UBP23_ARATH
ID UBP23_ARATH Reviewed; 859 AA.
AC Q9FPS4; Q9FJL7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 23;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 23;
DE Short=AtUBP23;
DE AltName: Full=Ubiquitin thioesterase 23;
DE AltName: Full=Ubiquitin-specific-processing protease 23;
GN Name=UBP23; OrderedLocusNames=At5g57990; ORFNames=MTI20.25;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08869.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF302671; AAG42761.1; -; mRNA.
DR EMBL; AB013396; BAB08869.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96982.1; -; Genomic_DNA.
DR RefSeq; NP_568873.1; NM_125184.3.
DR AlphaFoldDB; Q9FPS4; -.
DR SMR; Q9FPS4; -.
DR STRING; 3702.AT5G57990.1; -.
DR MEROPS; C19.A12; -.
DR PaxDb; Q9FPS4; -.
DR PRIDE; Q9FPS4; -.
DR ProteomicsDB; 233068; -.
DR EnsemblPlants; AT5G57990.1; AT5G57990.1; AT5G57990.
DR GeneID; 835910; -.
DR Gramene; AT5G57990.1; AT5G57990.1; AT5G57990.
DR KEGG; ath:AT5G57990; -.
DR Araport; AT5G57990; -.
DR TAIR; locus:2174403; AT5G57990.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_013307_0_0_1; -.
DR InParanoid; Q9FPS4; -.
DR OMA; VGHERRC; -.
DR OrthoDB; 561804at2759; -.
DR PhylomeDB; Q9FPS4; -.
DR PRO; PR:Q9FPS4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FPS4; baseline and differential.
DR Genevisible; Q9FPS4; 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..859
FT /note="Ubiquitin carboxyl-terminal hydrolase 23"
FT /id="PRO_0000313049"
FT DOMAIN 107..410
FT /note="USP"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 369
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT CONFLICT 657
FT /note="K -> N (in Ref. 1; AAG42761)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="K -> E (in Ref. 1; AAG42761)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 859 AA; 94903 MW; 046FE8764DBB4609 CRC64;
MEVATSSTEI TIQTDRDPSS NNNGSCAVAS STASAVFRKI EFHPARKPFN GFSNGRSDFK
IETLNPCSSN QRLLSAPSAK KPDSSDLLEH GFEPDLTFSI TFRKIGAGLQ NLGNTCFLNS
VLQCLTYTEP LAATLQTAAH QKYCHVAGFC ALCAIQKHVR TARQANGRIL APKDLVSNLR
CISRNFRNCR QEDAHEYMIN LLECMHKCSL PSGVPSESSD AYRRSLVHKI FGGSLRSQVK
CEQCSHCSNK FDPFLDLSLD ISKADSLQRA LSRFTAVELL DNGAKVYQCE RCKQKVKAKK
QLTVSKAPYV LTVHLKRFEA HRSEKIDRKV DFTSAIDMKP FVSGPHEGNL KYTLYGVLVH
YGRSSHSGHY ACFVRTSSGM WYSLDDNRVV QVSEKTVFNQ KAYMLFYVRD RQNAVPKNSV
PVVKKESFAT NRASLIVASN IKDQVNGSTV IKECGFGALV ANGLAPLKSC GPSTPAVLTQ
KDLNAKETQN NAISNVEAKE ILETENGSAP VKTCDLAAPT VLVQKDLNTK EIFQKEVPLP
QANGEGSLVK EDSKAACLIL PEKVSPHLDG SANAQTLVKL PTLGPKAENS VEEKNSLNNL
NEPANSLKVI NVSVGNPPVE KAVLIDQTMG HHLEESATSI ESLKLTSERE TLTTPKKTRK
PKTKTLKVEF KFFKLALGLR KKKVQRRERL STTVAGEIIS EELLSKKRVK YQDTSLIAPS
KMISSSDGAV TSDQQQPVGS SDLSEASQNA KRKRESVLLQ KEAVNILTRG VPETVVAKWD
EEISASQKRG SKSEGASSIG YVADEWDEEY DRGKKKKIRI KEESYRGPNP FQMLASKRQK
ETKKKWTQSI TDAKTAYRI
