UBP26_ARATH
ID UBP26_ARATH Reviewed; 1067 AA.
AC Q9SCJ9; Q9FPS1;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 26;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 26;
DE Short=AtUBP26;
DE AltName: Full=Ubiquitin thioesterase 26;
DE AltName: Full=Ubiquitin-specific-processing protease 26;
GN Name=UBP26; Synonyms=SUP32; OrderedLocusNames=At3g49600; ORFNames=T9C5.190;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=11115897; DOI=10.1104/pp.124.4.1828;
RA Yan N., Doelling J.H., Falbel T.G., Durski A.M., Vierstra R.D.;
RT "The ubiquitin-specific protease family from Arabidopsis. AtUBP1 and 2 are
RT required for the resistance to the amino acid analog canavanine.";
RL Plant Physiol. 124:1828-1843(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF CYS-115, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17554311; DOI=10.1038/nature05864;
RA Sridhar V.V., Kapoor A., Zhang K., Zhu J., Zhou T., Hasegawa P.M.,
RA Bressan R.A., Zhu J.-K.;
RT "Control of DNA methylation and heterochromatic silencing by histone H2B
RT deubiquitination.";
RL Nature 447:735-738(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
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. {ECO:0000269|PubMed:17554311}.
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:0000269|PubMed:17554311}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, stems, leaves and
CC inflorescences. {ECO:0000269|PubMed:17554311}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB62464.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF302674; AAG42764.1; -; mRNA.
DR EMBL; AL132964; CAB62464.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78564.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63555.1; -; Genomic_DNA.
DR PIR; T46237; T46237.
DR RefSeq; NP_001325635.1; NM_001339429.1.
DR RefSeq; NP_566922.1; NM_114820.4.
DR AlphaFoldDB; Q9SCJ9; -.
DR SMR; Q9SCJ9; -.
DR STRING; 3702.AT3G49600.1; -.
DR MEROPS; C19.068; -.
DR iPTMnet; Q9SCJ9; -.
DR PaxDb; Q9SCJ9; -.
DR PRIDE; Q9SCJ9; -.
DR ProteomicsDB; 228473; -.
DR EnsemblPlants; AT3G49600.1; AT3G49600.1; AT3G49600.
DR EnsemblPlants; AT3G49600.2; AT3G49600.2; AT3G49600.
DR GeneID; 824122; -.
DR Gramene; AT3G49600.1; AT3G49600.1; AT3G49600.
DR Gramene; AT3G49600.2; AT3G49600.2; AT3G49600.
DR KEGG; ath:AT3G49600; -.
DR Araport; AT3G49600; -.
DR TAIR; locus:2114653; AT3G49600.
DR eggNOG; KOG1863; Eukaryota.
DR eggNOG; KOG1869; Eukaryota.
DR HOGENOM; CLU_010287_0_0_1; -.
DR InParanoid; Q9SCJ9; -.
DR OrthoDB; 113272at2759; -.
DR PRO; PR:Q9SCJ9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SCJ9; baseline and differential.
DR Genevisible; Q9SCJ9; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
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; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd02668; Peptidase_C19L; 1.
DR CDD; cd01795; Ubl_USP48; 1.
DR Gene3D; 3.30.2230.10; -; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; 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 Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF143791; SSF143791; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54236; SSF54236; 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.
PE 1: Evidence at protein level;
KW Hydrolase; Nucleus; Protease; Reference proteome; Repeat; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..1067
FT /note="Ubiquitin carboxyl-terminal hydrolase 26"
FT /id="PRO_0000293492"
FT DOMAIN 106..442
FT /note="USP"
FT DOMAIN 503..595
FT /note="DUSP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 610..711
FT /note="DUSP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 738..861
FT /note="DUSP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 948..1031
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 115
FT /note="Nucleophile"
FT ACT_SITE 359
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MUTAGEN 115
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17554311"
FT CONFLICT 935
FT /note="E -> G (in Ref. 1; AAG42764)"
FT /evidence="ECO:0000305"
FT CONFLICT 989
FT /note="G -> E (in Ref. 1; AAG42764)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1067 AA; 119934 MW; C0338D496C035573 CRC64;
MSRPNTRNKN KRQRPDAVDS SSQILRKIHE ANDVTDDDIN QLFMIWKPVC QGCRVNTRDN
PNCFCGLVPP LNGSRKSGLW QKTSEIIQSL GPDPTLDRRD SESTPAGLTN LGATCYANSI
LQCLYMNTAF REGVFSVEVH VLKQNPVLDQ IARLFAQLHA SQKSFVDSDA FVKTLELDNG
VQQDTHEFLT LLLSLLERCL LHSGVKAKTI VQDLFSGSVS HVTTCSKCGR DSEASSKMED
FYALELNVKG LKSLDASLND YLSLEQLNGD NQYFCGSCNA RVDATRCIKL RTLPPVITFQ
LKRCIFLPKT TAKKKITSSF SFPQVLDMGS RLAESSQNKL TYDLSAVLIH KGSAVNSGHY
VAHIKDEKTG LWWEFDDEHV SELGKRPCNE ASSSTPQSES NGTASSGNIT DGIQSGSSDC
RSAIKSEVFS SSDAYMLMYS LRCDKQENQE GQKENPIDIT KGEVKQLKGG YLPKHLSEWI
NNMNAVFLES CKQYNLRKEK ELNALTERRQ EVRTILSEAA VQSLEEQYFW ISTDWLRLWA
DTTLPPALDN TPLLCSHGKV HASKVNCMKR ISELAWIKLE SKFNGGPKLG KGDYCRDCLM
DGARMVVSSD SYRDRRTFMK SIANDVLSGK CEDGMYYISR AWLQQWIKRK NLDAPTEADA
GPTNAITCNH GELMPEQAPG AKRVVVPENF WSFLFEDALK VMSEDTLDCT CFPVDSSQCC
HCTEVLSEVA CFEDSLRTLK VKQRQNHEKL ATGKGIPLTP QSRYFLLPSP WLVQWRIYIN
MTGKNSSSAP EPERLDGVIN TLKCKKHTRL LERLPELVCR RGSYFQKNPS TDKLTIIPEL
DWKYFCDEWG GLMENGISAF IEVGNTDQSS SPDVIDLEKD SSPDDNMDVD AQQLILRASP
EICEECIGER ESCELMQKLS YSEGDVFVCF VRGKEAPKAM LEASDSSFEV DRRTSKRSRR
TNYGNLTSLK VSATTTVYQL KMMIWELLGV MKENQELHKG SKVIDQESAT LADMNIFPGD
RLWVRDTEMH EHRDIADELC EKKPGAQDIE EGFRGTLLTG NISSEAC
