEVELOPMENTAL STAGE: Expressed in the gonadal distal tip cells (DTC)
CC during larval stages L2, L3 and L4. {ECO:0000269|PubMed:24811939}.
CC -!- PTM: Methylation by prmt-5 may repress the capacity of cbp-1 to enhance
CC cep-1-dependent transcription of egl-1. {ECO:0000303|PubMed:19521535}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown targeted to the gonadal
CC distal tip cells (DTC) causes DTC migration defects (PubMed:24811939).
CC Significant reduction in expression of src-1, tln-1 and nmy-2 in DTCs
CC (PubMed:24811939). RNAi-mediated knockdown on an mrg-1;cec-4 double
CC mutant background restores positioning of heterochromatin to the
CC nuclear periphery (PubMed:31118512). {ECO:0000269|PubMed:24811939,
CC ECO:0000269|PubMed:31118512}.
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DR EMBL; Z29095; CAA82353.3; -; Genomic_DNA.
DR EMBL; Z29095; CAD18875.2; -; Genomic_DNA.
DR EMBL; Z29095; CAP72377.2; -; Genomic_DNA.
DR PIR; G88564; G88564.
DR PIR; S60123; S60123.
DR RefSeq; NP_001122711.2; NM_001129239.2. [P34545-3]
DR RefSeq; NP_499160.2; NM_066759.3. [P34545-1]
DR RefSeq; NP_499161.2; NM_066760.5. [P34545-2]
DR AlphaFoldDB; P34545; -.
DR SMR; P34545; -.
DR BioGRID; 41575; 15.
DR ComplexPortal; CPX-1131; Prmt-5-cep-1-cbp-1 complex.
DR STRING; 6239.R10E11.1b; -.
DR iPTMnet; P34545; -.
DR EPD; P34545; -.
DR PaxDb; P34545; -.
DR PeptideAtlas; P34545; -.
DR EnsemblMetazoa; R10E11.1a.1; R10E11.1a.1; WBGene00000366. [P34545-2]
DR EnsemblMetazoa; R10E11.1a.2; R10E11.1a.2; WBGene00000366. [P34545-2]
DR EnsemblMetazoa; R10E11.1b.1; R10E11.1b.1; WBGene00000366. [P34545-1]
DR EnsemblMetazoa; R10E11.1c.1; R10E11.1c.1; WBGene00000366. [P34545-3]
DR GeneID; 176380; -.
DR KEGG; cel:CELE_R10E11.1; -.
DR UCSC; R10E11.1c; c. elegans. [P34545-1]
DR CTD; 176380; -.
DR WormBase; R10E11.1a; CE47039; WBGene00000366; cbp-1. [P34545-2]
DR WormBase; R10E11.1b; CE46860; WBGene00000366; cbp-1. [P34545-1]
DR WormBase; R10E11.1c; CE46909; WBGene00000366; cbp-1. [P34545-3]
DR eggNOG; KOG1778; Eukaryota.
DR GeneTree; ENSGT00940000166210; -.
DR InParanoid; P34545; -.
DR OMA; XTISKDQ; -.
DR OrthoDB; 619848at2759; -.
DR PhylomeDB; P34545; -.
DR Reactome; R-CEL-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR Reactome; R-CEL-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-CEL-3214847; HATs acetylate histones.
DR Reactome; R-CEL-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-CEL-5689901; Metalloprotease DUBs.
DR Reactome; R-CEL-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-CEL-6782135; Dual incision in TC-NER.
DR Reactome; R-CEL-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-CEL-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-CEL-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-CEL-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
DR Reactome; R-CEL-8951936; RUNX3 regulates p14-ARF.
DR Reactome; R-CEL-9018519; Estrogen-dependent gene expression.
DR Reactome; R-CEL-9617629; Regulation of FOXO transcriptional activity by acetylation.
DR Reactome; R-CEL-9701898; STAT3 nuclear events downstream of ALK signaling.
DR Reactome; R-CEL-9759194; Nuclear events mediated by NFE2L2.
DR SignaLink; P34545; -.
DR PRO; PR:P34545; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000366; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0017053; C:transcription repressor complex; IPI:ComplexPortal.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:WormBase.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IDA:WormBase.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IDA:WormBase.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0016573; P:histone acetylation; IDA:WormBase.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; IDA:WormBase.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:ComplexPortal.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:WormBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:WormBase.
DR GO; GO:1903354; P:regulation of distal tip cell migration; IMP:UniProtKB.
DR GO; GO:0010975; P:regulation of neuron projection development; IMP:WormBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:WormBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:WormBase.
DR CDD; cd15802; RING_CBP-p300; 1.
DR Gene3D; 1.10.246.20; -; 1.
DR Gene3D; 1.20.1020.10; -; 2.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 2.10.110.40; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR003101; KIX_dom.
DR InterPro; IPR036529; KIX_dom_sf.
DR InterPro; IPR010303; RING_CBP-p300.
DR InterPro; IPR038547; RING_CBP-p300_sf.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; PTHR13808; 3.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF06001; DUF902; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF02172; KIX; 1.
DR Pfam; PF02135; zf-TAZ; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47040; SSF47040; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57933; SSF57933; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS50952; KIX; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Activator; Acyltransferase; Alternative splicing; Apoptosis; Bromodomain;
KW Chromatin regulator; Metal-binding; Methylation; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..2017
FT /note="Protein cbp-1"
FT /id="PRO_0000211189"
FT DOMAIN 593..672
FT /note="KIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00311"
FT DOMAIN 881..953
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 1112..1492
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01065"
FT ZN_FING 399..505
FT /note="TAZ-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT ZN_FING 1494..1540
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1550..1631
FT /note="TAZ-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT REGION 1..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..948
FT /note="Interaction with histone"
FT /evidence="ECO:0000250|UniProtKB:Q92793"
FT REGION 1224..1226
FT /note="Interaction with histone"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT REGION 1349..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1656..1828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1908..2017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..168
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1396
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1663..1680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1742..1781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1791..1808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1908..1931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1940..2017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1225..1227
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1237..1238
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1284
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1289
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1293
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1499
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1502
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1510
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1513
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1519
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1522
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1528
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1530
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 234
FT /note="Symmetric dimethylarginine; by PRMT5; in vitro"
FT /evidence="ECO:0000269|PubMed:19521535"
FT VAR_SEQ 467..478
FT /note="SDTTQTTKKCSV -> F (in isoform a and isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_000557"
FT VAR_SEQ 1893..1921
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_044149"
FT MUTAGEN 234
FT /note="R->A: Loss of methylation by prmt-5."
FT /evidence="ECO:0000269|PubMed:19521535"
SQ SEQUENCE 2017 AA; 222415 MW; AAA0D2A7962DF163 CRC64;
MDEPPSKKSR ADSDYDSGLD ALSALESLEA FPTSSKDTDV DNNPSTSAGG SGGPSGSTPH
PQGTPQPAPS NNGGFNLQPG QSQPQQPPQN MGGGVNGSVL QELLMNPSQT SNNSPRPQAY
PPGQQNAFNR SPMMPNGTPN MMSPPSMGRV PGPSPGGPQP PGPGQPQMRP GQPGMFQGDQ
QQQMMMGAQG QQFPGMMHRY PYAQGGPPPG AQGMPQGYPG VSRGGPTPGQ PMGRGAMMNG
AMPRSGPMPT QGRPGIPPNQ QAMMQPMMTD RQFMQHGQYG QQRPEFMQQY GRPGGYPMMH
QGMMMDSNGQ PIRGPNQMMM MSNGHPGMSH GPPNGQPGPQ AAAAQHAAQQ QAAAQAQAQA
AAQQQQQQQR EQEAAAAAQR NGAGRATTPG SSMLATHQDP EKRKLIQQQL VLLLHAHKCS
QREKENRDFA AKNQPPPHAA CTLPHCSTMK EVLTHMTSCN VGRLCHSDTT QTTKKCSVAH
CASSRQIIAH WKNCSREDCP VCKPLKRIQD TPLQFSLPDL ANLIGVNGNS NGSAEGDGLH
QFGSPAMRTG NITNSLFEGF NGNPFQNGPN RGGPRPPGGN GEIPNLPPPD MPDCTKEWHH
QVTKDLRNHL VGKLVKAIFP EPNQEAMNDN RLKDLIAYAR KVEKEMFESA NDREEYYHLL
AEKIYKIQKE LQEKKNSRLN QGAAAHDQYA IPPSNELAQM LGVEGGRSDV HSEGSSMAVA
PSQQNQPWGG APNSNMHQQI PPNGQVPQVN NSSTFPSSGN STPNIGASST VSAMLQPKTE
PMDDQNTDSL SSRPPTAIGF GGSSSSTPAP IMNGIVKKEE DPEESSNQAP PSVKDTKDGV
AESKPKEQQA KREPTPPPTE DTVFSQEDLI KFLLPVWEKL DKSEDAAPFR VPVDAKLLNI
PDYHEIIKRP MDLETVHKKL YAGQYQNAGQ FCDDIWLMLD NAWLYNRKNS KVYKYGLKLS
EMFVSEMDPV MKSMGYCCAK KLAFTPLSLF CYGAAMCTIA REQQYWVFEQ SSTQYNVTVT
ERYTYCQKCF DALPPEGISL SENPNDRNNM APKTSFTEQK NSVIDYEPFE RCKYCMRKWH
RICALHDKKV YPEGFICECC RTAKKYQKPD NKYLASKLPH NKLSTFLEDR VNGFIKKQLQ
AEAHKYPVII RTLCVQDKEA EVKAQMKQKY VESNQFPEKF PYRTKAVFAF EIIDGVEVCF
FGLHVQEYGS ACPAPNARRV YIAYLDSVHF FQPRELRTDV YHELLLGYLD YAKMLGYTMA
HIWACPPSEG DDYIFHCHPP EQKIPKPKRL QDWYKKMLEK GVQEGSVVEF KDIYKQARDD
NLTTPTQLPY FEGDFWPNVI EDCIREASNE EAQRKVKEDD DDGEDADGGL GGGDSGKKKS
SKNKKNNLKK NAKMNKKKAG SITGNEVADK LYSQFEKHKE VFFTIRLVSL QNEPAVLAKP
ISDPDGLMQS DMMDGRDTFL TKAREEHWEF SSLRRAKYST LCLAYSLHET DSKGMEYTCN
KCSSPAVWHC QSCDDFDLCD GCKPTTQHPH EMEKIKSLIG GGEAGDSAAG GTRYESIQRC
IASLVHACQC RDANCRRMSC HKMKRVVQHT KMCKKRINGT CPVCKQLIAL CCYHAKHCTR
DACTVPFCMN IRQKLAEQKR SQQRRADMMM RRRMEGLQSH VGGAAPTPST VSNGTPSNAP
TPPVSAGPGP AVKGGGVGQV QMQQHQGSHV GGSGPAGMGQ PMNSFGGMPG MGLGPNAQNG
PGLPGMNPQM NANQSRYMPN GPGLGQSGAP GQQQQPMYSS GMPMQRPGGL GGMNPQQQPQ
QQQGHPGLQN PGGRPGGVHG MGQNQPVRNN QDMVMNMQMQ NQHQQPPPFD STLQPQIMKI
NSRLKAAKTE EERETVFSDL KKTPHLFHAW LRMRENQNLV PNRMQGYSQM SMGSSNLQNL
QQQQLQQQQA GAMRGGGGFA PGQNNSQPRA PSGQFASMNP SMQQQYPQQQ QGWPQQRQQN
PGGMQQNANP YNQFQNRQNM MMMPQQQQPH PSNAGGQ
