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   24-JAN-2024, entry version 113.
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,
RC   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).
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; 7.
DR   IntAct; B1AY13; 2.
DR   MINT; B1AY13; -.
DR   STRING; 10090.ENSMUSP00000092538; -.
DR   GlyGen; B1AY13; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; B1AY13; -.
DR   PhosphoSitePlus; B1AY13; -.
DR   SwissPalm; B1AY13; -.
DR   EPD; B1AY13; -.
DR   jPOST; B1AY13; -.
DR   MaxQB; B1AY13; -.
DR   PaxDb; 10090-ENSMUSP00000092538; -.
DR   PeptideAtlas; B1AY13; -.
DR   ProteomicsDB; 297792; -. [B1AY13-1]
DR   ProteomicsDB; 297793; -. [B1AY13-2]
DR   Pumba; B1AY13; -.
DR   Antibodypedia; 33232; 201 antibodies from 26 providers.
DR   DNASU; 329908; -.
DR   Ensembl; ENSMUST00000094933.5; ENSMUSP00000092538.5; ENSMUSG00000028514.16. [B1AY13-1]
DR   GeneID; 329908; -.
DR   KEGG; mmu:329908; -.
DR   UCSC; uc008tyf.2; mouse. [B1AY13-2]
DR   UCSC; uc008tyh.2; mouse. [B1AY13-1]
DR   AGR; MGI:1919936; -.
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; CSCYMNS; -.
DR   OrthoDB; 6206at2759; -.
DR   PhylomeDB; B1AY13; -.
DR   TreeFam; TF323966; -.
DR   Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR   BioGRID-ORCS; 329908; 9 hits in 81 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 258 other cell types or tissues.
DR   ExpressionAtlas; B1AY13; baseline and differential.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02659; peptidase_C19C; 1.
DR   CDD; cd14286; UBA_UBP24; 1.
DR   CDD; cd17065; Ubl_UBP24; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   InterPro; IPR016024; ARM-type_fold.
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; IPR047061; UBP24_Ubl.
DR   InterPro; IPR033382; USP24_UBA.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF729; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 24; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   Genevisible; B1AY13; MM.
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
//