UBP24_MOUSE
ID UBP24_MOUSE Reviewed; 2617 AA.
AC B1AY13; Q8BLI7;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 24;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 24;
DE AltName: Full=Ubiquitin thioesterase 24;
DE AltName: Full=Ubiquitin-specific-processing protease 24;
GN Name=Usp24;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 MRNA] OF 2384-2617 (ISOFORM 1).
RC STRAIN=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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-939, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2044 AND SER-2074, AND
RP IDENTIFICATION BY 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-2044, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1138; SER-1940; SER-2044;
RP THR-2562 AND SER-2601, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
CC -!- FUNCTION: Protease that can remove conjugated ubiquitin from target
CC proteins and polyubiquitin chains. Deubiquitinates DDB2, preventing its
CC proteasomal degradation (By similarity). {ECO:0000250}.
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;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B1AY13-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B1AY13-2; Sequence=VSP_035661, VSP_035662;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AK045043; BAC32195.1; -; mRNA.
DR EMBL; AL840623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL954352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029165; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS51251.1; -. [B1AY13-1]
DR RefSeq; NP_899048.2; NM_183225.2. [B1AY13-1]
DR AlphaFoldDB; B1AY13; -.
DR SMR; B1AY13; -.
DR BioGRID; 236858; 4.
DR IntAct; B1AY13; 2.
DR MINT; B1AY13; -.
DR STRING; 10090.ENSMUSP00000092538; -.
DR iPTMnet; B1AY13; -.
DR PhosphoSitePlus; B1AY13; -.
DR SwissPalm; B1AY13; -.
DR EPD; B1AY13; -.
DR jPOST; B1AY13; -.
DR MaxQB; B1AY13; -.
DR PaxDb; B1AY13; -.
DR PeptideAtlas; B1AY13; -.
DR PRIDE; B1AY13; -.
DR ProteomicsDB; 297792; -. [B1AY13-1]
DR ProteomicsDB; 297793; -. [B1AY13-2]
DR Antibodypedia; 33232; 177 antibodies from 26 providers.
DR DNASU; 329908; -.
DR Ensembl; ENSMUST00000094933; ENSMUSP00000092538; ENSMUSG00000028514. [B1AY13-1]
DR GeneID; 329908; -.
DR KEGG; mmu:329908; -.
DR UCSC; uc008tyf.2; mouse. [B1AY13-2]
DR UCSC; uc008tyh.2; mouse. [B1AY13-1]
DR CTD; 23358; -.
DR MGI; MGI:1919936; Usp24.
DR VEuPathDB; HostDB:ENSMUSG00000028514; -.
DR eggNOG; KOG1866; Eukaryota.
DR GeneTree; ENSGT00940000159474; -.
DR HOGENOM; CLU_058347_0_0_1; -.
DR InParanoid; B1AY13; -.
DR OMA; GRNTDQG; -.
DR OrthoDB; 625455at2759; -.
DR PhylomeDB; B1AY13; -.
DR TreeFam; TF323966; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 329908; 9 hits in 76 CRISPR screens.
DR ChiTaRS; Usp24; mouse.
DR PRO; PR:B1AY13; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; B1AY13; protein.
DR Bgee; ENSMUSG00000028514; Expressed in temporalis muscle and 255 other tissues.
DR ExpressionAtlas; B1AY13; baseline and differential.
DR Genevisible; B1AY13; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021905; DUF3517.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR033382; USP24.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006:SF729; PTHR24006:SF729; 1.
DR Pfam; PF12030; DUF3517; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..2617
FT /note="Ubiquitin carboxyl-terminal hydrolase 24"
FT /id="PRO_0000353213"
FT DOMAIN 3..44
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 1686..2039
FT /note="USP"
FT REGION 45..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1920..1942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2060..2087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2572..2617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2572..2597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1695
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 1967
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPU5"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPU5"
FT MOD_RES 939
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 1138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPU5"
FT MOD_RES 1940
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2044
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 2074
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 2558
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPU5"
FT MOD_RES 2562
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 408..418
FT /note="TKLIEDSTLSK -> SVHLSHMWPLM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035661"
FT VAR_SEQ 419..2617
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035662"
SQ SEQUENCE 2617 AA; 294001 MW; 802DFE22143B2C94 CRC64;
MESEEEQHMT TLLCMGFSDP ATIRKALRLA KNDINEAVAL LTNERPGLDY GGYEPMDSGG
PSPGPGGGPR GDSGSDGSGP SRGGSTGGGG GFDPPPAYHE VVDAEKNDEN GNCSGEGIEF
PTTNLYELES RVLTDHWSIP YKREESLGKC LLASTYLARL GLSESDENCK RFMERCMPEA
FKKLLTSSAV HKWGTEIHEG IYNMLMLLIE LVAERMKQDP IPIGLLGVLT MAFNPDNEYH
FKNRMKVSQR NWAEVFGEGN MFAISPVSTF QKEPHGWVVD LVNKFGELGG FAAIQAKLHS
EDIELGAVSA LVQPLGVCAE YLNSSVVQPM LDPVILTTIQ DVRSVEEKDL KDKRLVSIPE
LLSAIKLLCM RFQPALVTTV DALRLDILLR MLKSPHFSAK MNSLKEVTKL IEDSTLSKSV
KNAIDTDRLL DWLVENSVLS IALEGNIDQA QYCDRIKGII ELLGSKLSLD ELTKIWKIQS
GQSSTVIENI HTIIAAAAVK FNADQLNHLF VLIQKSWETE SDRVRQKLLS LIGRIGREAR
FEATSGKVLD VLWELAHLPT LPSSLIQQAL EEHLTILSDA YAVKEAVKRS YIIKCIEDIK
RPGEWSSLEK NKKDGFKSSQ LNNPQFVWVV PALRQLHEIT RSFIKQTYQK QDKSIIQDLK
KNFEIVKLVT GSLLACHRLA AAVAGPGGLT GLTLVDGRYT YREYLEAHLK FLAFFLQEAT
LYLGWNRAKE IWECLVTGQD VCELDREMCF EWFTKGQHDL ESDVQQQLFK EKILKLESYE
ITMNGFNLFK TFFENVNLCD HRLKRQGAQL YVEKLELVGM DFIWKIAMES PDEEIANEAI
QLIINYSYIN LNPRLKKDSV SLHKKFIADC YTRLEAASSA LGGPTLTHAV TRATKMLTAT
AMPTVATSVQ SPYRSTKLVI IERLLLLAER YVITIEDFYS VPRTILPHGA SFHGHLLTLN
VTYESTKDTF TVEAHSNETI GSVRWKIAKQ LCSPVDNIQI FTNDSLLTVN KDQKLLHQLG
FSDEQVLTVK TSGSGTPSGS SADSSTSSSS SSSGAFSSSY AMEQEKSLPG VVMALVCNVF
DMLYQLANLE EPRITLRVRK LLLLIPTDPA IQEALDQLDS LGRKKTLLSE TSSQSSKSPS
LSSKQQHQPS ASSILESLFR SFAPGMSTFR VLYNLEVLSS KLMPTADDDM ARSCAKSFCE
NFLKAGGLSL VVNVMQRDSI PSEVDYETRQ GVYSICLQLA RFLLVGQTMP TSLDEDLTKD
GIEALSSRPF RNVSRQTSRQ MSLCGTPEKS SYRQLSVSDR SSIRVEEIIP AARVAIQTME
ASDFTATVAC FMRLSWAAAA GRLDLVGSSQ PIKESNSLFP AGIRSRLSSS GSNCSSSSEG
EPAALHAGIC VRQQSVSTKD ALIAGEALSL LVTCLQLRSQ QLASFYSLPC VADFIIDILL
GSPSAEIRRV ACDQLYTLSQ TDTSAHPEVQ KPNQFLLGVI LTAQLPLWSP TSIMRGVNQR
LLSQCMEYFD LRCQLLDDLT TSEMDQLRIS PATMLEDEIT WLDNFEPNRT ADCETSEADN
ILLAGHLRLI KTLLSLCGAE KEMLGSSLIK PLLDDFLFRA SRIIVNSHSP ASSAAISQQD
FHPKCSTVNS RLAAYEVLVM LADSSPSNLQ IITKELLSMH HQPDPALTKE FDYLPPVDSR
SSSGFVGLRN GGATCYMNAV FQQLYMQPGL PESLLSVDDD TDNPDDSVFY QVQSLFGHLM
ESKLQYYVPE NFWKIFKMWN KELYVREQQD AYEFFTSLID QMDEYLKKMG REQIFKNTFQ
GIYSDQKICK DCPHRYEREE AFMALNLGVT SCQSLEISLD QFVRGEVLEG SNAYYCEKCK
EKRITVKRTC IKSLPSVLVI HLMRFGFDWE SGRSIKYDEQ IRFPWMLNME PYTVAGMARQ
DSSSEVGENG RNMDQGGGGS PRKKVALTEN YELVGVIVHS GQAHAGHYYS FIKDRRGCGK
GKWYKFNDTV IEEFDLNDET LEYECFGGEY RPKVYDQTNP YTDVRRRYWN AYMLFYQRVS
DQNSPVLPKK SRVSVVRQEA EDLSLSAPSS PEISPQSSPR PHRPNNDRLS ILTKLVKKGE
KKGLFVEKMP ARIYQMVRDE NLKFMKNRDV YSSDYFSFVL SLASLNATKL KHPYYPCMAK
VSLQLAIQFL FQTYLRTKKK LRVDTEEWIA TIEALLSKSL DACQWLVEYF ISSEGRELVK
VFLLECSVRE VRVAVATILE KTLDSALFYQ DKLKSLHQLL EVLLALLDKD VPENCKNCAQ
YFSLFNTFVQ KQGIRAGDLL LRHSALRHMI SFLLGVSRQN SQIRRWSSAQ AREFGNLHNT
VALLVLHSDV SSQRNVAPGI FKQRPPISVA PSSPLLPLHE EVEALLFLSE GKPYLLEVMF
ALRELTGSLL ALMEMVVYCC FCNEHFSFTM LHFIKNQLET APPHELKNTF QLLHEVLVIE
DPIQVERVKF VFETENGLLA LMHHSNHVDS SRCYQCVKFL VTLAQKCPAA KEYFKENSHH
WSWAVQWLQK KMSEHYWTPQ SNVSNETSTG KTFQRTISAQ DTLAYATALL NEKEQSGSSN
GSESSPANEN GERHLQQGSE SPMMIGELRS DLDDVDP
