CSN2_HUMAN
ID CSN2_HUMAN Reviewed; 443 AA.
AC P61201; O88950; Q15647; Q6FGP4; Q9BY54; Q9R249; Q9UNI2; Q9UNQ5;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=COP9 signalosome complex subunit 2;
DE Short=SGN2;
DE Short=Signalosome subunit 2;
DE AltName: Full=Alien homolog;
DE AltName: Full=JAB1-containing signalosome subunit 2;
DE AltName: Full=Thyroid receptor-interacting protein 15;
DE Short=TR-interacting protein 15;
DE Short=TRIP-15;
GN Name=COPS2; Synonyms=CSN2, TRIP15;
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).
RA Dumdey R., Bech-Otschir D., Ferrell K., Dubiel W.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pituitary;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Pituitary;
RA Peng Y., Li Y., Tu Y., Xu S., Han Z., Fu G., Chen Z.;
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-236 (ISOFORM 1).
RX PubMed=7776974; DOI=10.1210/mend.9.2.7776974;
RA Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
RT "Two classes of proteins dependent on either the presence or absence of
RT thyroid hormone for interaction with the thyroid hormone receptor.";
RL Mol. Endocrinol. 9:243-254(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-443 (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH NR2F1.
RX PubMed=10207062; DOI=10.1128/mcb.19.5.3383;
RA Dressel U., Thormeyer D., Altincicek B., Paululat A., Eggert M.,
RA Schneider S., Tenbaum S.P., Renkawitz R., Baniahmad A.;
RT "Alien, a highly conserved protein with characteristics of a corepressor
RT for members of the nuclear hormone receptor superfamily.";
RL Mol. Cell. Biol. 19:3383-3394(1999).
RN [8]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9535219; DOI=10.1096/fasebj.12.6.469;
RA Seeger M., Kraft R., Ferrell K., Bech-Otschir D., Dumdey R., Schade R.,
RA Gordon C., Naumann M., Dubiel W.;
RT "A novel protein complex involved in signal transduction possessing
RT similarities to 26S proteasome subunits.";
RL FASEB J. 12:469-478(1998).
RN [9]
RP INTERACTION WITH NR0B1.
RX PubMed=10713076; DOI=10.1074/jbc.275.11.7662;
RA Altincicek B., Tenbaum S.P., Dressel U., Thormeyer D., Renkawitz R.,
RA Baniahmad A.;
RT "Interaction of the corepressor Alien with DAX-1 is abrogated by mutations
RT of DAX-1 involved in adrenal hypoplasia congenita.";
RL J. Biol. Chem. 275:7662-7667(2000).
RN [10]
RP INTERACTION WITH IRF8/ICSBP1.
RX PubMed=10991940; DOI=10.1074/jbc.m004900200;
RA Cohen H., Azriel A., Cohen T., Meraro D., Hashmueli S., Bech-Otschir D.,
RA Kraft R., Dubiel W., Levi B.Z.;
RT "Interaction between interferon consensus sequence-binding protein and
RT COP9/signalosome subunit CSN2 (Trip15). A possible link between interferon
RT regulatory factor signaling and the COP9/signalosome.";
RL J. Biol. Chem. 275:39081-39089(2000).
RN [11]
RP FUNCTION.
RX PubMed=11285227; DOI=10.1093/emboj/20.7.1630;
RA Bech-Otschir D., Kraft R., Huang X., Henklein P., Kapelari B., Pollmann C.,
RA Dubiel W.;
RT "COP9 signalosome-specific phosphorylation targets p53 to degradation by
RT the ubiquitin system.";
RL EMBO J. 20:1630-1639(2001).
RN [12]
RP FUNCTION, COMPOSITION OF THE CSN COMPLEX, AND INTERACTION WITH CUL1.
RX PubMed=11337588; DOI=10.1126/science.1059780;
RA Lyapina S., Cope G., Shevchenko A., Serino G., Tsuge T., Zhou C.,
RA Wolf D.A., Wei N., Shevchenko A., Deshaies R.J.;
RT "Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome.";
RL Science 292:1382-1385(2001).
RN [13]
RP FUNCTION.
RX PubMed=12732143; DOI=10.1016/s0092-8674(03)00316-7;
RA Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R.,
RA Kisselev A.F., Tanaka K., Nakatani Y.;
RT "The ubiquitin ligase activity in the DDB2 and CSA complexes is
RT differentially regulated by the COP9 signalosome in response to DNA
RT damage.";
RL Cell 113:357-367(2003).
RN [14]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=12628923; DOI=10.1093/emboj/cdg127;
RA Uhle S., Medalia O., Waldron R., Dumdey R., Henklein P., Bech-Otschir D.,
RA Huang X., Berse M., Sperling J., Schade R., Dubiel W.;
RT "Protein kinase CK2 and protein kinase D are associated with the COP9
RT signalosome.";
RL EMBO J. 22:1302-1312(2003).
RN [15]
RP IDENTIFICATION IN THE CSN COMPLEX.
RX PubMed=18850735; DOI=10.1021/pr800574c;
RA Fang L., Wang X., Yamoah K., Chen P.L., Pan Z.Q., Huang L.;
RT "Characterization of the human COP9 signalosome complex using affinity
RT purification and mass spectrometry.";
RL J. Proteome Res. 7:4914-4925(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP IDENTIFICATION BY 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).
RN [18]
RP COMPOSITION OF THE CSN COMPLEX.
RX PubMed=26456823; DOI=10.1016/j.celrep.2015.09.021;
RA Rozen S., Fuezesi-Levi M.G., Ben-Nissan G., Mizrachi L., Gabashvili A.,
RA Levin Y., Ben-Dor S., Eisenstein M., Sharon M.;
RT "CSNAP is a stoichiometric subunit of the COP9 signalosome.";
RL Cell Rep. 13:585-598(2015).
CC -!- FUNCTION: Essential component of the COP9 signalosome complex (CSN), a
CC complex involved in various cellular and developmental processes. The
CC CSN complex is an essential regulator of the ubiquitin (Ubl)
CC conjugation pathway by mediating the deneddylation of the cullin
CC subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl
CC ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The
CC complex is also involved in phosphorylation of p53/TP53, c-jun/JUN,
CC IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association
CC with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN
CC promotes and protects degradation by the Ubl system, respectively.
CC Involved in early stage of neuronal differentiation via its interaction
CC with NIF3L1. {ECO:0000269|PubMed:11285227, ECO:0000269|PubMed:11337588,
CC ECO:0000269|PubMed:12628923, ECO:0000269|PubMed:12732143,
CC ECO:0000269|PubMed:9535219}.
CC -!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1, COPS2,
CC COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9
CC isoform 1 (PubMed:11337588, PubMed:18850735, PubMed:26456823). In the
CC complex, it probably interacts directly with COPS1, COPS4, COPS5, COPS6
CC and COPS7 (COPS7A or COPS7B) (PubMed:11337588, PubMed:18850735).
CC Specifically interacts with the ligand binding domain of the thyroid
CC receptor (TR). Does not require the presence of thyroid hormone for its
CC interaction (By similarity). Interacts with CUL1 and CUL2
CC (PubMed:11337588). Interacts with IRF8/ICSBP1 and with nuclear
CC receptors NR2F1 and NR0B1 (PubMed:10207062, PubMed:10713076,
CC PubMed:10991940). Interacts with NIF3L1 (By similarity).
CC {ECO:0000250|UniProtKB:P61202, ECO:0000269|PubMed:10207062,
CC ECO:0000269|PubMed:10713076, ECO:0000269|PubMed:10991940,
CC ECO:0000269|PubMed:11337588, ECO:0000269|PubMed:18850735,
CC ECO:0000269|PubMed:26456823}.
CC -!- INTERACTION:
CC P61201; Q9UNS2: COPS3; NbExp=11; IntAct=EBI-1050386, EBI-350590;
CC P61201; Q92793: CREBBP; NbExp=3; IntAct=EBI-1050386, EBI-81215;
CC P61201; Q09472: EP300; NbExp=2; IntAct=EBI-1050386, EBI-447295;
CC P61201; Q13098-7: GPS1; NbExp=5; IntAct=EBI-1050386, EBI-10983983;
CC P61201; P49821: NDUFV1; NbExp=3; IntAct=EBI-1050386, EBI-748312;
CC P61201; O00231: PSMD11; NbExp=3; IntAct=EBI-1050386, EBI-357816;
CC P61201; O76024: WFS1; NbExp=3; IntAct=EBI-1050386, EBI-720609;
CC P61201; Q9NWS9-2: ZNF446; NbExp=3; IntAct=EBI-1050386, EBI-740232;
CC P61201; P45481: Crebbp; Xeno; NbExp=2; IntAct=EBI-1050386, EBI-296306;
CC P61201; PRO_0000037946 [P29991]; Xeno; NbExp=3; IntAct=EBI-1050386, EBI-8826488;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9535219}. Nucleus
CC {ECO:0000269|PubMed:10207062}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61201-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61201-2; Sequence=VSP_011884;
CC -!- PTM: Phosphorylated by CK2 and PKD kinases.
CC {ECO:0000269|PubMed:12628923}.
CC -!- SIMILARITY: Belongs to the CSN2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD30269.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/COPS2ID47362ch15q21.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF084260; AAC34122.1; -; mRNA.
DR EMBL; AF100762; AAD43026.1; -; mRNA.
DR EMBL; AF212227; AAK26250.1; -; mRNA.
DR EMBL; CR542063; CAG46860.1; -; mRNA.
DR EMBL; BC012629; AAH12629.1; -; mRNA.
DR EMBL; L40388; AAC41734.1; -; mRNA.
DR EMBL; AF120268; AAD30269.1; ALT_FRAME; mRNA.
DR CCDS; CCDS32235.1; -. [P61201-1]
DR CCDS; CCDS45257.1; -. [P61201-2]
DR RefSeq; NP_001137359.1; NM_001143887.1. [P61201-2]
DR RefSeq; NP_004227.1; NM_004236.3. [P61201-1]
DR PDB; 4D10; X-ray; 3.80 A; B/J=1-443.
DR PDB; 4D18; X-ray; 4.08 A; B/J=1-443.
DR PDB; 4WSN; X-ray; 5.50 A; B/J/R/Z/h/p=1-443.
DR PDB; 6A73; X-ray; 2.45 A; A/B=29-162.
DR PDB; 6R6H; EM; 8.40 A; B=1-443.
DR PDB; 6R7F; EM; 8.20 A; B=1-443.
DR PDB; 6R7H; EM; 8.80 A; B=30-443.
DR PDB; 6R7I; EM; 5.90 A; B=1-443.
DR PDB; 6R7N; EM; 6.50 A; B=1-443.
DR PDBsum; 4D10; -.
DR PDBsum; 4D18; -.
DR PDBsum; 4WSN; -.
DR PDBsum; 6A73; -.
DR PDBsum; 6R6H; -.
DR PDBsum; 6R7F; -.
DR PDBsum; 6R7H; -.
DR PDBsum; 6R7I; -.
DR PDBsum; 6R7N; -.
DR AlphaFoldDB; P61201; -.
DR SMR; P61201; -.
DR BioGRID; 114729; 187.
DR ComplexPortal; CPX-1870; COP9 signalosome variant 1.
DR ComplexPortal; CPX-1871; COP9 signalosome variant 2.
DR CORUM; P61201; -.
DR DIP; DIP-42076N; -.
DR IntAct; P61201; 69.
DR MINT; P61201; -.
DR STRING; 9606.ENSP00000299259; -.
DR GlyConnect; 2031; 1 N-Linked glycan (1 site).
DR GlyGen; P61201; 2 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P61201; -.
DR MetOSite; P61201; -.
DR PhosphoSitePlus; P61201; -.
DR SwissPalm; P61201; -.
DR BioMuta; COPS2; -.
DR DMDM; 47117681; -.
DR EPD; P61201; -.
DR jPOST; P61201; -.
DR MassIVE; P61201; -.
DR MaxQB; P61201; -.
DR PaxDb; P61201; -.
DR PeptideAtlas; P61201; -.
DR PRIDE; P61201; -.
DR ProteomicsDB; 57272; -. [P61201-1]
DR ProteomicsDB; 57273; -. [P61201-2]
DR Antibodypedia; 12106; 424 antibodies from 39 providers.
DR DNASU; 9318; -.
DR Ensembl; ENST00000299259.10; ENSP00000299259.6; ENSG00000166200.15. [P61201-2]
DR Ensembl; ENST00000388901.10; ENSP00000373553.5; ENSG00000166200.15. [P61201-1]
DR GeneID; 9318; -.
DR KEGG; hsa:9318; -.
DR MANE-Select; ENST00000388901.10; ENSP00000373553.5; NM_004236.4; NP_004227.1.
DR UCSC; uc001zxf.4; human. [P61201-1]
DR CTD; 9318; -.
DR DisGeNET; 9318; -.
DR GeneCards; COPS2; -.
DR HGNC; HGNC:30747; COPS2.
DR HPA; ENSG00000166200; Low tissue specificity.
DR MIM; 604508; gene.
DR neXtProt; NX_P61201; -.
DR OpenTargets; ENSG00000166200; -.
DR PharmGKB; PA134952445; -.
DR VEuPathDB; HostDB:ENSG00000166200; -.
DR eggNOG; KOG1464; Eukaryota.
DR GeneTree; ENSGT00530000063301; -.
DR HOGENOM; CLU_028981_0_1_1; -.
DR InParanoid; P61201; -.
DR OMA; RNYQEAG; -.
DR PhylomeDB; P61201; -.
DR TreeFam; TF105738; -.
DR PathwayCommons; P61201; -.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle.
DR SignaLink; P61201; -.
DR BioGRID-ORCS; 9318; 710 hits in 1101 CRISPR screens.
DR ChiTaRS; COPS2; human.
DR GeneWiki; COPS2; -.
DR GenomeRNAi; 9318; -.
DR Pharos; P61201; Tbio.
DR PRO; PR:P61201; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P61201; protein.
DR Bgee; ENSG00000166200; Expressed in cartilage tissue and 212 other tissues.
DR ExpressionAtlas; P61201; baseline and differential.
DR Genevisible; P61201; HS.
DR GO; GO:0008180; C:COP9 signalosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0001833; P:inner cell mass cell proliferation; IEA:Ensembl.
DR GO; GO:1903507; P:negative regulation of nucleic acid-templated transcription; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0000338; P:protein deneddylation; IDA:UniProtKB.
DR GO; GO:0045116; P:protein neddylation; IC:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:2000434; P:regulation of protein neddylation; IC:ComplexPortal.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:UniProtKB.
DR GO; GO:0001834; P:trophectodermal cell proliferation; IEA:Ensembl.
DR InterPro; IPR037750; COPS2.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10678:SF3; PTHR10678:SF3; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Nucleus; Phosphoprotein; Reference proteome; Signalosome.
FT CHAIN 1..443
FT /note="COP9 signalosome complex subunit 2"
FT /id="PRO_0000120968"
FT DOMAIN 254..416
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..275
FT /note="Mediates interaction with NIF3L1"
FT /evidence="ECO:0000250|UniProtKB:P61203"
FT VAR_SEQ 124
FT /note="Q -> QNSDFLCQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_011884"
FT CONFLICT 36
FT /note="Y -> N (in Ref. 3; CAG46860)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="T -> A (in Ref. 2; AAD43026)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="N -> T (in Ref. 3; CAG46860)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="R -> Q (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="C -> S (in Ref. 7)"
FT /evidence="ECO:0000305"
FT HELIX 34..42
FT /evidence="ECO:0007829|PDB:6A73"
FT HELIX 47..60
FT /evidence="ECO:0007829|PDB:6A73"
FT HELIX 65..82
FT /evidence="ECO:0007829|PDB:6A73"
FT HELIX 85..101
FT /evidence="ECO:0007829|PDB:6A73"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:6A73"
FT HELIX 125..139
FT /evidence="ECO:0007829|PDB:6A73"
FT HELIX 147..162
FT /evidence="ECO:0007829|PDB:6A73"
SQ SEQUENCE 443 AA; 51597 MW; 1DB6FA774C13BC59 CRC64;
MSDMEDDFMC DDEEDYDLEY SEDSNSEPNV DLENQYYNSK ALKEDDPKAA LSSFQKVLEL
EGEKGEWGFK ALKQMIKINF KLTNFPEMMN RYKQLLTYIR SAVTRNYSEK SINSILDYIS
TSKQMDLLQE FYETTLEALK DAKNDRLWFK TNTKLGKLYL EREEYGKLQK ILRQLHQSCQ
TDDGEDDLKK GTQLLEIYAL EIQMYTAQKN NKKLKALYEQ SLHIKSAIPH PLIMGVIREC
GGKMHLREGE FEKAHTDFFE AFKNYDESGS PRRTTCLKYL VLANMLMKSG INPFDSQEAK
PYKNDPEILA MTNLVSAYQN NDITEFEKIL KTNHSNIMDD PFIREHIEEL LRNIRTQVLI
KLIKPYTRIH IPFISKELNI DVADVESLLV QCILDNTIHG RIDQVNQLLE LDHQKRGGAR
YTALDKWTNQ LNSLNQAVVS KLA
