UBP5_ARATH
ID UBP5_ARATH Reviewed; 924 AA.
AC O22207; Q9SEX3;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 5;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 5;
DE Short=AtUBP5;
DE AltName: Full=Ubiquitin thioesterase 5;
DE AltName: Full=Ubiquitin-specific-processing protease 5;
GN Name=UBP5; OrderedLocusNames=At2g40930; ORFNames=T20B5.13;
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], FUNCTION, AND MUTAGENESIS OF CYS-326.
RC STRAIN=cv. Landsberg erecta; TISSUE=Flower;
RX PubMed=10898935; DOI=10.1006/abbi.2000.1874;
RA Rao-Naik C., Chandler J.S., McArdle B., Callis J.;
RT "Ubiquitin-specific proteases from Arabidopsis thaliana: cloning of AtUBP5
RT and analysis of substrate specificity of AtUBP3, AtUBP4, and AtUBP5 using
RT Escherichia coli in vivo and in vitro assays.";
RL Arch. Biochem. Biophys. 379:198-208(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP 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).
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.
CC {ECO:0000269|PubMed:10898935}.
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 -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AF048705; AAF21246.1; -; mRNA.
DR EMBL; AC002409; AAB86453.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09900.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61508.1; -; Genomic_DNA.
DR EMBL; AY099701; AAM20552.1; -; mRNA.
DR EMBL; BT000300; AAN15619.1; -; mRNA.
DR PIR; T00757; T00757.
DR RefSeq; NP_001323724.1; NM_001336876.1.
DR RefSeq; NP_565944.1; NM_129656.4.
DR AlphaFoldDB; O22207; -.
DR SMR; O22207; -.
DR BioGRID; 4028; 2.
DR IntAct; O22207; 1.
DR STRING; 3702.AT2G40930.1; -.
DR MEROPS; C19.093; -.
DR iPTMnet; O22207; -.
DR PaxDb; O22207; -.
DR PRIDE; O22207; -.
DR ProteomicsDB; 233058; -.
DR EnsemblPlants; AT2G40930.1; AT2G40930.1; AT2G40930.
DR EnsemblPlants; AT2G40930.2; AT2G40930.2; AT2G40930.
DR GeneID; 818691; -.
DR Gramene; AT2G40930.1; AT2G40930.1; AT2G40930.
DR Gramene; AT2G40930.2; AT2G40930.2; AT2G40930.
DR KEGG; ath:AT2G40930; -.
DR Araport; AT2G40930; -.
DR TAIR; locus:2058490; AT2G40930.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_7_1_1; -.
DR InParanoid; O22207; -.
DR OMA; RRKHALM; -.
DR OrthoDB; 1283205at2759; -.
DR PhylomeDB; O22207; -.
DR PRO; PR:O22207; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22207; baseline and differential.
DR Genevisible; O22207; AT.
DR GO; GO:0005634; C:nucleus; ISS:TAIR.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:TAIR.
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; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF143791; SSF143791; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51283; DUSP; 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; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..924
FT /note="Ubiquitin carboxyl-terminal hydrolase 5"
FT /id="PRO_0000080696"
FT DOMAIN 15..145
FT /note="DUSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 317..916
FT /note="USP"
FT REGION 64..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 326
FT /note="Nucleophile"
FT ACT_SITE 874
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MUTAGEN 326
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10898935"
SQ SEQUENCE 924 AA; 103875 MW; 0DF2EA93C8D2D51A CRC64;
MAEVSMGSSS SSTDLSPEEE RVFIRDIAIA AEANSKEGDT FYLITQRWWQ EWIEYVNQDQ
PCNTNDGSSL SEHCDSPGSS TLKKPSRIDN SDLIYDSSLE DPSNTSEIIE TLQEGRDYVL
LPQEVWNQLR SWYGGGPTLA RRVISSGLSQ TELAVEVYPL RLQLLLMPKS DHSAIRISKK
ETIRELHRRA CEIFDLDSEH VRIWDYYGHQ KYSLMNDLDK TLDDANLQMD QDILVEVLDI
NGTLSSAHIQ SAQENGLVDG DSTSILIEPS KSSLAAAGGF SSSRNAFRTG SVEVSQSFDN
TYSSTGVTTR GSTAGLTGLL NLGNTCFMNS AIQCLVHTPE FASYFQEDYH QEINWQNPLG
MVGELALAFG DLLRKLWAPG RTPIAPRPFK AKLARFAPQF SGYNQHDSQE LLAFLLDGLH
EDLNRVKHKP YINSRDADGR PDEEVADEFW KNHIARNDSI IVDVCQGQYK STLVCPICNK
VSVTFDPFMY LSLPLQFNTT RAITVTVFSC DKTALPSTIT VNVSKQGRCR DLIQALTNAC
SLKQSEELKL AEIRNNFIHR LFEDPLIPLS SIKDDDHLAA YKLSKSSENT TLLRLVLRRR
DQKAGEREST VQLKPCGTPL LSSASCGDAL TKGKIHCLVQ NMLSPFRREE SVGKKGNSDS
SIPERRSARF NNTEEEDKVG GLKKAKKSNS SDLGASKLSL QLIDEDNKTI NLPDNEAEAM
KLPSSATVTI YLDWTPELSG MYDITCLESL PEVLKYGPTT KKARSEPLSL YACLEAFLRE
EPLVPDEMWF CPQCNERRQA SKKLDLWRLP EVLVIHLKRF SYSRSMKHKL ETFVNFPIHD
LDLTKYVANK NLSQPQLYEL YALTNHYGGM GSGHYTAHIK LLDDSRWYNF DDSHISHINE
DDVKSGAAYV LFYRRKSDAG GKMT
