ID UBP16_MOUSE Reviewed; 825 AA. AC Q99LG0; G5E860; Q99KM0; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 11-DEC-2013, sequence version 2. DT 27-MAR-2024, entry version 168. DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 16 {ECO:0000255|HAMAP-Rule:MF_03062}; DE EC=3.4.19.12 {ECO:0000255|HAMAP-Rule:MF_03062}; DE AltName: Full=Deubiquitinating enzyme 16 {ECO:0000255|HAMAP-Rule:MF_03062}; DE AltName: Full=Ubiquitin thioesterase 16 {ECO:0000255|HAMAP-Rule:MF_03062}; DE AltName: Full=Ubiquitin-specific-processing protease 16 {ECO:0000255|HAMAP-Rule:MF_03062}; GN Name=Usp16; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor; 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414 AND SER-531, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver, Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [7] RP FUNCTION, AND PHOSPHORYLATION. RX PubMed=24034696; DOI=10.1016/j.molcel.2013.08.022; RA Frangini A., Sjoberg M., Roman-Trufero M., Dharmalingam G., Haberle V., RA Bartke T., Lenhard B., Malumbres M., Vidal M., Dillon N.; RT "The Aurora B kinase and the Polycomb protein Ring1B combine to regulate RT active promoters in quiescent lymphocytes."; RL Mol. Cell 51:647-661(2013). RN [8] RP UP-REGULATION IN DOWN SYNDROME MODELS. RX PubMed=24025767; DOI=10.1038/nature12530; RA Adorno M., Sikandar S., Mitra S.S., Kuo A., Nicolis Di Robilant B., RA Haro-Acosta V., Ouadah Y., Quarta M., Rodriguez J., Qian D., Reddy V.M., RA Cheshier S., Garner C.C., Clarke M.F.; RT "Usp16 contributes to somatic stem-cell defects in Down's syndrome."; RL Nature 501:380-384(2013). CC -!- FUNCTION: Specifically deubiquitinates 'Lys-120' of histone H2A CC (H2AK119Ub), a specific tag for epigenetic transcriptional repression, CC thereby acting as a coactivator. Deubiquitination of histone H2A is a CC prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 CC (H3S10ph), and is required for chromosome segregation when cells enter CC into mitosis. In resting B- and T-lymphocytes, phosphorylation by AURKB CC leads to enhance its activity, thereby maintaining transcription in CC resting lymphocytes (PubMed:24034696). Regulates Hox gene expression CC via histone H2A deubiquitination. Prefers nucleosomal substrates. Does CC not deubiquitinate histone H2B. Also deubiquitinates non-histone CC proteins, such as ribosomal protein RPS27A: deubiquitination of CC monoubiquitinated RPS27A promotes maturation of the 40S ribosomal CC subunit. {ECO:0000255|HAMAP-Rule:MF_03062, CC ECO:0000269|PubMed:24034696}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- CC residue protein attached to proteins as an intracellular targeting CC signal).; EC=3.4.19.12; Evidence={ECO:0000255|HAMAP-Rule:MF_03062}; CC -!- SUBUNIT: Homotetramer. Associates with late pre-40S ribosomes. CC {ECO:0000255|HAMAP-Rule:MF_03062}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03062}. CC Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03062}. CC -!- DOMAIN: The UBP-type zinc finger binds 3 zinc ions that form a pair of CC cross-braced ring fingers encapsulated within a third zinc finger in CC the primary structure. It recognizes the C-terminal tail of free CC ubiquitin. {ECO:0000255|HAMAP-Rule:MF_03062}. CC -!- PTM: Phosphorylated at the onset of mitosis and dephosphorylated during CC the metaphase/anaphase transition. Phosphorylation by AURKB enhances CC the deubiquitinase activity. {ECO:0000255|HAMAP-Rule:MF_03062, CC ECO:0000269|PubMed:24034696}. CC -!- MISCELLANEOUS: Usp16 acts as a regulator of stem cell self-renewal and CC its overexpression contributes to somatic stem cell defects observed in CC Down syndrome models in mouse. Usp16 is triplicated in Ts65D Down CC syndrome mouse model and its overexpression leads to reduce the self- CC renewal of haematopoietic stem cells and the expansion of mammary CC epithelial cells, neural progenitors and fibroblasts. Defects are CC rescued by down-regulating Usp16 in Ts65D mice by short interfering CC RNAs (PubMed:24025767). {ECO:0000305|PubMed:24025767}. CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP16 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_03062}. 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; AK160038; BAE35580.1; -; mRNA. DR EMBL; AC154631; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466521; EDK98336.1; -; Genomic_DNA. DR EMBL; BC003278; AAH03278.1; -; mRNA. DR EMBL; BC004577; AAH04577.1; -; mRNA. DR CCDS; CCDS28291.1; -. DR RefSeq; NP_077220.2; NM_024258.2. DR RefSeq; XP_006523163.1; XM_006523100.2. DR AlphaFoldDB; Q99LG0; -. DR BioGRID; 216501; 8. DR STRING; 10090.ENSMUSP00000026710; -. DR MEROPS; C19.050; -. DR GlyGen; Q99LG0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q99LG0; -. DR PhosphoSitePlus; Q99LG0; -. DR EPD; Q99LG0; -. DR MaxQB; Q99LG0; -. DR PaxDb; 10090-ENSMUSP00000026710; -. DR PeptideAtlas; Q99LG0; -. DR ProteomicsDB; 298455; -. DR Pumba; Q99LG0; -. DR Antibodypedia; 6359; 400 antibodies from 34 providers. DR DNASU; 74112; -. DR Ensembl; ENSMUST00000026710.12; ENSMUSP00000026710.6; ENSMUSG00000025616.15. DR GeneID; 74112; -. DR KEGG; mmu:74112; -. DR UCSC; uc007zuk.2; mouse. DR AGR; MGI:1921362; -. DR CTD; 10600; -. DR MGI; MGI:1921362; Usp16. DR VEuPathDB; HostDB:ENSMUSG00000025616; -. DR eggNOG; KOG1873; Eukaryota. DR GeneTree; ENSGT00940000156013; -. DR HOGENOM; CLU_007938_1_0_1; -. DR InParanoid; Q99LG0; -. DR OMA; MAAGHYV; -. DR OrthoDB; 227085at2759; -. DR PhylomeDB; Q99LG0; -. DR TreeFam; TF326075; -. DR Reactome; R-MMU-5689880; Ub-specific processing proteases. DR BioGRID-ORCS; 74112; 13 hits in 80 CRISPR screens. DR ChiTaRS; Usp16; mouse. DR PRO; PR:Q99LG0; -. DR Proteomes; UP000000589; Chromosome 16. DR RNAct; Q99LG0; Protein. DR Bgee; ENSMUSG00000025616; Expressed in animal zygote and 269 other cell types or tissues. DR ExpressionAtlas; Q99LG0; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB. DR GO; GO:0042393; F:histone binding; ISS:UniProtKB. DR GO; GO:0140950; F:histone H2A deubiquitinase activity; IMP:UniProtKB. DR GO; GO:0043024; F:ribosomal small subunit binding; ISS:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB. DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0006974; P:DNA damage response; ISS:UniProtKB. DR GO; GO:0016578; P:histone deubiquitination; IEA:UniProtKB-UniRule. DR GO; GO:0140014; P:mitotic nuclear division; IEA:UniProtKB-UniRule. DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0090070; P:positive regulation of ribosome biogenesis; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB. DR GO; GO:0045901; P:positive regulation of translational elongation; ISS:UniProtKB. DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR CDD; cd02667; Peptidase_C19K; 1. DR Gene3D; 3.90.70.10; Cysteine proteinases; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR HAMAP; MF_03062; UBP16; 1. DR InterPro; IPR038765; Papain-like_cys_pep_sf. DR InterPro; IPR001394; Peptidase_C19_UCH. DR InterPro; IPR030849; UBP16. DR InterPro; IPR018200; USP_CS. DR InterPro; IPR028889; USP_dom. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR001607; Znf_UBP. DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1. DR PANTHER; PTHR21646:SF12; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 16; 1. DR Pfam; PF00443; UCH; 1. DR Pfam; PF02148; zf-UBP; 1. DR SMART; SM00290; ZnF_UBP; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS00972; USP_1; 1. DR PROSITE; PS00973; USP_2; 1. DR PROSITE; PS50235; USP_3; 1. DR PROSITE; PS50271; ZF_UBP; 1. DR Genevisible; Q99LG0; MM. PE 1: Evidence at protein level; KW Activator; Cell cycle; Cell division; Chromatin regulator; Cytoplasm; KW Hydrolase; Isopeptide bond; Metal-binding; Mitosis; Nucleus; KW Phosphoprotein; Protease; Reference proteome; Thiol protease; KW Transcription; Transcription regulation; Ubl conjugation; KW Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..825 FT /note="Ubiquitin carboxyl-terminal hydrolase 16" FT /id="PRO_0000367503" FT DOMAIN 195..824 FT /note="USP" FT ZN_FING 22..141 FT /note="UBP-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 164..184 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 393..456 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 164..181 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 394..425 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 436..452 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 204 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03062" FT ACT_SITE 759 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03062" FT BINDING 24 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 26 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 48 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 51 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 73 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 76 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 81 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 89 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 93 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 102 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 115 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 118 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT MOD_RES 188 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y5T5" FT MOD_RES 414 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 520 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355" FT MOD_RES 531 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT CROSSLNK 139 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9Y5T5" FT CONFLICT 173 FT /note="R -> K (in Ref. 1; BAE35580 and 4; AAH03278)" FT /evidence="ECO:0000305" SQ SEQUENCE 825 AA; 93434 MW; 08E8ED64D233461E CRC64; MGKKRTKGRS APDTVASESA EPVCRHLRKG LEQGNLKKAL VNVEWNICQD CKTDNKVKDK PEEEAEDPSV WLCLKCGHQG CGRDSQEQHA LKHYTTPRSE PHYLVLSLDN WSVWCYKCDE EVKYCSSNRL GQVVDYVRKQ AGVRTSKPAE KNNGHIELEN KKLEKESKNE QEREKSENLA KETIPMDSAS QITVKGLSNL GNTCFFNAVM QNLSQTPVLR ELLKEVKMSG TIVKIEPPDL ALTEPLEVNL EPPGPLTLAM SQFLSEMQEN KKRVVTPKEL FSQVCKKATR FKGYQQQDSQ ELLRYLLDGM RAEEHQRVSK GILKAFGNST EKLDEEVKNK VKDYEKKKAI PSFVDRIFGG ELTSTIMCDE CRTVSLVHES FLDLSLPVLD DQSGKKSIND KNVKMTMEEE DKDSEEEKDD SYMKSRSDLP SGTSKHLQKK AKKQAKKQAK NQRRQQKIQE RFLHFNELCA TDYTEDNERE ADTALAGEVE VDTDSTHGSQ EEATQIELSV NQKDLDGQES MIERTPDVQE SPEDLGVKSA NTESDLGIVT PAPECPRDFN GAFLEERTSG ELDIINGLKN LNLNAAVDPD EINIEIPNDS HSAPKVYEVM NEDPETAFCT LANREAFSTD ECSIQHCLYQ FTRNEKLQDA NKLLCEVCSR RQCNGPKANI KGDRRHVYTN AKKQMLVSLA PPVLTLHLKR FQQAGFNLRK VNKHIKFPEI LDLAPFCTLK CKNVAEESTR VLYSLYGVVE HSGTMRSGHY TAYAKERTAS CHLSNLVLHG DIPQDCEMES TKGQWFHISD THVQAVPITK VLNSQAYLLF YERIL //