OTU7B_HUMAN
ID OTU7B_HUMAN Reviewed; 843 AA.
AC Q6GQQ9; B7Z643; D3DUZ8; Q5SZ60; Q8WWA7; Q9NQ53; Q9UFF4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=OTU domain-containing protein 7B;
DE EC=3.4.19.12 {ECO:0000269|PubMed:12682062, ECO:0000269|PubMed:14748687, ECO:0000269|PubMed:22179831, ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:26903241, ECO:0000269|PubMed:27732584};
DE AltName: Full=Cellular zinc finger anti-NF-kappa-B protein {ECO:0000303|PubMed:11463333};
DE Short=Cezanne {ECO:0000303|PubMed:11463333, ECO:0000303|PubMed:18178551, ECO:0000303|PubMed:27732584};
DE AltName: Full=Zinc finger A20 domain-containing protein 1;
DE AltName: Full=Zinc finger protein Cezanne {ECO:0000305};
GN Name=OTUD7B; Synonyms=ZA20D1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH TRAF6.
RC TISSUE=Lymphocyte;
RX PubMed=11463333; DOI=10.1042/0264-6021:3570617;
RA Evans P.C., Taylor E.R., Coadwell J., Heyninck K., Beyaert R.,
RA Kilshaw P.J.;
RT "Isolation and characterization of two novel A20-like proteins.";
RL Biochem. J. 357:617-623(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Prostate;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 437-843.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP CYS-194.
RX PubMed=12682062; DOI=10.1074/jbc.m301863200;
RA Evans P.C., Smith T.S., Lai M.-J., Williams M.G., Burke D.F., Heyninck K.,
RA Kreike M.M., Beyaert R., Blundell T.L., Kilshaw P.J.;
RT "A novel type of deubiquitinating enzyme.";
RL J. Biol. Chem. 278:23180-23186(2003).
RN [8]
RP MUTAGENESIS OF CYS-194, AND CATALYTIC ACTIVITY.
RX PubMed=14748687; DOI=10.1042/bj20031377;
RA Evans P.C., Ovaa H., Hamon M., Kilshaw P.J., Hamm S., Bauer S.,
RA Ploegh H.L., Smith T.S.;
RT "Zinc-finger protein A20, a regulator of inflammation and cell survival,
RT has de-ubiquitinating activity.";
RL Biochem. J. 378:727-734(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP FUNCTION, AND INDUCTION.
RX PubMed=18178551; DOI=10.1074/jbc.m708690200;
RA Enesa K., Zakkar M., Chaudhury H., Luong le A., Rawlinson L., Mason J.C.,
RA Haskard D.O., Dean J.L., Evans P.C.;
RT "NF-kappaB suppression by the deubiquitinating enzyme Cezanne: a novel
RT negative feedback loop in pro-inflammatory signaling.";
RL J. Biol. Chem. 283:7036-7045(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP FUNCTION.
RX PubMed=20622874; DOI=10.1038/nsmb.1873;
RA Bremm A., Freund S.M., Komander D.;
RT "Lys11-linked ubiquitin chains adopt compact conformations and are
RT preferentially hydrolyzed by the deubiquitinase Cezanne.";
RL Nat. Struct. Mol. Biol. 17:939-947(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP ACTIVITY REGULATION, AND INTERACTION WITH PARK7.
RX PubMed=21097510; DOI=10.1074/jbc.m110.147371;
RA McNally R.S., Davis B.K., Clements C.M., Accavitti-Loper M.A., Mak T.W.,
RA Ting J.P.;
RT "DJ-1 enhances cell survival through the binding of cezanne, a negative
RT regulator of NF-{kappa}B.";
RL J. Biol. Chem. 286:4098-4106(2011).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP SUBCELLULAR LOCATION.
RX PubMed=21888622; DOI=10.1042/bj20111300;
RA Garcia-Santisteban I., Banuelos S., Rodriguez J.A.;
RT "A global survey of CRM1-dependent nuclear export sequences in the human
RT deubiquitinase family.";
RL Biochem. J. 441:209-217(2012).
RN [20]
RP FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION, INTERACTION WITH EGFR; ITCH
RP AND NEDD4, AND MUTAGENESIS OF CYS-194; PHE-809 AND TYR-810.
RX PubMed=22179831; DOI=10.1038/onc.2011.587;
RA Pareja F., Ferraro D.A., Rubin C., Cohen-Dvashi H., Zhang F., Aulmann S.,
RA Ben-Chetrit N., Pines G., Navon R., Crosetto N., Kostler W., Carvalho S.,
RA Lavi S., Schmitt F., Dikic I., Yakhini Z., Sinn P., Mills G.B., Yarden Y.;
RT "Deubiquitination of EGFR by Cezanne-1 contributes to cancer progression.";
RL Oncogene 31:4599-4608(2012).
RN [21]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23827681; DOI=10.1016/j.cell.2013.05.046;
RA Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M.,
RA Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M.,
RA Ovaa H., Komander D.;
RT "OTU deubiquitinases reveal mechanisms of linkage specificity and enable
RT ubiquitin chain restriction analysis.";
RL Cell 154:169-184(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100 AND SER-467, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP FUNCTION, INTERACTION WITH ZAP70, MUTAGENESIS OF CYS-194 AND HIS-358, AND
RP CATALYTIC ACTIVITY.
RX PubMed=26903241; DOI=10.1084/jem.20151426;
RA Hu H., Wang H., Xiao Y., Jin J., Chang J.H., Zou Q., Xie X., Cheng X.,
RA Sun S.C.;
RT "Otud7b facilitates T cell activation and inflammatory responses by
RT regulating Zap70 ubiquitination.";
RL J. Exp. Med. 213:399-414(2016).
RN [25] {ECO:0007744|PDB:5LRU, ECO:0007744|PDB:5LRV, ECO:0007744|PDB:5LRW}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 129-438 OF APOPROTEIN AND IN
RP COMPLEXES WITH UBIQUITIN, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP FUNCTION, ACTIVE SITE, DOMAIN, AND MUTAGENESIS OF 155-LEU-ILE-156; GLU-157;
RP ASN-193; CYS-194; HIS-197; ASP-210; GLU-295 AND HIS-358.
RX PubMed=27732584; DOI=10.1038/nature19836;
RA Mevissen T.E., Kulathu Y., Mulder M.P., Geurink P.P., Maslen S.L.,
RA Gersch M., Elliott P.R., Burke J.E., van Tol B.D., Akutsu M., El Oualid F.,
RA Kawasaki M., Freund S.M., Ovaa H., Komander D.;
RT "Molecular basis of Lys11-polyubiquitin specificity in the deubiquitinase
RT Cezanne.";
RL Nature 538:402-405(2016).
CC -!- FUNCTION: Negative regulator of the non-canonical NF-kappa-B pathway
CC that acts by mediating deubiquitination of TRAF3, an inhibitor of the
CC NF-kappa-B pathway, thereby acting as a negative regulator of B-cell
CC responses. In response to non-canonical NF-kappa-B stimuli,
CC deubiquitinates 'Lys-48'-linked polyubiquitin chains of TRAF3,
CC preventing TRAF3 proteolysis and over-activation of non-canonical NF-
CC kappa-B. Negatively regulates mucosal immunity against infections (By
CC similarity). Deubiquitinates ZAP70, and thereby regulates T cell
CC receptor (TCR) signaling that leads to the activation of NF-kappa-B
CC (PubMed:26903241). Plays a role in T cell homeostasis and is required
CC for normal T cell responses, including production of IFNG and IL2 (By
CC similarity). Mediates deubiquitination of EGFR (PubMed:22179831). Has
CC deubiquitinating activity toward 'Lys-11', 'Lys-48' and 'Lys-63'-linked
CC polyubiquitin chains (PubMed:27732584). Has a much higher catalytic
CC rate with 'Lys-11'-linked polyubiquitin chains (in vitro); however the
CC physiological significance of these data are unsure (PubMed:27732584).
CC Hydrolyzes both linear and branched forms of polyubiquitin.
CC {ECO:0000250|UniProtKB:B2RUR8, ECO:0000269|PubMed:11463333,
CC ECO:0000269|PubMed:12682062, ECO:0000269|PubMed:18178551,
CC ECO:0000269|PubMed:20622874, ECO:0000269|PubMed:22179831,
CC ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:27732584}.
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:0000269|PubMed:12682062,
CC ECO:0000269|PubMed:14748687, ECO:0000269|PubMed:22179831,
CC ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:26903241,
CC ECO:0000269|PubMed:27732584};
CC -!- ACTIVITY REGULATION: Deubiquitinase activity is inhibited following
CC interaction with PARK7. {ECO:0000269|PubMed:21097510}.
CC -!- SUBUNIT: Interacts with ZAP70 in activated T cells, but not in resting
CC T cells (PubMed:26903241). Interacts with TRAF3 (By similarity).
CC Interacts with TRAF6 (PubMed:11463333). Interacts with PARK7, leading
CC to inhibit deubiquitinase activity (PubMed:21097510). Interacts with
CC EGFR, ITCH and NEDD4 (PubMed:22179831). {ECO:0000250|UniProtKB:B2RUR8,
CC ECO:0000269|PubMed:11463333, ECO:0000269|PubMed:21097510,
CC ECO:0000269|PubMed:22179831, ECO:0000269|PubMed:26903241}.
CC -!- INTERACTION:
CC Q6GQQ9; Q8IVM0: CCDC50; NbExp=5; IntAct=EBI-527784, EBI-723996;
CC Q6GQQ9; Q9H305: CDIP1; NbExp=3; IntAct=EBI-527784, EBI-2876678;
CC Q6GQQ9; Q15038: DAZAP2; NbExp=3; IntAct=EBI-527784, EBI-724310;
CC Q6GQQ9; Q7L775: EPM2AIP1; NbExp=3; IntAct=EBI-527784, EBI-6255981;
CC Q6GQQ9; Q96LI6: HSFY2; NbExp=3; IntAct=EBI-527784, EBI-3957665;
CC Q6GQQ9; P46934: NEDD4; NbExp=2; IntAct=EBI-527784, EBI-726944;
CC Q6GQQ9; Q96BN8: OTULIN; NbExp=3; IntAct=EBI-527784, EBI-750730;
CC Q6GQQ9; Q99497: PARK7; NbExp=3; IntAct=EBI-527784, EBI-1164361;
CC Q6GQQ9; Q92569: PIK3R3; NbExp=3; IntAct=EBI-527784, EBI-79893;
CC Q6GQQ9; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-527784, EBI-12000762;
CC Q6GQQ9; P20618: PSMB1; NbExp=3; IntAct=EBI-527784, EBI-372273;
CC Q6GQQ9; Q8N0X7: SPART; NbExp=3; IntAct=EBI-527784, EBI-2643803;
CC Q6GQQ9-2; P01023: A2M; NbExp=3; IntAct=EBI-25830200, EBI-640741;
CC Q6GQQ9-2; P02768-3: ALB; NbExp=3; IntAct=EBI-25830200, EBI-25830928;
CC Q6GQQ9-2; P54253: ATXN1; NbExp=6; IntAct=EBI-25830200, EBI-930964;
CC Q6GQQ9-2; P46379-2: BAG6; NbExp=3; IntAct=EBI-25830200, EBI-10988864;
CC Q6GQQ9-2; P55212: CASP6; NbExp=3; IntAct=EBI-25830200, EBI-718729;
CC Q6GQQ9-2; P09172: DBH; NbExp=3; IntAct=EBI-25830200, EBI-8589586;
CC Q6GQQ9-2; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-25830200, EBI-25840379;
CC Q6GQQ9-2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-25830200, EBI-10976677;
CC Q6GQQ9-2; O14645: DNALI1; NbExp=3; IntAct=EBI-25830200, EBI-395638;
CC Q6GQQ9-2; P41091: EIF2S3; NbExp=3; IntAct=EBI-25830200, EBI-1054228;
CC Q6GQQ9-2; O75460-2: ERN1; NbExp=3; IntAct=EBI-25830200, EBI-25852368;
CC Q6GQQ9-2; P22607: FGFR3; NbExp=3; IntAct=EBI-25830200, EBI-348399;
CC Q6GQQ9-2; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-25830200, EBI-10226858;
CC Q6GQQ9-2; P14136: GFAP; NbExp=3; IntAct=EBI-25830200, EBI-744302;
CC Q6GQQ9-2; Q14957: GRIN2C; NbExp=3; IntAct=EBI-25830200, EBI-8285963;
CC Q6GQQ9-2; P06396: GSN; NbExp=3; IntAct=EBI-25830200, EBI-351506;
CC Q6GQQ9-2; P54652: HSPA2; NbExp=3; IntAct=EBI-25830200, EBI-356991;
CC Q6GQQ9-2; P04792: HSPB1; NbExp=3; IntAct=EBI-25830200, EBI-352682;
CC Q6GQQ9-2; O43464: HTRA2; NbExp=3; IntAct=EBI-25830200, EBI-517086;
CC Q6GQQ9-2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-25830200, EBI-1055254;
CC Q6GQQ9-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-25830200, EBI-10975473;
CC Q6GQQ9-2; O14901: KLF11; NbExp=3; IntAct=EBI-25830200, EBI-948266;
CC Q6GQQ9-2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-25830200, EBI-21591415;
CC Q6GQQ9-2; P27361: MAPK3; NbExp=3; IntAct=EBI-25830200, EBI-73995;
CC Q6GQQ9-2; P51608: MECP2; NbExp=3; IntAct=EBI-25830200, EBI-1189067;
CC Q6GQQ9-2; P19404: NDUFV2; NbExp=3; IntAct=EBI-25830200, EBI-713665;
CC Q6GQQ9-2; P35240-4: NF2; NbExp=3; IntAct=EBI-25830200, EBI-1014514;
CC Q6GQQ9-2; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-25830200, EBI-2811583;
CC Q6GQQ9-2; O14832: PHYH; NbExp=3; IntAct=EBI-25830200, EBI-721853;
CC Q6GQQ9-2; D3DTS7: PMP22; NbExp=3; IntAct=EBI-25830200, EBI-25882629;
CC Q6GQQ9-2; O60260-5: PRKN; NbExp=3; IntAct=EBI-25830200, EBI-21251460;
CC Q6GQQ9-2; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-25830200, EBI-5280197;
CC Q6GQQ9-2; P60891: PRPS1; NbExp=3; IntAct=EBI-25830200, EBI-749195;
CC Q6GQQ9-2; P62826: RAN; NbExp=3; IntAct=EBI-25830200, EBI-286642;
CC Q6GQQ9-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-25830200, EBI-396669;
CC Q6GQQ9-2; P37840: SNCA; NbExp=3; IntAct=EBI-25830200, EBI-985879;
CC Q6GQQ9-2; P00441: SOD1; NbExp=3; IntAct=EBI-25830200, EBI-990792;
CC Q6GQQ9-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25830200, EBI-5235340;
CC Q6GQQ9-2; Q13148: TARDBP; NbExp=6; IntAct=EBI-25830200, EBI-372899;
CC Q6GQQ9-2; Q86WV8: TSC1; NbExp=3; IntAct=EBI-25830200, EBI-12806590;
CC Q6GQQ9-2; P02766: TTR; NbExp=3; IntAct=EBI-25830200, EBI-711909;
CC Q6GQQ9-2; P0CG47: UBB; NbExp=3; IntAct=EBI-25830200, EBI-413034;
CC Q6GQQ9-2; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-25830200, EBI-741480;
CC Q6GQQ9-2; O76024: WFS1; NbExp=3; IntAct=EBI-25830200, EBI-720609;
CC Q6GQQ9-2; Q9Y649; NbExp=3; IntAct=EBI-25830200, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11463333,
CC ECO:0000269|PubMed:21888622}. Nucleus {ECO:0000269|PubMed:21888622}.
CC Note=Shuttles be cytoplasm and the nucleus in a XPO1/CRM1-dependent
CC manner. {ECO:0000269|PubMed:21888622}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6GQQ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6GQQ9-2; Sequence=VSP_046015;
CC -!- TISSUE SPECIFICITY: Widely expressed. Abundant in kidney, heart and
CC fetal liver. Expressed differentially among B-cells at distinct
CC developmental stages. Higher expression seen in primary immature B-
CC cells as compared to the mature cells. {ECO:0000269|PubMed:11463333,
CC ECO:0000269|PubMed:12682062}.
CC -!- INDUCTION: By TNF-alpha. {ECO:0000269|PubMed:18178551}.
CC -!- DOMAIN: The protein undergoes a significant conformation change upon
CC binding to ubiquitinated substrates. The loop that precedes the active
CC site is in an autoinhibitory conformation in the apoprotein. Ubiquitin
CC binding leads to a conformation change; the loop is stabilized in a
CC catalytically competent conformation with the result that the active
CC site Cys can form the reaction state intermediate.
CC {ECO:0000269|PubMed:27732584}.
CC -!- PTM: Phosphorylated by EGFR. {ECO:0000269|PubMed:22179831}.
CC -!- SIMILARITY: Belongs to the peptidase C64 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB97494.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ293573; CAB97494.1; ALT_INIT; mRNA.
DR EMBL; AK299790; BAH13129.1; -; mRNA.
DR EMBL; AL590487; CAI12651.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53586.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53587.1; -; Genomic_DNA.
DR EMBL; BC020622; AAH20622.1; -; mRNA.
DR EMBL; BC072681; AAH72681.1; -; mRNA.
DR EMBL; AL122102; CAB59268.1; -; mRNA.
DR CCDS; CCDS72903.1; -. [Q6GQQ9-1]
DR PIR; T34535; T34535.
DR RefSeq; NP_064590.2; NM_020205.3. [Q6GQQ9-1]
DR PDB; 5LRU; X-ray; 2.20 A; A=129-438.
DR PDB; 5LRV; X-ray; 2.80 A; A=129-438.
DR PDB; 5LRW; X-ray; 2.00 A; A/C=129-266, A/C=292-438.
DR PDBsum; 5LRU; -.
DR PDBsum; 5LRV; -.
DR PDBsum; 5LRW; -.
DR AlphaFoldDB; Q6GQQ9; -.
DR SMR; Q6GQQ9; -.
DR BioGRID; 121281; 58.
DR DIP; DIP-33805N; -.
DR IntAct; Q6GQQ9; 72.
DR STRING; 9606.ENSP00000462729; -.
DR BindingDB; Q6GQQ9; -.
DR ChEMBL; CHEMBL4630838; -.
DR MEROPS; C64.001; -.
DR GlyGen; Q6GQQ9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6GQQ9; -.
DR PhosphoSitePlus; Q6GQQ9; -.
DR BioMuta; OTUD7B; -.
DR DMDM; 51701318; -.
DR EPD; Q6GQQ9; -.
DR jPOST; Q6GQQ9; -.
DR MassIVE; Q6GQQ9; -.
DR MaxQB; Q6GQQ9; -.
DR PaxDb; Q6GQQ9; -.
DR PeptideAtlas; Q6GQQ9; -.
DR PRIDE; Q6GQQ9; -.
DR ProteomicsDB; 66318; -. [Q6GQQ9-1]
DR Antibodypedia; 72463; 239 antibodies from 30 providers.
DR DNASU; 56957; -.
DR Ensembl; ENST00000581312.6; ENSP00000462729.1; ENSG00000264522.6. [Q6GQQ9-1]
DR GeneID; 56957; -.
DR KEGG; hsa:56957; -.
DR MANE-Select; ENST00000581312.6; ENSP00000462729.1; NM_020205.4; NP_064590.2.
DR UCSC; uc001etn.5; human. [Q6GQQ9-1]
DR CTD; 56957; -.
DR DisGeNET; 56957; -.
DR GeneCards; OTUD7B; -.
DR HGNC; HGNC:16683; OTUD7B.
DR HPA; ENSG00000264522; Tissue enhanced (brain).
DR MIM; 611748; gene.
DR neXtProt; NX_Q6GQQ9; -.
DR OpenTargets; ENSG00000264522; -.
DR PharmGKB; PA134873802; -.
DR VEuPathDB; HostDB:ENSG00000264522; -.
DR eggNOG; KOG4345; Eukaryota.
DR GeneTree; ENSGT00940000159172; -.
DR HOGENOM; CLU_013263_0_0_1; -.
DR InParanoid; Q6GQQ9; -.
DR OMA; LSIMRIT; -.
DR OrthoDB; 728724at2759; -.
DR PhylomeDB; Q6GQQ9; -.
DR TreeFam; TF323312; -.
DR PathwayCommons; Q6GQQ9; -.
DR Reactome; R-HSA-5357786; TNFR1-induced proapoptotic signaling.
DR Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
DR SignaLink; Q6GQQ9; -.
DR SIGNOR; Q6GQQ9; -.
DR BioGRID-ORCS; 56957; 16 hits in 1116 CRISPR screens.
DR ChiTaRS; OTUD7B; human.
DR GeneWiki; OTUD7B; -.
DR GenomeRNAi; 56957; -.
DR Pharos; Q6GQQ9; Tbio.
DR PRO; PR:Q6GQQ9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6GQQ9; protein.
DR Bgee; ENSG00000264522; Expressed in buccal mucosa cell and 181 other tissues.
DR ExpressionAtlas; Q6GQQ9; baseline and differential.
DR Genevisible; Q6GQQ9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0002385; P:mucosal immune response; ISS:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:HGNC-UCL.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; IDA:ParkinsonsUK-UCL.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
DR GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR GO; GO:0071947; P:protein deubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0035871; P:protein K11-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR002653; Znf_A20.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF01754; zf-A20; 1.
DR SMART; SM00259; ZnF_A20; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS51036; ZF_A20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cytoplasm;
KW Hydrolase; Immunity; Metal-binding; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..843
FT /note="OTU domain-containing protein 7B"
FT /id="PRO_0000188788"
FT DOMAIN 183..365
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT ZN_FING 796..831
FT /note="A20-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT REGION 50..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..401
FT /note="TRAF-binding"
FT REGION 167..440
FT /note="Catalytic"
FT REGION 187..193
FT /note="Regulatory loop"
FT /evidence="ECO:0000269|PubMed:27732584"
FT REGION 442..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 483..498
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 67..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 191
FT /evidence="ECO:0000250"
FT ACT_SITE 194
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:12682062,
FT ECO:0000269|PubMed:14748687, ECO:0000269|PubMed:22179831,
FT ECO:0000269|PubMed:27732584"
FT ACT_SITE 358
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:27732584"
FT BINDING 802
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 807
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 819
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 822
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT SITE 197
FT /note="Stabilizes the conformation of the regulatory loop"
FT /evidence="ECO:0000269|PubMed:27732584"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RUR8"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RUR8"
FT MOD_RES 729
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:B2RUR8"
FT VAR_SEQ 805..833
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046015"
FT MUTAGEN 155..156
FT /note="LI->GG: Reduces deubiquitinating activity."
FT /evidence="ECO:0000269|PubMed:27732584"
FT MUTAGEN 157
FT /note="E->K: Reduces deubiquitinating activity with 'Lys-
FT 11'-linked ubiquitin chains; no effect on cleavage of 'Lys-
FT 48'-linked and 'Lys-63'-linked ubiquitin chains."
FT /evidence="ECO:0000269|PubMed:27732584"
FT MUTAGEN 193
FT /note="N->L,M: Loss of deubiquitinating activity due to
FT stabilization of the autoinhibited conformation."
FT /evidence="ECO:0000269|PubMed:27732584"
FT MUTAGEN 194
FT /note="C->A: Loss of deubiquitinating activity. Increased
FT ability to interact with polyubiquitin."
FT /evidence="ECO:0000269|PubMed:12682062,
FT ECO:0000269|PubMed:14748687, ECO:0000269|PubMed:22179831,
FT ECO:0000269|PubMed:27732584"
FT MUTAGEN 194
FT /note="C->S: Loss of deubiquitinating activity."
FT /evidence="ECO:0000269|PubMed:12682062,
FT ECO:0000269|PubMed:14748687, ECO:0000269|PubMed:22179831"
FT MUTAGEN 194
FT /note="C->S: Loss of deubiquitinating activity; when
FT associated with N-358."
FT /evidence="ECO:0000269|PubMed:26903241"
FT MUTAGEN 197
FT /note="H->A,E: Strongly reduces deubiquitinating activity."
FT /evidence="ECO:0000269|PubMed:27732584"
FT MUTAGEN 197
FT /note="H->D,N: Reduces deubiquitinating activity."
FT /evidence="ECO:0000269|PubMed:27732584"
FT MUTAGEN 210
FT /note="D->A: Reduces deubiquitinating activity."
FT /evidence="ECO:0000269|PubMed:27732584"
FT MUTAGEN 295
FT /note="E->K: Loss of deubiquitinating activity."
FT /evidence="ECO:0000269|PubMed:27732584"
FT MUTAGEN 358
FT /note="H->A: Loss of deubiquitinating activity."
FT /evidence="ECO:0000269|PubMed:27732584"
FT MUTAGEN 358
FT /note="H->N: Loss of deubiquitinating activity; when
FT associated with S-194."
FT /evidence="ECO:0000269|PubMed:26903241"
FT MUTAGEN 809
FT /note="F->A: Does not affect interaction with EGFR."
FT /evidence="ECO:0000269|PubMed:22179831"
FT MUTAGEN 810
FT /note="Y->A: Impairs interaction with EGFR."
FT /evidence="ECO:0000269|PubMed:22179831"
FT CONFLICT 243
FT /note="K -> E (in Ref. 5; AAH20622)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="K -> R (in Ref. 5; AAH20622)"
FT /evidence="ECO:0000305"
FT CONFLICT 791
FT /note="G -> S (in Ref. 2; BAH13129)"
FT /evidence="ECO:0000305"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:5LRW"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:5LRW"
FT HELIX 144..152
FT /evidence="ECO:0007829|PDB:5LRW"
FT HELIX 158..166
FT /evidence="ECO:0007829|PDB:5LRW"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:5LRU"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:5LRW"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:5LRV"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:5LRW"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:5LRW"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:5LRW"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:5LRW"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:5LRV"
FT HELIX 209..222
FT /evidence="ECO:0007829|PDB:5LRW"
FT HELIX 227..243
FT /evidence="ECO:0007829|PDB:5LRW"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:5LRW"
FT HELIX 251..266
FT /evidence="ECO:0007829|PDB:5LRW"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:5LRW"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:5LRW"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:5LRW"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:5LRW"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:5LRW"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:5LRW"
FT STRAND 350..355
FT /evidence="ECO:0007829|PDB:5LRW"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:5LRW"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:5LRW"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:5LRW"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:5LRW"
FT HELIX 401..406
FT /evidence="ECO:0007829|PDB:5LRV"
FT HELIX 412..428
FT /evidence="ECO:0007829|PDB:5LRW"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:5LRW"
SQ SEQUENCE 843 AA; 92526 MW; 6D386C864B12EE57 CRC64;
MTLDMDAVLS DFVRSTGAEP GLARDLLEGK NWDVNAALSD FEQLRQVHAG NLPPSFSEGS
GGSRTPEKGF SDREPTRPPR PILQRQDDIV QEKRLSRGIS HASSSIVSLA RSHVSSNGGG
GGSNEHPLEM PICAFQLPDL TVYNEDFRSF IERDLIEQSM LVALEQAGRL NWWVSVDPTS
QRLLPLATTG DGNCLLHAAS LGMWGFHDRD LMLRKALYAL MEKGVEKEAL KRRWRWQQTQ
QNKESGLVYT EDEWQKEWNE LIKLASSEPR MHLGTNGANC GGVESSEEPV YESLEEFHVF
VLAHVLRRPI VVVADTMLRD SGGEAFAPIP FGGIYLPLEV PASQCHRSPL VLAYDQAHFS
ALVSMEQKEN TKEQAVIPLT DSEYKLLPLH FAVDPGKGWE WGKDDSDNVR LASVILSLEV
KLHLLHSYMN VKWIPLSSDA QAPLAQPESP TASAGDEPRS TPESGDSDKE SVGSSSTSNE
GGRRKEKSKR DREKDKKRAD SVANKLGSFG KTLGSKLKKN MGGLMHSKGS KPGGVGTGLG
GSSGTETLEK KKKNSLKSWK GGKEEAAGDG PVSEKPPAES VGNGGSKYSQ EVMQSLSILR
TAMQGEGKFI FVGTLKMGHR HQYQEEMIQR YLSDAEERFL AEQKQKEAER KIMNGGIGGG
PPPAKKPEPD AREEQPTGPP AESRAMAFST GYPGDFTIPR PSGGGVHCQE PRRQLAGGPC
VGGLPPYATF PRQCPPGRPY PHQDSIPSLE PGSHSKDGLH RGALLPPPYR VADSYSNGYR
EPPEPDGWAG GLRGLPPTQT KCKQPNCSFY GHPETNNFCS CCYREELRRR EREPDGELLV
HRF
