ID   UBP34_MOUSE             Reviewed;        3582 AA.
AC   Q6ZQ93; A2AF26; A2AF27; A2AF77; Q3UF93; Q3UPN0; Q6P563; Q7TMJ6; Q8CCH0;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 3.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 34;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q70CQ2};
DE   AltName: Full=Deubiquitinating enzyme 34;
DE   AltName: Full=Ubiquitin thioesterase 34;
DE   AltName: Full=Ubiquitin-specific-processing protease 34;
GN   Name=Usp34; Synonyms=Kiaa0570, Murr2;
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 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 225-639; 2096-2278 AND 2437-3582
RP   (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Ovary, Sympathetic ganglion, and Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2279-3582 (ISOFORM 3).
RC   TISSUE=Embryonic tail;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2346-2569 AND 3160-3376.
RC   STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and 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   IDENTIFICATION.
RX   PubMed=9001233; DOI=10.1128/mcb.17.2.789;
RA   Nabetani A., Hatada I., Morisaki H., Oshimura M., Mukai T.;
RT   "Mouse U2af1-rs1 is a neomorphic imprinted gene.";
RL   Mol. Cell. Biol. 17:789-798(1997).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2525, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486; SER-487; SER-490;
RP   SER-1506; SER-2525; SER-3395; SER-3396; THR-3418 AND SER-3443, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, 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: Ubiquitin hydrolase that can remove conjugated ubiquitin from
CC       AXIN1 and AXIN2, thereby acting as a regulator of Wnt signaling
CC       pathway. Acts as an activator of the Wnt signaling pathway downstream
CC       of the beta-catenin destruction complex by deubiquitinating and
CC       stabilizing AXIN1 and AXIN2, leading to promote nuclear accumulation of
CC       AXIN1 and AXIN2 and positively regulate beta-catenin (CTNBB1)-mediated
CC       transcription. Recognizes and hydrolyzes the peptide bond at the C-
CC       terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin
CC       precursors as well as that of ubiquitinated proteins.
CC       {ECO:0000250|UniProtKB:Q70CQ2}.
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:0000250|UniProtKB:Q70CQ2};
CC   -!- SUBUNIT: Interacts with AXIN1 and AXIN2.
CC       {ECO:0000250|UniProtKB:Q70CQ2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6ZQ93-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZQ93-2; Sequence=VSP_035641, VSP_035642;
CC       Name=3;
CC         IsoId=Q6ZQ93-3; Sequence=VSP_035641, VSP_035642, VSP_020465;
CC       Name=4;
CC         IsoId=Q6ZQ93-4; Sequence=VSP_035641, VSP_035642, VSP_020464;
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH55938.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=CAM20294.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL672049; CAM16931.1; -; Genomic_DNA.
DR   EMBL; AL672049; CAM16940.1; -; Genomic_DNA.
DR   EMBL; AL672004; CAM16940.1; JOINED; Genomic_DNA.
DR   EMBL; AL772359; CAM16940.1; JOINED; Genomic_DNA.
DR   EMBL; AL928722; CAM16940.1; JOINED; Genomic_DNA.
DR   EMBL; AL672004; CAM17339.1; -; Genomic_DNA.
DR   EMBL; AL672004; CAM17340.1; -; Genomic_DNA.
DR   EMBL; AL672049; CAM17340.1; JOINED; Genomic_DNA.
DR   EMBL; AL772359; CAM17340.1; JOINED; Genomic_DNA.
DR   EMBL; AL928722; CAM17340.1; JOINED; Genomic_DNA.
DR   EMBL; AL772359; CAM20294.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL672004; CAM20294.1; JOINED; Genomic_DNA.
DR   EMBL; AL672049; CAM20294.1; JOINED; Genomic_DNA.
DR   EMBL; AL928722; CAM20294.1; JOINED; Genomic_DNA.
DR   EMBL; AL928722; CAO77877.1; -; Genomic_DNA.
DR   EMBL; AL672004; CAO77877.1; JOINED; Genomic_DNA.
DR   EMBL; AL672049; CAO77877.1; JOINED; Genomic_DNA.
DR   EMBL; AL772359; CAO77877.1; JOINED; Genomic_DNA.
DR   EMBL; AK033182; BAC28186.1; -; mRNA.
DR   EMBL; AK143407; BAE25365.1; -; mRNA.
DR   EMBL; AK148805; BAE28668.1; -; mRNA.
DR   EMBL; AK129165; BAC97975.1; -; mRNA.
DR   EMBL; BC055938; AAH55938.1; ALT_SEQ; mRNA.
DR   EMBL; BC063062; AAH63062.1; -; mRNA.
DR   CCDS; CCDS56763.1; -. [Q6ZQ93-1]
DR   RefSeq; NP_001177330.2; NM_001190401.2. [Q6ZQ93-1]
DR   SMR; Q6ZQ93; -.
DR   BioGRID; 201621; 4.
DR   STRING; 10090.ENSMUSP00000137430; -.
DR   MEROPS; C19.067; -.
DR   GlyGen; Q6ZQ93; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6ZQ93; -.
DR   PhosphoSitePlus; Q6ZQ93; -.
DR   EPD; Q6ZQ93; -.
DR   jPOST; Q6ZQ93; -.
DR   MaxQB; Q6ZQ93; -.
DR   PaxDb; 10090-ENSMUSP00000120747; -.
DR   PeptideAtlas; Q6ZQ93; -.
DR   ProteomicsDB; 298417; -. [Q6ZQ93-1]
DR   ProteomicsDB; 298418; -. [Q6ZQ93-2]
DR   ProteomicsDB; 298419; -. [Q6ZQ93-3]
DR   ProteomicsDB; 298420; -. [Q6ZQ93-4]
DR   Pumba; Q6ZQ93; -.
DR   Antibodypedia; 7689; 108 antibodies from 24 providers.
DR   Ensembl; ENSMUST00000180046.8; ENSMUSP00000137430.2; ENSMUSG00000056342.17. [Q6ZQ93-1]
DR   GeneID; 17847; -.
DR   KEGG; mmu:17847; -.
DR   UCSC; uc029rkw.1; mouse. [Q6ZQ93-1]
DR   AGR; MGI:109473; -.
DR   CTD; 9736; -.
DR   MGI; MGI:109473; Usp34.
DR   VEuPathDB; HostDB:ENSMUSG00000056342; -.
DR   eggNOG; KOG1866; Eukaryota.
DR   GeneTree; ENSGT00940000158659; -.
DR   HOGENOM; CLU_000109_0_0_1; -.
DR   InParanoid; Q6ZQ93; -.
DR   OMA; KLMYSLY; -.
DR   OrthoDB; 6206at2759; -.
DR   PhylomeDB; Q6ZQ93; -.
DR   Reactome; R-MMU-201681; TCF dependent signaling in response to WNT.
DR   Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR   BioGRID-ORCS; 17847; 8 hits in 78 CRISPR screens.
DR   ChiTaRS; Usp34; mouse.
DR   PRO; PR:Q6ZQ93; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q6ZQ93; Protein.
DR   Bgee; ENSMUSG00000056342; Expressed in superior cervical ganglion and 259 other cell types or tissues.
DR   ExpressionAtlas; Q6ZQ93; 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; ISS:UniProtKB.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd02659; peptidase_C19C; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF948; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 34; 1.
DR   Pfam; PF12030; DUF3517; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   Genevisible; Q6ZQ93; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Phosphoprotein; Protease;
KW   Reference proteome; Thiol protease; Ubl conjugation pathway;
KW   Wnt signaling pathway.
FT   CHAIN           1..3582
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 34"
FT                   /id="PRO_0000249520"
FT   DOMAIN          1931..2276
FT                   /note="USP"
FT   REGION          503..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          775..801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1496..1515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3369..3484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..608
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..653
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..701
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        775..797
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3371..3410
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3414..3446
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3466..3484
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1940
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        2201
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   MOD_RES         352
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q70CQ2"
FT   MOD_RES         486
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         487
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         490
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1506
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2525
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15345747,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         3395
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         3396
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         3418
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         3423
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q70CQ2"
FT   MOD_RES         3443
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         3539
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q70CQ2"
FT   VAR_SEQ         1..151
FT                   /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14621295,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_035641"
FT   VAR_SEQ         152..160
FT                   /note="DEKEKLLLC -> MRRKNYYYV (in isoform 2, isoform 3 and
FT                   isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14621295,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_035642"
FT   VAR_SEQ         2569..3582
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_020464"
FT   VAR_SEQ         3124..3206
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14621295"
FT                   /id="VSP_020465"
FT   CONFLICT        2163
FT                   /note="K -> Q (in Ref. 2; BAE25365)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3582 AA;  408214 MW;  27BA0032ED7E06A2 CRC64;
     MCENCADLVE VLNEISDIEG GDGLQLRKEH TLKIFAYINS WTQRQCLCCF KEYKHLEIFN
     QVVCALINLV IAQVQVLRDQ LCKHCTTINI DSTWQDESNQ AEEPLSIDRE CNEGNTERQK
     SIEKKSNSTR TCNLTEEESS KSSDPFSLWN TDEKEKLLLC VAKIFQIQFP LYTAYKHNTH
     PTIEDISTQE SNILGAFCDM NDVEVPLHLL RYVCLFCGKN GLSLMKDCFE YGTPETLPFL
     IAHAFITVVS NIRIWLHIPA VMQHIIPFRT YVIRYLCKLS DQELRQSAAR NMADLMWSTV
     KEPLDTTLCF DKESLDLAFK YFMSPTLTMR LAGLSQITNQ LHTFNDVCNN ESLVSDTETS
     IAKELADWLI SNNVVEHIFG PNLHIEIIKQ CQVILNFLAA EGRLSTQHID CIWAAAQLKH
     CSRYIHDLFP SLIKNLDPVP LRHLLNLVSA LEPGVHTEQT LYLASMLIKA LWNNALAAKA
     QLSKQSSFAS LLNTNMPIGN KKEEEELRRA APSPWSPAAS PQSSDNSDTH QSGASDIEMD
     EQLINRNKHV QQRLSDTEES MQGSSDETAN SGEDGSSGPG SSSGHSDGSS NEVNSSHASQ
     SAGSPGSEVQ SEDIADIEAL KEEEEEEEEE EEEEEEEDDE EEEDEEEDDD DDDDHGHNPA
     KNTCGTELRN RKLENPAGIC LGESQGTSER NGTNSGTGKD LVFNTEPLPS VDNRIRMLDA
     CAHSEDPEHG ISGEVSSAHL AQGSQEACIT RSGDFLGETI GNELFNCRQF IGPQHHHHHH
     HHHHHHHHHH HHHHHHHDGH MVDDMLSADD VSCSSSQVSA KSEKNMADFD GEESGCEEEL
     VQINSHAELT SHLQQHLPNL ASIYHEHLSQ GPAVHKHQFS SNAVTDINLD NVCKKGNTLL
     WDIVQDDDAI NLSEGLINEA EKLLCSLVCW FTDRQIRMRF IEGCLENLGN NRSVVISLRL
     LPKLFGTFQQ FGSSYDTHWI TMWAEKELNM MKLFFDNLVY YIQGIREGRQ KHALYSHSAE
     VQVRLQFLTC VFSTLGSPDH FRLSLEQVDI LWHCLVEDSE CYDDALHWFL NQVRSKDQHA
     MGMETYKHLF LEKMPQLKPE TISMTGLNLF QHLCNLARLA TSAYDGGSNS ELCGMDQFWG
     IALRAQSGDV SRAAIQYINS YYINGKTGLE KEQEFISKCM ESLMIASSSL EQESHSSLTV
     IERGLLMLKT HLEAFRRRFA YHLRQWQIEG TGISSHLKAL SDKQSLPLRV VCQPAGLPDK
     MTIEMYPSDQ VADLRAEVTH WYENLQKEQI NQQAQLQEFG QSSRKGEFPG GLMGPVRMIS
     SGHELTTDYD EKALHELGFK DMQMVFVSLG APRRERKGEG VQLPASCLPP PQKDNIPMLL
     LLQEPHLTTL FDLLEMLASF KPPSGKVAVD DSESLKCEEL HLHAENLSRR VWELLMLLPT
     CPNMLTAFQN VSDEQSNDGL NWKELLKIKS AHKLLYALEI IEALGKPNRR IRRESTGSYS
     DLYPDSDDSS EDQVENSKNS WTCKFVAAGG LQQLLEIFNS AILEPKEQES WTVWQLDCLA
     CLLKLICQFA VDPSDLDLAY HDVFAWSGIA ESHRKRTWPG KSRKAAGDHA KSLHIPRLTE
     VFLVLVQGTS LIQRLMSVAY TYDNLAPRVL KAQSDHRSRH EVSHYSMWLL VSWAHCCSLV
     KSSLADSDHL QDWLKQLTLL IPETAVRHES CNGLYKLSLS GLDGGDSIHR SFLLLAASTL
     LKFLPDAQAL KPPRIDDYEE EPLLKPGCKE YFWLLCKLVD NIHIKDASQT TLLDLDALAR
     HLADCIRSRE ILDHLDGSIE DDGLSGLLRL ATSVIKHKPP FKFSREGQEF LRDIFNLLFL
     LPSLKDRRQP KCKSHSCRAA AYDLLVEMVK GSVENYRLIH NWVMAQHMQS HAPYKWDYWP
     HEDVRAECRF VGLTNLGATC YLASTIQQLY MIPEARQAVF TAKYSEDMKH KTTLLELQKM
     FTYLMESECK AYNPRPFCKT YTMDKQPLNT GEQKDMTEFF TDLITKVEEM SPELKNTVKS
     LFGGVITNNV VSLDCEHVSQ TAEEFYTVRC QVADMKNIYE SLDEVTIKDT LEGDNMYTCS
     HCGKKVRAEK RACFKKLPRI LSFNTMRYTF NMVTMMKEKV NTHFSFPLRL DMTPYTEDFL
     MGKSDRKEGF KDVGDRSKDT ESYEYDLIGV TVHTGTADGG HYYSFIRDIV NPHAYKNNKW
     YLFNDAEVKP FDSAQLASEC FGGEMTTKTY DSVTDKFMDF SFEKTHSAYM LFYKRMEPEE
     ENGREYKFDV SSELLEWIWH DNMQFLQDKN IFEHTYFGFM WQLCSCIPST LPDPKAVSLM
     TAKLSTSFVL ETFIHSKEKP TMLQWIELLT KQFNNSQAAC EWFLDRMADD DWWPMQILIK
     CPNQIVRQMF QRLCIHVIQR LRPVHAHLYL QPGMEDGSDD MDASVEDIGG RSCVTRFVRT
     LLLIMEHGVK PHSKHLTEYF AFLYEFAKMG EEESQFLLSL QAISTMVHFY MGTKGPENPQ
     VEVLSEEEGE EEEEEEDILS LAEEKYRPAA LEKMIALVAL LVEQSRSERH LTLSQTDMAA
     LTGGKGFPFL FQHIRDGINI RQTCNLIFSL CRYNNRLAEH IVSMLFTSIA KLTPEAANPF
     FKLLTMLMEF AGGPPGMPPF ASYILQRIWE VIEYNPSQCL DWLAVQTPRN KLAHSWVLQN
     MENWVERFLL AHNYPRVRTS AAYLLVSLIP SNSFRQMFRS TRSLHIPTRD LPLSPDTTVV
     LHQVYNVLLG LLSRAKLYVD AAVHGTTKLV PYLSFMTYCL ISKTEKLMFS TYFMDLWNLF
     QPKLSEPAIA TNHNKQALLS FWYNVCADCP ENIRLIVQNP VVTKNIAFNY ILADHDDQDV
     VLFNRGMLPA YYGILRLCCE QSPAFTRQLA SHQNIQWAFK NLTPHASQYP GAVEELFNLM
     QLFIAQRPDM REEELEDIKQ FKKTTISCYL RCLDGRSCWT TLISAFRILL ESDEDRLLVV
     FNRGLILMTE SFNTLHMMYH EATACHVTGD LVELLSIFLS VLKSTRPYLQ RKDVKQALIQ
     WQERIEFAHK LLTLLNSYSP PELRNACIDV LKELVLLSPH DFLHTLVPFL QHNHCTYHHS
     NIPMSLGPYF PCRENIKLIG GKSNIRPPRP ELNMCLLPTM VETSKGKDDV YDRMLLDYFF
     SYHQFIHLLC RVAINCEKFT ETLVKLSVLV AYEGLPLHLA LFPKLWTELC QTQSAMSKNC
     IKLLCEDPVF AEYIKCILMD ERTFLNNNIV YTFMTHFLLK VQSQVFSEAN CASLISTLIT
     NLINQYQNLQ SDFTNRVEIS KASAALNGDL RALALLLSVH TPKQLNPALI PTLQELLNKC
     RTCLQQRNSL QEQEAKERKT KDDEGATPVK RRRVSSDEEH TVDSCIGDIK TETREVLTPT
     STSDNETRDS SIIDPGTEQD LPSPENSSVK EYRMEGPSSF SEDGSHIRSQ HAEEQSNNGR
     FDDCKEFKDH CSKDTTLAED ESEFPSTSIS AVLSDLADLR SCDGQALSSQ DPEAAVSLSC
     GHSRGLISHM QQHDILDTLC RTIESTIHVV TRISGKGNQA AS
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