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   27-MAR-2024, entry version 178.
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,
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).
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 (By similarity). Deubiquitinates PDPK1 (By
CC       similarity). Deubiquitinates TRIM21 (By similarity). Deubiquitinates
CC       receptor ADORA2A which increases the amount of functional receptor at
CC       the cell surface (By similarity). Deubiquitinates HAS2 (By similarity).
CC       Deubiquitinates RHEB in response to EGF signaling, promoting mTORC1
CC       signaling (By similarity). May regulate mRNA splicing through
CC       deubiquitination of the U4 spliceosomal protein PRPF3 (By similarity).
CC       This may prevent its recognition by the U5 component PRPF8 thereby
CC       destabilizing interactions within the U4/U6.U5 snRNP (By similarity).
CC       May also play a role in the regulation of quality control in the ER (By
CC       similarity). {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: Phosphorylated at Ser-445 by PKB/AKT1 in response to EGF stimulus,
CC       promoting its ability deubiquitinate RHEB.
CC       {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   IntAct; P35123; 1.
DR   STRING; 10090.ENSMUSP00000035237; -.
DR   MEROPS; C19.010; -.
DR   GlyGen; P35123; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P35123; -.
DR   PhosphoSitePlus; P35123; -.
DR   SwissPalm; P35123; -.
DR   EPD; P35123; -.
DR   jPOST; P35123; -.
DR   MaxQB; P35123; -.
DR   PaxDb; 10090-ENSMUSP00000035237; -.
DR   PeptideAtlas; P35123; -.
DR   ProteomicsDB; 298366; -.
DR   Pumba; P35123; -.
DR   Antibodypedia; 13556; 402 antibodies from 32 providers.
DR   DNASU; 22258; -.
DR   Ensembl; ENSMUST00000035237.12; ENSMUSP00000035237.7; ENSMUSG00000032612.15.
DR   GeneID; 22258; -.
DR   KEGG; mmu:22258; -.
DR   UCSC; uc009rph.2; mouse.
DR   AGR; MGI:98905; -.
DR   CTD; 7375; -.
DR   MGI; MGI:98905; Usp4.
DR   VEuPathDB; HostDB:ENSMUSG00000032612; -.
DR   eggNOG; KOG1870; Eukaryota.
DR   GeneTree; ENSGT00940000156645; -.
DR   InParanoid; P35123; -.
DR   OMA; ALKWHHD; -.
DR   OrthoDB; 5474185at2759; -.
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 NF-kappa-B signaling pathway.
DR   Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR   BioGRID-ORCS; 22258; 0 hits in 77 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 152 other cell types or tissues.
DR   ExpressionAtlas; P35123; baseline and differential.
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:1904263; P:positive regulation of TORC1 signaling; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR   GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; ISS:UniProtKB.
DR   CDD; cd02674; Peptidase_C19R; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 3.30.2230.10; DUSP-like; 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   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF45; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 4; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF14836; Ubiquitin_3; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   PROSITE; PS51283; DUSP; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   Genevisible; P35123; MM.
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         445
FT                   /note="Phosphoserine"
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
//