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   27-MAR-2024, entry version 116.
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.Q9FPS4; -.
DR   MEROPS; C19.A12; -.
DR   PaxDb; 3702-AT5G57990-1; -.
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; AT5G57990; UBP23.
DR   eggNOG; KOG1865; Eukaryota.
DR   HOGENOM; CLU_013307_0_0_1; -.
DR   InParanoid; Q9FPS4; -.
DR   OMA; CEQCSHC; -.
DR   OrthoDB; 227085at2759; -.
DR   PhylomeDB; Q9FPS4; -.
DR   PRO; PR:Q9FPS4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FPS4; 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:SF758; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 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; Q9FPS4; AT.
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
//