RPN2_YEAST
ID RPN2_YEAST Reviewed; 945 AA.
AC P32565; D6VVK9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=26S proteasome regulatory subunit RPN2;
GN Name=RPN2; Synonyms=SEN3; OrderedLocusNames=YIL075C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7565784; DOI=10.1128/mcb.15.11.6311;
RA Demarini D.J., Papa F.R., Swaminathan S., Ursic D., Rasmussen T.P.,
RA Culbertson M.R., Hochstrasser M.;
RT "The yeast SEN3 gene encodes a regulatory subunit of the 26S proteasome
RT complex required for ubiquitin-dependent protein degradation in vivo.";
RL Mol. Cell. Biol. 15:6311-6321(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 2-9, AND ACETYLATION AT SER-2.
RX PubMed=12504901; DOI=10.1016/s0003-9861(02)00639-2;
RA Kimura Y., Saeki Y., Yokosawa H., Polevoda B., Sherman F., Hirano H.;
RT "N-terminal modifications of the 19S regulatory particle subunits of the
RT yeast proteasome.";
RL Arch. Biochem. Biophys. 409:341-348(2003).
RN [5]
RP FUNCTION.
RX PubMed=9584156; DOI=10.1128/mcb.18.6.3149;
RA Glickman M.H., Rubin D.M., Fried V.A., Finley D.;
RT "The regulatory particle of the Saccharomyces cerevisiae proteasome.";
RL Mol. Cell. Biol. 18:3149-3162(1998).
RN [6]
RP INTERACTION WITH UBR1.
RX PubMed=10688918; DOI=10.1073/pnas.060025497;
RA Xie Y., Varshavsky A.;
RT "Physical association of ubiquitin ligases and the 26S proteasome.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2497-2502(2000).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-801 AND THR-932, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.
RX PubMed=22927375; DOI=10.1073/pnas.1213333109;
RA Beck F., Unverdorben P., Bohn S., Schweitzer A., Pfeifer G., Sakata E.,
RA Nickell S., Plitzko J.M., Villa E., Baumeister W., Forster F.;
RT "Near-atomic resolution structural model of the yeast 26S proteasome.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:14870-14875(2012).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC {ECO:0000269|PubMed:9584156}.
CC -!- SUBUNIT: Interacts with UBR1. {ECO:0000269|PubMed:10688918}.
CC -!- INTERACTION:
CC P32565; P38764: RPN1; NbExp=3; IntAct=EBI-15919, EBI-15913;
CC P32565; P19812: UBR1; NbExp=2; IntAct=EBI-15919, EBI-19909;
CC -!- PTM: N-acetylated by NAT1. {ECO:0000269|PubMed:12504901}.
CC -!- MISCELLANEOUS: Present with 4750 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S1 family. {ECO:0000305}.
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DR EMBL; L06321; AAA87613.1; -; Genomic_DNA.
DR EMBL; Z37997; CAA86095.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08475.1; -; Genomic_DNA.
DR PIR; S48369; S48369.
DR RefSeq; NP_012190.1; NM_001179425.1.
DR PDB; 3JCO; EM; 4.80 A; N=1-945.
DR PDB; 3JCP; EM; 4.60 A; N=1-945.
DR PDB; 4ADY; X-ray; 2.70 A; A/B=2-945.
DR PDB; 4CR2; EM; 7.70 A; N=1-945.
DR PDB; 4CR3; EM; 9.30 A; N=1-945.
DR PDB; 4CR4; EM; 8.80 A; N=1-945.
DR PDB; 5A5B; EM; 9.50 A; N=1-945.
DR PDB; 5MPB; EM; 7.80 A; N=1-945.
DR PDB; 5MPC; EM; 7.70 A; N=1-945.
DR PDB; 5MPD; EM; 4.10 A; N=1-945.
DR PDB; 5MPE; EM; 4.50 A; N=1-945.
DR PDB; 5WVI; EM; 6.30 A; N=1-945.
DR PDB; 5WVK; EM; 4.20 A; N=1-945.
DR PDB; 6FVT; EM; 4.10 A; N=4-925.
DR PDB; 6FVU; EM; 4.50 A; N=4-925.
DR PDB; 6FVV; EM; 5.40 A; N=4-925.
DR PDB; 6FVW; EM; 4.50 A; N=4-925.
DR PDB; 6FVX; EM; 4.90 A; N=4-925.
DR PDB; 6FVY; EM; 6.10 A; N=4-925.
DR PDB; 6J2C; EM; 7.00 A; N=1-945.
DR PDB; 6J2N; EM; 7.50 A; N=1-945.
DR PDB; 6J2Q; EM; 3.80 A; N=1-945.
DR PDB; 6J2X; EM; 3.80 A; N=1-945.
DR PDB; 6J30; EM; 4.50 A; N=1-945.
DR PDB; 7QO3; EM; 6.10 A; N=1-945.
DR PDB; 7QO5; EM; 6.00 A; N=1-945.
DR PDBsum; 3JCO; -.
DR PDBsum; 3JCP; -.
DR PDBsum; 4ADY; -.
DR PDBsum; 4CR2; -.
DR PDBsum; 4CR3; -.
DR PDBsum; 4CR4; -.
DR PDBsum; 5A5B; -.
DR PDBsum; 5MPB; -.
DR PDBsum; 5MPC; -.
DR PDBsum; 5MPD; -.
DR PDBsum; 5MPE; -.
DR PDBsum; 5WVI; -.
DR PDBsum; 5WVK; -.
DR PDBsum; 6FVT; -.
DR PDBsum; 6FVU; -.
DR PDBsum; 6FVV; -.
DR PDBsum; 6FVW; -.
DR PDBsum; 6FVX; -.
DR PDBsum; 6FVY; -.
DR PDBsum; 6J2C; -.
DR PDBsum; 6J2N; -.
DR PDBsum; 6J2Q; -.
DR PDBsum; 6J2X; -.
DR PDBsum; 6J30; -.
DR PDBsum; 7QO3; -.
DR PDBsum; 7QO5; -.
DR AlphaFoldDB; P32565; -.
DR SMR; P32565; -.
DR BioGRID; 34917; 144.
DR ComplexPortal; CPX-2262; 26S Proteasome complex.
DR DIP; DIP-4638N; -.
DR IntAct; P32565; 84.
DR MINT; P32565; -.
DR STRING; 4932.YIL075C; -.
DR iPTMnet; P32565; -.
DR MaxQB; P32565; -.
DR PaxDb; P32565; -.
DR PRIDE; P32565; -.
DR EnsemblFungi; YIL075C_mRNA; YIL075C; YIL075C.
DR GeneID; 854735; -.
DR KEGG; sce:YIL075C; -.
DR SGD; S000001337; RPN2.
DR VEuPathDB; FungiDB:YIL075C; -.
DR eggNOG; KOG2062; Eukaryota.
DR GeneTree; ENSGT00940000153386; -.
DR HOGENOM; CLU_002323_0_0_1; -.
DR InParanoid; P32565; -.
DR OMA; MIMVQQN; -.
DR BioCyc; YEAST:G3O-31340-MON; -.
DR Reactome; R-SCE-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-SCE-382556; ABC-family proteins mediated transport.
DR Reactome; R-SCE-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-68949; Orc1 removal from chromatin.
DR Reactome; R-SCE-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-SCE-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-SCE-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-SCE-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-SCE-8951664; Neddylation.
DR Reactome; R-SCE-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P32565; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P32565; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000502; C:proteasome complex; IPI:ComplexPortal.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IDA:SGD.
DR GO; GO:0034515; C:proteasome storage granule; IDA:SGD.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:SGD.
DR GO; GO:0043248; P:proteasome assembly; IGI:SGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR016642; 26S_Psome_Rpn2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR035266; PSMD1.
DR InterPro; IPR040623; RPN2_C.
DR PANTHER; PTHR10943:SF2; PTHR10943:SF2; 1.
DR Pfam; PF01851; PC_rep; 2.
DR Pfam; PF18004; RPN2_C; 1.
DR PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Phosphoprotein;
KW Proteasome; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12504901,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..945
FT /note="26S proteasome regulatory subunit RPN2"
FT /id="PRO_0000173808"
FT REPEAT 366..399
FT /note="PC 1"
FT REPEAT 403..440
FT /note="PC 2"
FT REPEAT 445..479
FT /note="PC 3"
FT REPEAT 480..514
FT /note="PC 4"
FT REPEAT 516..549
FT /note="PC 5"
FT REPEAT 550..585
FT /note="PC 6"
FT REPEAT 586..618
FT /note="PC 7"
FT REPEAT 620..654
FT /note="PC 8"
FT REPEAT 655..692
FT /note="PC 9"
FT REPEAT 698..734
FT /note="PC 10"
FT REGION 810..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:12504901,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 801
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 932
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 333..334
FT /note="SV -> RL (in Ref. 1; AAA87613)"
FT /evidence="ECO:0000305"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 18..40
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 58..72
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 96..119
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 131..147
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 179..195
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 200..216
FT /evidence="ECO:0007829|PDB:4ADY"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 251..264
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 267..279
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 293..306
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 311..320
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 326..339
FT /evidence="ECO:0007829|PDB:4ADY"
FT TURN 340..343
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 347..351
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 362..374
FT /evidence="ECO:0007829|PDB:4ADY"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 382..386
FT /evidence="ECO:0007829|PDB:4ADY"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 398..411
FT /evidence="ECO:0007829|PDB:4ADY"
FT TURN 412..416
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 417..430
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 437..453
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 460..471
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 475..489
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 495..507
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 511..524
FT /evidence="ECO:0007829|PDB:4ADY"
FT TURN 525..527
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 529..532
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 533..541
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 545..558
FT /evidence="ECO:0007829|PDB:4ADY"
FT TURN 559..561
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 565..577
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 581..594
FT /evidence="ECO:0007829|PDB:4ADY"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 602..605
FT /evidence="ECO:0007829|PDB:4ADY"
FT TURN 606..608
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 609..611
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 615..628
FT /evidence="ECO:0007829|PDB:4ADY"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 635..645
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 650..663
FT /evidence="ECO:0007829|PDB:4ADY"
FT TURN 669..671
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 675..687
FT /evidence="ECO:0007829|PDB:4ADY"
FT STRAND 689..691
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 693..706
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 709..711
FT /evidence="ECO:0007829|PDB:4ADY"
FT STRAND 713..715
FT /evidence="ECO:0007829|PDB:4ADY"
FT TURN 720..722
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 727..736
FT /evidence="ECO:0007829|PDB:4ADY"
FT TURN 737..741
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 743..752
FT /evidence="ECO:0007829|PDB:4ADY"
FT STRAND 753..755
FT /evidence="ECO:0007829|PDB:4ADY"
FT STRAND 757..762
FT /evidence="ECO:0007829|PDB:4ADY"
FT TURN 763..766
FT /evidence="ECO:0007829|PDB:4ADY"
FT STRAND 767..769
FT /evidence="ECO:0007829|PDB:4ADY"
FT STRAND 772..775
FT /evidence="ECO:0007829|PDB:4ADY"
FT TURN 779..782
FT /evidence="ECO:0007829|PDB:4ADY"
FT STRAND 866..869
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 878..881
FT /evidence="ECO:0007829|PDB:4ADY"
FT STRAND 886..894
FT /evidence="ECO:0007829|PDB:4ADY"
FT STRAND 898..908
FT /evidence="ECO:0007829|PDB:4ADY"
FT HELIX 920..924
FT /evidence="ECO:0007829|PDB:4ADY"
SQ SEQUENCE 945 AA; 104232 MW; 881E78EBC6BD934F CRC64;
MSLTTAAPLL ALLRENQDSV KTYALESINN VVDQLWSEIS NELPDIEALY DDDTFSDREM
AALIASKVYY NLGEYESAVK YALAAKDRFD IDEKSQFVET IVSKSIEMYV QEASKQYTKD
EQFYTKDIID PKLTSIFERM IEKCLKASEL KLALGIALEG YRLDIIESAL KSKLDQDSTS
ENVKIINYLL TLAITTVTNS KFRSSILRKS FDFLMNMPNC DYLTLNKVVV NLNDAGLALQ
LFKKLKEEND EGLSAQIAFD LVSSASQQLL EILVTELTAQ GYDPALLNIL SGLPTCDYYN
TFLLNNKNID IGLLNKSKSS LDGKFSLFHT AVSVANGFMH AGTTDNSFIK ANLPWLGKAQ
NWAKFTATAS LGVIHKGNLL EGKKVMAPYL PGSRASSRFI KGGSLYGLGL IYAGFGRDTT
DYLKNIIVEN SGTSGDEDVD VLLHGASLGI GLAAMGSANI EVYEALKEVL YNDSATSGEA
AALGMGLCML GTGKPEAIHD MFTYSQETQH GNITRGLAVG LALINYGRQE LADDLITKML
ASDESLLRYG GAFTIALAYA GTGNNSAVKR LLHVAVSDSN DDVRRAAVIA LGFVLLRDYT
TVPRIVQLLS KSHNAHVRCG TAFALGIACA GKGLQSAIDV LDPLTKDPVD FVRQAAMIAL
SMILIQQTEK LNPQVADINK NFLSVITNKH QEGLAKFGAC VAQGIMNAGG RNVTIQLENA
DTGTLDTKSV VGLVMFSQFW YWFPLAHFLS LSFTPTTVIG IRGSDQAIPK FQMNCYAKED
AFSYPRMYEE ASGKEVEKVA TAVLSTTARA KARAKKTKKE KGPNEEEKKK EHEEKEKERE
TNKKGIKETK ENDEEFYKNK YSSKPYKVDN MTRILPQQSR YISFIKDDRF VPVRKFKGNN
GVVVLRDREP KEPVALIETV RQMKDVNAPL PTPFKVDDNV DFPSA
