UBP21_RAT
ID UBP21_RAT Reviewed; 565 AA.
AC B2GUX4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 21;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 21;
DE AltName: Full=Ubiquitin thioesterase 21;
DE AltName: Full=Ubiquitin-specific-processing protease 21;
GN Name=Usp21;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Deubiquitinates histone H2A, a specific tag for epigenetic
CC transcriptional repression, thereby acting as a coactivator.
CC Deubiquitination of histone H2A releaves the repression of di- and
CC trimethylation of histone H3 at 'Lys-4', resulting in regulation of
CC transcriptional initiation. Regulates gene expression via histone H2A
CC deubiquitination. Also capable of removing NEDD8 from NEDD8 conjugates
CC but has no effect on Sentrin-1 conjugates. Deubiquitinates BAZ2A/TIP5
CC leading to its stabilization. {ECO:0000250|UniProtKB:Q9UK80}.
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 -!- SUBUNIT: Interacts with BEND3 and BAZ2A/TIP5.
CC {ECO:0000250|UniProtKB:Q9UK80}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP21 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC166443; AAI66443.1; -; mRNA.
DR RefSeq; NP_001121110.1; NM_001127638.1.
DR AlphaFoldDB; B2GUX4; -.
DR SMR; B2GUX4; -.
DR STRING; 10116.ENSRNOP00000055192; -.
DR PaxDb; B2GUX4; -.
DR PRIDE; B2GUX4; -.
DR GeneID; 688466; -.
DR KEGG; rno:688466; -.
DR UCSC; RGD:1588822; rat.
DR CTD; 27005; -.
DR RGD; 1588822; Usp21.
DR VEuPathDB; HostDB:ENSRNOG00000038347; -.
DR eggNOG; KOG1868; Eukaryota.
DR HOGENOM; CLU_035237_0_0_1; -.
DR InParanoid; B2GUX4; -.
DR OMA; ERRNPGP; -.
DR OrthoDB; 561804at2759; -.
DR PhylomeDB; B2GUX4; -.
DR Reactome; R-RNO-5357786; TNFR1-induced proapoptotic signaling.
DR Reactome; R-RNO-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-RNO-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR PRO; PR:B2GUX4; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000038347; Expressed in thymus and 20 other tissues.
DR Genevisible; B2GUX4; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0019784; F:deNEDDylase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016578; P:histone deubiquitination; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IMP:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
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 Activator; Chromatin regulator; Cytoplasm; Hydrolase; Metal-binding;
KW Nucleus; Protease; Reference proteome; Thiol protease; Transcription;
KW Transcription regulation; Ubl conjugation pathway; Zinc.
FT CHAIN 1..565
FT /note="Ubiquitin carboxyl-terminal hydrolase 21"
FT /id="PRO_0000367509"
FT DOMAIN 212..558
FT /note="USP"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 134..152
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 57..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 221
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 518
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 437
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 565 AA; 62700 MW; 37ABEBF9CE07E938 CRC64;
MPQASEHRLG RTREPPVNVQ PRVGAKIPFP PRARSKERRN PVPGPNSMLR PLPPRPGPPD
ERLKKLDLGR GRTSGSRPRG PLRADHGVPL PGSPPPTVAL PLPSRTNLTR SKSVSSGDLR
PMGIALGGHR GTGELGAALS RLALRPEPPT LRRSTSLRRL GGFPGPPTLL SIRTEPPPSH
GSFHMISARP SEPFYSDDKM AHHTLLLGSG HVGLRNLGNT CFLNAVLQCL SSTRPLRDFC
LRRDFRQEVP GGGRAQELTE AFADVIGALW HPDSCEAVNP TRFRAVFQKY VPSFSGYSQQ
DAQEFLKLLM ERLHLEINRR GRRAPPILAS GPVPSPPRRG GALHEEPELS DDDRANLMWK
RYLEREDSKI VDLFVGQLKS CLKCQACGYR STTFEVFCDL SLPIPKKGFA GGKVSLRDCF
SLFTKEEELE SENAPVCDRC RQKTRSTKKL TVQRFPRILV LHLNRFSTSR GSIKKSSVGV
DFPLQRLSLG DFASDKVGSP VYQLYALCNH SGSVHYGHYT ALCRCQTGWH VYNDSRVSPV
SENQVASSEG YVLFYQLMQE PPRCL
