UBP34_MOUSE
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 03-AUG-2022, entry version 132.
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.ENSMUSP00000120747; -.
DR MEROPS; C19.067; -.
DR iPTMnet; Q6ZQ93; -.
DR PhosphoSitePlus; Q6ZQ93; -.
DR EPD; Q6ZQ93; -.
DR jPOST; Q6ZQ93; -.
DR MaxQB; Q6ZQ93; -.
DR PaxDb; Q6ZQ93; -.
DR PeptideAtlas; Q6ZQ93; -.
DR PRIDE; Q6ZQ93; -.
DR ProteomicsDB; 298417; -. [Q6ZQ93-1]
DR ProteomicsDB; 298418; -. [Q6ZQ93-2]
DR ProteomicsDB; 298419; -. [Q6ZQ93-3]
DR ProteomicsDB; 298420; -. [Q6ZQ93-4]
DR Antibodypedia; 7689; 100 antibodies from 23 providers.
DR Ensembl; ENSMUST00000180046; ENSMUSP00000137430; ENSMUSG00000056342. [Q6ZQ93-1]
DR GeneID; 17847; -.
DR KEGG; mmu:17847; -.
DR UCSC; uc029rkw.1; mouse. [Q6ZQ93-1]
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; LETRHNT; -.
DR OrthoDB; 625455at2759; -.
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 73 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 255 other tissues.
DR ExpressionAtlas; Q6ZQ93; baseline and differential.
DR Genevisible; Q6ZQ93; 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; 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:0016579; P:protein deubiquitination; ISO:MGI.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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 Pfam; PF12030; DUF3517; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF54001; SSF54001; 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;
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
