UBP21_ARATH
ID UBP21_ARATH Reviewed; 732 AA.
AC Q9FIQ1; Q9FPS6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 21;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 21;
DE Short=AtUBP21;
DE AltName: Full=Ubiquitin thioesterase 21;
DE AltName: Full=Ubiquitin-specific-processing protease 21;
GN Name=UBP21; OrderedLocusNames=At5g46740; ORFNames=MZA15.16;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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}.
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DR EMBL; AF302669; AAG42759.1; -; mRNA.
DR EMBL; AB016882; BAB08918.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95420.1; -; Genomic_DNA.
DR RefSeq; NP_568667.1; NM_124044.2.
DR AlphaFoldDB; Q9FIQ1; -.
DR SMR; Q9FIQ1; -.
DR STRING; 3702.AT5G46740.1; -.
DR MEROPS; C19.A15; -.
DR iPTMnet; Q9FIQ1; -.
DR PaxDb; Q9FIQ1; -.
DR PRIDE; Q9FIQ1; -.
DR ProteomicsDB; 233050; -.
DR EnsemblPlants; AT5G46740.1; AT5G46740.1; AT5G46740.
DR GeneID; 834717; -.
DR Gramene; AT5G46740.1; AT5G46740.1; AT5G46740.
DR KEGG; ath:AT5G46740; -.
DR Araport; AT5G46740; -.
DR TAIR; locus:2178535; AT5G46740.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_018749_0_0_1; -.
DR InParanoid; Q9FIQ1; -.
DR OMA; ITNPFRI; -.
DR OrthoDB; 561804at2759; -.
DR PhylomeDB; Q9FIQ1; -.
DR PRO; PR:Q9FIQ1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIQ1; baseline and differential.
DR Genevisible; Q9FIQ1; 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:0006281; P:DNA repair; IMP:TAIR.
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..732
FT /note="Ubiquitin carboxyl-terminal hydrolase 21"
FT /id="PRO_0000313047"
FT DOMAIN 163..469
FT /note="USP"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 172
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 428
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT CONFLICT 732
FT /note="L -> LWRVSY (in Ref. 1; AAG42759)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 732 AA; 82417 MW; FDEEDE5B92703F08 CRC64;
MAEFSDPPPS NLSSSHKLTK PNQTLDESSP TAPIRDLVTN SLSLSSPIRQ IQALSPAKPD
GSSSSPPDKT LNFNPEENRD VNPDESSSSP SDKTLIAPPA QISPVSNNNH LRITNTSDSY
LYRPPRRYIE YESDDDELNK MEPTKPLQLS WWYPRIEPTG VGAGLYNSGN TCFIASVLQC
FTHTVPLIDS LRSFMYGNPC NCGNEKFCVM QALRDHIELA LRSSGYGINI DRFRDNLTYF
SSDFMINHQE DAHEFLQSFL DKLERCCLDP KNQLGSVSSQ DLNIVDNVFG GGLMSTLCCC
NCNSVSNTFE PSLGWSLEIE DVNTLWKALE SFTCVEKLED QLTCDNCKEK VTKEKQLRFD
KLPPVATFHL KRFTNDGVTM EKIFDHIEFP LELDLSPFMS SNHDPEVSTR YHLYAFVEHI
GIRATFGHYS SYVRSAPETW HNFDDSKVTR ISEERVLSRP AYILFYAREG TPWFSSTFEQ
LKTVFEATPL HFSPVSVLDN SYESVDNSSK ACNDSVGVSI PDVKWPDSCC QEPKEEVFHS
AESSNNEDSS AMIDALGSPQ SEKPFAETSQ QTEPESCPTE NKAYIDKSEK PFAETSQPKE
PKPFADRASI DAPLLKVQNQ DISPKRKAGE RATLGGPKLK YQKPNSHQKR QGTFQIQRAH
LQTKKQEESR KTKRPLFRSN VAASAPDPKY KNHALSYLNR AQTPRARKLA NALSDSPTKK
KKSSNMRRSI KL
