ID UBP26_ORYSJ Reviewed; 1079 AA. AC A3AF13; Q0DUD1; Q10QK5; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 2. DT 24-JAN-2024, entry version 100. DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 26; DE EC=3.4.19.12; DE AltName: Full=Deubiquitinating enzyme 26; DE AltName: Full=Ubiquitin thioesterase 26; DE AltName: Full=Ubiquitin-specific-processing protease 26; GN Name=UBP26; OrderedLocusNames=Os03g0192800, LOC_Os03g09260; GN ORFNames=OsJ_009385; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16109971; DOI=10.1101/gr.3869505; RG The rice chromosome 3 sequencing consortium; RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B., RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T., RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K., RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T., RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R., RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J., RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S., RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M., RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M., RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L., RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., RA Jin W., Lee H.R., Jiang J., Jackson S.; RT "Sequence, annotation, and analysis of synteny between rice chromosome 3 RT and diverged grass species."; RL Genome Res. 15:1284-1291(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=18089549; DOI=10.1093/nar/gkm978; RG The rice annotation project (RAP); RT "The rice annotation project database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R., RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L., RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H., RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using next RT generation sequence and optical map data."; RL Rice 6:4-4(2013). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L., RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). CC -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal CC Gly of ubiquitin. Involved in the processing of poly-ubiquitin CC precursors as well as that of ubiquitinated proteins. Deubiquitinates CC H2BK143ub1 of histone H2B (By similarity). {ECO:0000250}. 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; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=ABF94422.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=BAF11157.2; Type=Erroneous gene model prediction; 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; DP000009; ABF94422.1; ALT_SEQ; Genomic_DNA. DR EMBL; AP008209; BAF11157.2; ALT_SEQ; Genomic_DNA. DR EMBL; AP014959; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CM000140; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; A3AF13; -. DR SMR; A3AF13; -. DR STRING; 39947.A3AF13; -. DR MEROPS; C19.068; -. DR iPTMnet; A3AF13; -. DR PaxDb; 39947-A3AF13; -. DR eggNOG; KOG1863; Eukaryota. DR HOGENOM; CLU_008279_9_0_1; -. DR InParanoid; A3AF13; -. DR Proteomes; UP000000763; Chromosome 3. DR Proteomes; UP000007752; Chromosome 3. DR Proteomes; UP000059680; Chromosome 3. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd02668; Peptidase_C19L; 1. DR CDD; cd01795; Ubl_USP48; 1. DR Gene3D; 3.90.70.10; Cysteine proteinases; 1. DR Gene3D; 3.30.2230.10; DUSP-like; 2. 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; IPR000626; Ubiquitin-like_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR InterPro; IPR044743; Ubl_USP48. DR InterPro; IPR033841; USP48. DR InterPro; IPR018200; USP_CS. DR InterPro; IPR028889; USP_dom. DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1. DR PANTHER; PTHR24006:SF722; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 48; 1. DR Pfam; PF06337; DUSP; 2. DR Pfam; PF00443; UCH; 1. DR SMART; SM00695; DUSP; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR SUPFAM; SSF143791; DUSP-like; 2. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS51283; DUSP; 3. DR PROSITE; PS50053; UBIQUITIN_2; 1. DR PROSITE; PS00972; USP_1; 1. DR PROSITE; PS00973; USP_2; 1. DR PROSITE; PS50235; USP_3; 1. DR Genevisible; A3AF13; OS. PE 3: Inferred from homology; KW Hydrolase; Nucleus; Protease; Reference proteome; Repeat; Thiol protease; KW Ubl conjugation pathway. FT CHAIN 1..1079 FT /note="Ubiquitin carboxyl-terminal hydrolase 26" FT /id="PRO_0000293494" FT DOMAIN 106..446 FT /note="USP" FT DOMAIN 495..598 FT /note="DUSP 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613" FT DOMAIN 613..715 FT /note="DUSP 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613" FT DOMAIN 738..862 FT /note="DUSP 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613" FT DOMAIN 961..1037 FT /note="Ubiquitin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 384..419 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 948..972 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 384..398 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 399..419 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 115 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, FT ECO:0000255|PROSITE-ProRule:PRU10093" FT ACT_SITE 359 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, FT ECO:0000255|PROSITE-ProRule:PRU10093" SQ SEQUENCE 1079 AA; 119884 MW; 70581F22368079E4 CRC64; MSRPNTRNKS KRPRADDCES PSAVFKKIHS TGAITKGDIK QLYMVWKPVC HGCHGNSKDS PNCFCGLIPA ANGVRKSGLW QRTNEIIRAL GPNPSTDLRD STETPAGLTN LGATCYANSI LQCLYMNTSF RLGIFSLEPD ILKMHPVLDQ LARLFAQLHS SKMAFIDSAP FIKTLELDNG VQQDSHEFLT LFLSLLEGSL SHSKVPGART IVQHLFRGSV SHVTRCSSCG RDSEASSKME DFYELELNIK GLNNLEQSLD DYLSTEALDG ENQYFCESCQ KRVDATRCIK LRSLPPVVNF QLKRYVFLPK TTTKKKISSA FSFPGQLDMG KRLSNPSSSY TYGLSAILIH KGSAANSGHY VAHVKDESNG QWWEFDDEHV SKLGLHPFGE KPGKSSDKTD QKPQGSSTAD SVTNDDNNSC HEAAFTSTME EMFSSTDAYM LMYKRIAKDE NGIESNNISS NNSLPHHFVD EIDERNTSYV KECEEYESKK DVHLAYITER RQEVKSVLTE APATPEEDSY FWISTDWLRQ WADNVNPPSP IITGVRVHSS IDNSPIQCEH GKVPASKVTS MKRLSAGAWH KLFSKYGGGP TLSSDDFCME CLKDGAKNSV SADVYRDRKA SLRSIAEAAL AGNNPDGPLY FVSRPWLTQW LRRKNVDIPS DADSGPTIAL TCTHGNLLPE HASGAKRVTV PEDLWLFLYE TSGMKIDDIV TFPSDSQPCG ICSQQLSVVA SVEDNLRAVK LKQRQSHEKL TSGKSLALHP GQKYYLVPSS WLSEWRAYIT ATGKNISSLP EPQSLEVTIN SLICEKHSRL LQRPLDLVCK RGTITQKASN TDGLTMISES DWILFSEEWN VAHGKGLCAE IVFSKSSQDN LQSSEAVPIL VEDLDQSTND LSNDLGGREP YVRTDPEVCE ECIGEKESCA LVEKLNYQNE DIQVYLVRGK EAPKSIREAS AAVPVPDRRT SKRSRRTTSG NSISLKVSGS TTVYQLKLMI WESLGIVKEN QELHKGSVEI EDDFATLADK CIFPGDVLWV KDSEIYENRD IADEISEQKV VVQTEEGFRG TLLTSSASAQ LCQDISFSD //