ID   UBP22_DANRE             Reviewed;         506 AA.
AC   A6H8I0; Q1JQ28;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 22;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 22;
DE   AltName: Full=Ubiquitin thioesterase 22;
DE   AltName: Full=Ubiquitin-specific-processing protease 22;
GN   Name=usp22; ORFNames=zgc:136342;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Embryo, and Eye;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone deubiquitinating component of the transcription
CC       regulatory histone acetylation (HAT) complex SAGA. Catalyzes the
CC       deubiquitination of both histones H2A and H2B, thereby acting as a
CC       coactivator. Recruited to specific gene promoters by activators, where
CC       it is required for transcription (By similarity). {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   -!- SUBUNIT: Component of some SAGA transcription coactivator-HAT
CC       complexes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5DU02}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A6H8I0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A6H8I0-2; Sequence=VSP_036726, VSP_036727;
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. UBP8 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC116508; AAI16509.1; -; mRNA.
DR   EMBL; BC146618; AAI46619.1; -; mRNA.
DR   RefSeq; NP_001038713.1; NM_001045248.1.
DR   AlphaFoldDB; A6H8I0; -.
DR   SMR; A6H8I0; -.
DR   STRING; 7955.ENSDARP00000059142; -.
DR   PaxDb; 7955-ENSDARP00000126663; -.
DR   GeneID; 692275; -.
DR   KEGG; dre:692275; -.
DR   AGR; ZFIN:ZDB-GENE-060512-211; -.
DR   CTD; 23326; -.
DR   ZFIN; ZDB-GENE-060512-211; usp22.
DR   eggNOG; KOG1867; Eukaryota.
DR   InParanoid; A6H8I0; -.
DR   OMA; QRDQWFK; -.
DR   OrthoDB; 227085at2759; -.
DR   PhylomeDB; A6H8I0; -.
DR   Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR   PRO; PR:A6H8I0; -.
DR   Proteomes; UP000000437; Chromosome 12.
DR   Bgee; ENSDARG00000040407; Expressed in tail and 21 other cell types or tissues.
DR   ExpressionAtlas; A6H8I0; baseline.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02660; Peptidase_C19D; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF33; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 22; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   2: Evidence at transcript level;
KW   Activator; Alternative splicing; Cell cycle; Chromatin regulator;
KW   Hydrolase; Metal-binding; Nucleus; Protease; Reference proteome;
KW   Thiol protease; Transcription; Transcription regulation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..506
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 22"
FT                   /id="PRO_0000367511"
FT   DOMAIN          159..501
FT                   /note="USP"
FT   ZN_FING         4..121
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   ACT_SITE        168
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        460
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   BINDING         6
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         8
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         49
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   VAR_SEQ         261
FT                   /note="K -> KG (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_036726"
FT   VAR_SEQ         392..506
FT                   /note="RFEHSAKLRRKITTYVSFPLELDMTPFMASSKESRMNGQYQQPVDSLNNDNK
FT                   YSLFAVVNHQGTLESGHYTTFIRQHKDQWFKCDDAIITKASIKDVLDSEGYLLFYHKQF
FT                   LEYE -> VRAELLLSVLIFQHPLNVFVCFSAV (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_036727"
FT   CONFLICT        90
FT                   /note="Y -> H (in Ref. 1; AAI16509)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   506 AA;  58120 MW;  D749E025E4A15C03 CRC64;
     MSPAGCSHVN GFKVDNWKQN LRVIYQCFVW SGSAETRKRK AKSCICHMCG AHLNRLHSCL
     HCVFFGCFSK KHIHEHAKNK RHNLAIDLLY GGIYCFVCQD YIYDKDMEQI AKEEQRKAWK
     LQGIGEKYSM WEPTKRELEL LRHNPKRRKI TANCTIGLRG LINLGNTCFM NCIVQALTHT
     PLLRDFFLSD RHKCEMQSNS CLVCEMSQLF QEFYSGHRSP HIPFRLLHLV WTHARHLAGY
     EQQDAHEFLI AALDVLHRHC KDDNGKKANN PNHCNCIIDQ IFTGGLQSDV TCQVCHGVST
     TIDPFWDISL DLPGSSTPFW PLSPGSDGSV VNGDSHPSGA TTLTDCLRRF TRPEHLGSSA
     KIKCSGCHSY QESTKQLTMK RLPIVACFHL KRFEHSAKLR RKITTYVSFP LELDMTPFMA
     SSKESRMNGQ YQQPVDSLNN DNKYSLFAVV NHQGTLESGH YTTFIRQHKD QWFKCDDAII
     TKASIKDVLD SEGYLLFYHK QFLEYE
//