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   24-JAN-2024, entry version 119.
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.Q9FPS7; -.
DR   MEROPS; C19.A16; -.
DR   PaxDb; 3702-AT4G17895-1; -.
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; AT4G17895; UBP20.
DR   eggNOG; KOG0706; Eukaryota.
DR   eggNOG; KOG1865; Eukaryota.
DR   HOGENOM; CLU_018749_0_0_1; -.
DR   InParanoid; Q9FPS7; -.
DR   OMA; TCDNCNE; -.
DR   OrthoDB; 227085at2759; -.
DR   PhylomeDB; Q9FPS7; -.
DR   PRO; PR:Q9FPS7; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9FPS7; baseline and differential.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02661; Peptidase_C19E; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF747; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 20; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   Genevisible; Q9FPS7; AT.
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
//