UBP20_ARATH
ID UBP20_ARATH Reviewed; 695 AA.
AC Q9FPS7; O49688;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 20;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 20;
DE Short=AtUBP20;
DE AltName: Full=Ubiquitin thioesterase 20;
DE AltName: Full=Ubiquitin-specific-processing protease 20;
GN Name=UBP20; OrderedLocusNames=At4g17895; ORFNames=T6K21.70;
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.
RC STRAIN=cv. Columbia;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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).
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 (By similarity).
CC {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 -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA17132.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g17890 has been split into 2 genes: At4g17890 and At4g17895.; Evidence={ECO:0000305};
CC Sequence=CAB78791.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g17890 has been split into 2 genes: At4g17890 and At4g17895.; Evidence={ECO:0000305};
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DR EMBL; AF302668; AAG42758.1; -; mRNA.
DR EMBL; AL021889; CAA17132.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161547; CAB78791.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83963.1; -; Genomic_DNA.
DR PIR; T05075; T05075.
DR RefSeq; NP_567544.1; NM_117899.3.
DR AlphaFoldDB; Q9FPS7; -.
DR SMR; Q9FPS7; -.
DR BioGRID; 12806; 1.
DR IntAct; Q9FPS7; 1.
DR STRING; 3702.AT4G17895.1; -.
DR MEROPS; C19.A16; -.
DR PaxDb; Q9FPS7; -.
DR PRIDE; Q9FPS7; -.
DR ProteomicsDB; 228484; -.
DR EnsemblPlants; AT4G17895.1; AT4G17895.1; AT4G17895.
DR GeneID; 827513; -.
DR Gramene; AT4G17895.1; AT4G17895.1; AT4G17895.
DR KEGG; ath:AT4G17895; -.
DR Araport; AT4G17895; -.
DR TAIR; locus:505006491; AT4G17895.
DR eggNOG; KOG0706; Eukaryota.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_018749_0_0_1; -.
DR InParanoid; Q9FPS7; -.
DR OMA; QERTFEM; -.
DR OrthoDB; 561804at2759; -.
DR PhylomeDB; Q9FPS7; -.
DR PRO; PR:Q9FPS7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9FPS7; baseline and differential.
DR Genevisible; Q9FPS7; AT.
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; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..695
FT /note="Ubiquitin carboxyl-terminal hydrolase 20"
FT /id="PRO_0000313046"
FT DOMAIN 176..476
FT /note="USP"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 185
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 435
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 695 AA; 78633 MW; 8FD6265E169892D2 CRC64;
MLMAKPDVPS SILPRSSSIL PNSIETLDEN ESIEAQVNNV QSLALSSPNR DRSDDDDNNN
NHDSVSIPPP IYDGYSSSSS DESQSVPSPP INLDHDDDEC QIPIRNTSQA LDDIDDDIWG
DDDLPETRRP WTPNVSPGFG SDDDDDNDDD NSKNEPRKSL FYGFRQEPEP VTGVGAGLWN
LGNSCFLNSV FQCFTHTVPL IESLLSFRYE VPCHCGNEFF CVIRAIRYHI EAALRPERCP
IAPYFFFDNL NYFSPDFQRY QQEDAHEFLQ AFLEKLEICG SDRTSFRGDI TSQDVFSGRL
ISGLRCCNCD YVSETYEKSV GLSLEIEDVD TLGSALESFT RVEKLDEQLT CDNCNEKVSK
EKQLLLDKLP LVATFHLKRF KNNGLYMEKI YKHVKIPLEI DLQPYMRNIQ ENEVSTKYHL
YALVEHFGYS VAYGHYSSYV RSAPKIWHHF DDSKVTRIDE DMVLSQDSYI LFYAREGTRW
FSSVYEEMQP LVEASLLNSS PKSVLDSSTN GECLSEISYE NGDKASKPCD SAGVCNQHVK
TKEDFVSLSN DDVFLSAESS SGEESPMGEL LDPLDPDDSY SPCTEKESDS CLAIERATIR
DDFFPLLLDQ NQESSTSSPK LQERTFEMQL LQMEETTKSQ EPWKQPLSSI SNIADSMEAE
FVYGDLMKKP SPRARELLDQ AISTNGSPPK KLKTT
