UBP2_CHICK
ID UBP2_CHICK Reviewed; 357 AA.
AC O57429;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 2;
DE EC=3.4.19.12;
DE AltName: Full=41 kDa ubiquitin-specific protease;
DE AltName: Full=Deubiquitinating enzyme 2;
DE AltName: Full=Ubiquitin thioesterase 2;
DE AltName: Full=Ubiquitin-specific-processing protease 2;
GN Name=USP2; Synonyms=UBP41;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=9325273; DOI=10.1074/jbc.272.41.25560;
RA Baek S., Choi K.S., Yoo Y.J., Cho J.M., Baker R.T., Tanaka K., Chung C.H.;
RT "Molecular cloning of a novel ubiquitin-specific protease, UBP41, with
RT isopeptidase activity in chick skeletal muscle.";
RL J. Biol. Chem. 272:25560-25565(1997).
CC -!- FUNCTION: Hydrolase that deubiquitinates polyubiquitinated target
CC proteins such as MDM2, MDM4 and CCND1. Possesses both ubiquitin-
CC specific peptidase and isopeptidase activities. May play a role in the
CC regulation of the circadian clock. {ECO:0000250|UniProtKB:O75604,
CC ECO:0000250|UniProtKB:O88623}.
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: Homooligomer. {ECO:0000250|UniProtKB:O88623}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O88623}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O88623}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF016107; AAC13729.1; -; mRNA.
DR AlphaFoldDB; O57429; -.
DR SMR; O57429; -.
DR STRING; 9031.ENSGALP00000040033; -.
DR MEROPS; C19.013; -.
DR PaxDb; O57429; -.
DR PRIDE; O57429; -.
DR VEuPathDB; HostDB:geneid_395766; -.
DR eggNOG; KOG1868; Eukaryota.
DR InParanoid; O57429; -.
DR OrthoDB; 1283205at2759; -.
DR PhylomeDB; O57429; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:Roslin.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016579; P:protein deubiquitination; IDA:Roslin.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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 Biological rhythms; Cytoplasm; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway; Zinc.
FT CHAIN 1..357
FT /note="Ubiquitin carboxyl-terminal hydrolase 2"
FT /id="PRO_0000080618"
FT DOMAIN 19..351
FT /note="USP"
FT ACT_SITE 28
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 309
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75604"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75604"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75604"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75604"
SQ SEQUENCE 357 AA; 40932 MW; EC39E6454937C455 CRC64;
MAARMAPTPR SSKVVQGLTG LRNLGNTCFM NSILQCLSNT KELRDYCLQN QYLRDLNNNS
RMRTALMSEF AKLIQLLWTS SPNDSVSPSE FKTQIQRYAP RFVGYNQQDA QEFLRFLLDG
LHGEVNRVLV RPRANADTLD HLPDDEKSRQ MWRRYQERED SRVSDLFVGQ LKSSLTCSEC
GYCSTAFDPF WDLSLPIPKK GYGEVTLMDC LRLFTKEDVL DGDEKPTCCR CKARTRCTKK
FSIQKFPKIL VLHLKRFSEA RIRASKLTTF VNFPLKDLDL REFASQSCNH AVYNLYAVSN
HSGTTMGGHY TAYCKSPISS EWHSFNDSRV TPMSSSHVRS SDAYLLFYEL ASPSSRM
