UBP4_MOUSE
ID UBP4_MOUSE Reviewed; 962 AA.
AC P35123; O54704; Q8BTL9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 4;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q13107};
DE AltName: Full=Deubiquitinating enzyme 4;
DE AltName: Full=Ubiquitin thioesterase 4;
DE AltName: Full=Ubiquitin-specific-processing protease 4;
DE AltName: Full=Ubiquitous nuclear protein;
GN Name=Usp4; Synonyms=Unp;
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 PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8336951;
RA Gupta K., Copeland N.G., Gilbert D.J., Jenkins N.A., Gray D.A.;
RT "Unp, a mouse gene related to the tre oncogene.";
RL Oncogene 8:2307-2310(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129; TISSUE=Testis;
RX PubMed=9602026; DOI=10.1016/s0167-4781(98)00035-9;
RA di Fruscio M., Gilchrist C.A., Baker R.T., Gray D.A.;
RT "Genomic structure of Unp, a murine gene encoding a ubiquitin-specific
RT protease.";
RL Biochim. Biophys. Acta 1398:9-17(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Spleen;
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 [4]
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 [5]
RP INTERACTION WITH RB1; RBL1 AND RBL2, AND MUTAGENESIS OF CYS-461.
RX PubMed=11571651; DOI=10.1038/sj.onc.1204823;
RA Blanchette P., Gilchrist C.A., Baker R.T., Gray D.A.;
RT "Association of UNP, a ubiquitin-specific protease, with the pocket
RT proteins pRb, p107 and p130.";
RL Oncogene 20:5533-5537(2001).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, NUCLEAR LOCALIZATION SIGNAL, AND
RP MUTAGENESIS OF 770-GLN--LYS-771.
RX PubMed=15494318; DOI=10.1074/jbc.m401394200;
RA Soboleva T.A., Jans D.A., Johnson-Saliba M., Baker R.T.;
RT "Nuclear-cytoplasmic shuttling of the oncogenic mouse UNP/USP4
RT deubiquitylating enzyme.";
RL J. Biol. Chem. 280:745-752(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675 AND SER-680, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 1-229.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the N-terminal domains of the ubiquitin specific
RT peptidase 4 (USP4).";
RL Submitted (NOV-2009) to the PDB data bank.
CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC from target proteins. Deubiquitinates PDPK1. Deubiquitinates TRIM21.
CC Deubiquitinates receptor ADORA2A which increases the amount of
CC functional receptor at the cell surface. Deubiquitinates HAS2. May
CC regulate mRNA splicing through deubiquitination of the U4 spliceosomal
CC protein PRPF3. This may prevent its recognition by the U5 component
CC PRPF8 thereby destabilizing interactions within the U4/U6.U5 snRNP. May
CC also play a role in the regulation of quality control in the ER.
CC {ECO:0000250|UniProtKB:Q13107}.
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:Q13107};
CC -!- ACTIVITY REGULATION: The completion of the deubiquitinase reaction is
CC mediated by the DUSP and ubiquitin-like 1 domains which promotes the
CC release of ubiquitin from the catalytic site enabling subsequent
CC reactions to occur. {ECO:0000250|UniProtKB:Q13107}.
CC -!- SUBUNIT: Interacts with RB1 (both dephosphorylated and
CC hypophosphorylated forms) (PubMed:11571651). Interacts with RBL1 and
CC RBL2 (PubMed:11571651). Interacts with ADORA2A (via cytoplasmic C-
CC terminus); the interaction is direct. Interacts with SART3; recruits
CC USP4 to its substrate PRPF3 (By similarity).
CC {ECO:0000250|UniProtKB:Q13107, ECO:0000269|PubMed:11571651}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15494318}. Nucleus
CC {ECO:0000269|PubMed:15494318}. Note=Shuttles between the nucleus and
CC cytoplasm. Exported to the cytoplasm in a CRM1-dependent manner and
CC recycled back to the nucleus via the importin alpha/beta heterodimeric
CC import receptor. {ECO:0000269|PubMed:15494318}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney, liver and spleen (at
CC protein level). {ECO:0000269|PubMed:15494318}.
CC -!- DEVELOPMENTAL STAGE: Overexpression leads to oncogenic transformation
CC of NIH 3T3 cells.
CC -!- DOMAIN: The DUSP and ubiquitin-like 1 domains promote ubiquitin release
CC and thus enhance USB4 catalytic activity. However, these domains do not
CC bind ubiquitin. {ECO:0000250|UniProtKB:Q13107}.
CC -!- PTM: Monoubiquitinated by TRIM21. Ubiquitination does not lead to its
CC proteasomal degradation. Autodeubiquitinated.
CC {ECO:0000250|UniProtKB:Q13107}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP4 subfamily.
CC {ECO:0000305}.
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DR EMBL; L00681; AAB82339.1; -; mRNA.
DR EMBL; AF026469; AAC53587.1; -; Genomic_DNA.
DR EMBL; AK089425; BAC40877.1; -; mRNA.
DR EMBL; AK143582; BAE25450.1; -; mRNA.
DR EMBL; AK149964; BAE29198.1; -; mRNA.
DR EMBL; AK169933; BAE41468.1; -; mRNA.
DR EMBL; AK171271; BAE42357.1; -; mRNA.
DR EMBL; CH466560; EDL21282.1; -; Genomic_DNA.
DR CCDS; CCDS23523.1; -.
DR PIR; I58376; I58376.
DR RefSeq; NP_035808.2; NM_011678.2.
DR PDB; 3JYU; X-ray; 2.37 A; A/B=1-229.
DR PDBsum; 3JYU; -.
DR AlphaFoldDB; P35123; -.
DR SMR; P35123; -.
DR BioGRID; 204448; 2.
DR STRING; 10090.ENSMUSP00000035237; -.
DR MEROPS; C19.010; -.
DR iPTMnet; P35123; -.
DR PhosphoSitePlus; P35123; -.
DR SwissPalm; P35123; -.
DR EPD; P35123; -.
DR jPOST; P35123; -.
DR MaxQB; P35123; -.
DR PaxDb; P35123; -.
DR PeptideAtlas; P35123; -.
DR PRIDE; P35123; -.
DR ProteomicsDB; 298366; -.
DR Antibodypedia; 13556; 381 antibodies from 32 providers.
DR DNASU; 22258; -.
DR Ensembl; ENSMUST00000035237; ENSMUSP00000035237; ENSMUSG00000032612.
DR GeneID; 22258; -.
DR KEGG; mmu:22258; -.
DR UCSC; uc009rph.2; mouse.
DR CTD; 7375; -.
DR MGI; MGI:98905; Usp4.
DR VEuPathDB; HostDB:ENSMUSG00000032612; -.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000156645; -.
DR InParanoid; P35123; -.
DR OMA; SGTCNEA; -.
DR OrthoDB; 1283205at2759; -.
DR PhylomeDB; P35123; -.
DR TreeFam; TF106276; -.
DR Reactome; R-MMU-5357786; TNFR1-induced proapoptotic signaling.
DR Reactome; R-MMU-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-MMU-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 22258; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Usp4; mouse.
DR EvolutionaryTrace; P35123; -.
DR PRO; PR:P35123; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P35123; protein.
DR Bgee; ENSMUSG00000032612; Expressed in spermatid and 148 other tissues.
DR ExpressionAtlas; P35123; baseline and differential.
DR Genevisible; P35123; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0031685; F:adenosine receptor binding; ISO:MGI.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.2230.10; -; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028135; Ub_USP-typ.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF143791; SSF143791; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51283; DUSP; 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 3D-structure; Cytoplasm; Hydrolase; Metal-binding; Nucleus; Phosphoprotein;
KW Protease; Proto-oncogene; Reference proteome; Repeat; Thiol protease;
KW Ubl conjugation; Ubl conjugation pathway; Zinc.
FT CHAIN 1..962
FT /note="Ubiquitin carboxyl-terminal hydrolase 4"
FT /id="PRO_0000080622"
FT DOMAIN 11..122
FT /note="DUSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 142..226
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 302..922
FT /note="USP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT DOMAIN 483..571
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255"
FT REGION 27..216
FT /note="Necessary for interaction with SART3"
FT /evidence="ECO:0000250|UniProtKB:Q13107"
FT REGION 220..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..295
FT /note="Required for USP4 activation by providing
FT conformational flexibility between the DUSP and catalytic
FT domains"
FT /evidence="ECO:0000250|UniProtKB:Q13107"
FT REGION 384..386
FT /note="Regulates ubiquitin dissociation"
FT /evidence="ECO:0000250|UniProtKB:Q13107"
FT REGION 405..407
FT /note="Necessary for interaction with RBL2"
FT /evidence="ECO:0000269|PubMed:11571651"
FT REGION 459..463
FT /note="Necessary for interaction with RB1 and RBL2"
FT /evidence="ECO:0000269|PubMed:11571651"
FT REGION 485..774
FT /note="Interacts with DUSP and ubiquitin-like 1 domains and
FT is required for USP4 activation"
FT /evidence="ECO:0000250|UniProtKB:Q13107"
FT REGION 638..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 133..141
FT /note="Nuclear export signal"
FT /evidence="ECO:0000269|PubMed:15494318"
FT MOTIF 766..771
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:15494318"
FT COMPBIAS 221..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 311
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT ACT_SITE 880
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT BINDING 461
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q13107"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q13107"
FT BINDING 798
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q13107"
FT BINDING 801
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q13107"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2GUZ1"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 461
FT /note="C->Q: Reduces the interaction with RB1."
FT /evidence="ECO:0000269|PubMed:11571651"
FT MUTAGEN 770..771
FT /note="KK->NS: Reduces nuclear localization."
FT /evidence="ECO:0000269|PubMed:15494318"
FT CONFLICT 123..124
FT /note="EH -> DD (in Ref. 1; AAB82339 and 2; AAC53587)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="P -> A (in Ref. 1; AAB82339)"
FT /evidence="ECO:0000305"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:3JYU"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:3JYU"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:3JYU"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:3JYU"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3JYU"
FT TURN 56..60
FT /evidence="ECO:0007829|PDB:3JYU"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3JYU"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3JYU"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3JYU"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:3JYU"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:3JYU"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:3JYU"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:3JYU"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:3JYU"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3JYU"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:3JYU"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:3JYU"
FT STRAND 147..156
FT /evidence="ECO:0007829|PDB:3JYU"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:3JYU"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3JYU"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:3JYU"
FT TURN 202..206
FT /evidence="ECO:0007829|PDB:3JYU"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:3JYU"
SQ SEQUENCE 962 AA; 108343 MW; 95F95BE86186DA52 CRC64;
MAEGRGSRER PDVETQKTEL GALMGTTLQR GAQWYLIDSR WFKQWKKYVG FDSWDMYNVG
EHNLFPGPID NSGLFSDPES QTLKEHLIDE LDYVLVPAEA WNKLLNWYGC VEGQQPIVRK
VVEHGLFVKH CKVEVYLLEL KLCENSDPTN VLSCHFSKAD TIATIEKEMR KLFNIPAERE
TRLWNKYMSN TYEQLSKLDN TIQDAGLYQG QVLVIEPQNE DGTWPRQSLQ SKSSTAPSRN
FTTSSKPSAS PYCSVSASLI ANGDSTNSSG MHSSGVSRGG SGFSASYNCQ EPPSPHIQPG
LCGLGNLGNT CFMNSALQCL SNTAPLTEYF LKDEYEAEIN RDNPLGMKGE IAEAYAELIK
QMWSGRDTHV APRMFKTQVG RFAPQFSGYQ QQDSQELLAF ILDGLHEDLN RVKKKPYLEP
KDANGRPDAV VAKEAWENHR LRNDSVIVDT FHGLFKSTLV CPECAKVSVT FDPFCYLTLP
LPLKKDRIME VFLVPADPQC RPIQYRVTVP LMGAISDLCE ALSKLSGIAA ENMVVTDVYN
HRFHKIFQMD EGLSHITPRD DIFVYEVCNT SMDGSECITL PVYFREKKSR PSSASSGAVL
YGQPLLVSVP KHKLTLESLY QAVCDRISRY IKQPLPDEFL SSPLEPGACN GSRSSYEGDE
EEEMDHQEEG KEQLSEVEGS GEDDQGDDHS ESAQKVKGQP RHKRLFTFSL VNSCGTADIN
SLATDGKLLK LNSRSTLAID WDSETRSLYF DEQESEACEK HLSMSQPQKK KKAAVALREC
IELFTTMETL GEHDPWYCPT CKKHQQATKK FDLWSLPKIL VVHLKRFSYN RYWRDKLDTV
VEFPVRALNM SEFVCDRSAR PYVYDLIAVS NHYGAMGVGH YTAYAKNRLN GKWYYFDDSS
VSLASEDQIV TKAAYVLFYQ RRDDECSSTS SLGSFPGSDG GVKLSSSHQG MGDEEAYNMD
TN
