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 27-MAR-2024, entry version 183. 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; 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; P20618: PSMB1; NbExp=3; IntAct=EBI-527784, EBI-372273; CC Q6GQQ9; Q7Z5V6-2: SAXO4; NbExp=3; IntAct=EBI-527784, EBI-12000762; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 67. DR DIP; DIP-33805N; -. DR IntAct; Q6GQQ9; 70. DR STRING; 9606.ENSP00000462729; -. DR BindingDB; Q6GQQ9; -. DR ChEMBL; CHEMBL4630838; -. DR MEROPS; C64.001; -. DR GlyCosmos; Q6GQQ9; 1 site, 1 glycan. 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; 9606-ENSP00000462729; -. DR PeptideAtlas; Q6GQQ9; -. DR ProteomicsDB; 66318; -. [Q6GQQ9-1] DR Pumba; Q6GQQ9; -. DR Antibodypedia; 72463; 274 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 AGR; HGNC:16683; -. DR CTD; 56957; -. DR DisGeNET; 56957; -. DR GeneCards; OTUD7B; -. DR HGNC; HGNC:16683; OTUD7B. DR HPA; ENSG00000264522; Low tissue specificity. 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; 2909231at2759; -. 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 NF-kappa-B signaling pathway. DR Reactome; R-HSA-5689896; Ovarian tumor domain proteases. DR SignaLink; Q6GQQ9; -. DR SIGNOR; Q6GQQ9; -. DR BioGRID-ORCS; 56957; 21 hits in 1198 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 183 other cell types or tissues. DR ExpressionAtlas; Q6GQQ9; baseline and differential. 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:1990380; F:K48-linked deubiquitinase activity; IDA:ParkinsonsUK-UCL. DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IBA:GO_Central. 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 canonical NF-kappaB signal transduction; 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: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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd22772; OTU_OTUD7B; 1. DR CDD; cd14347; UBA_Cezanne_like; 1. DR Gene3D; 1.20.5.4770; -; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR InterPro; IPR003323; OTU_dom. DR InterPro; IPR002653; Znf_A20. DR PANTHER; PTHR13367:SF8; OTU DOMAIN-CONTAINING PROTEIN 7B; 1. DR PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1. DR Pfam; PF02338; OTU; 1. DR Pfam; PF14555; UBA_4; 1. DR Pfam; PF01754; zf-A20; 1. DR SMART; SM00259; ZnF_A20; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR PROSITE; PS50802; OTU; 1. DR PROSITE; PS51036; ZF_A20; 1. DR Genevisible; Q6GQQ9; HS. 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 FT 'Lys-11'-linked ubiquitin chains; no effect on cleavage of FT 'Lys-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 //