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Database: UniProt
Entry: H3CPM5_TETNG
LinkDB: H3CPM5_TETNG
Original site: H3CPM5_TETNG 
ID   H3CPM5_TETNG            Unreviewed;       524 AA.
AC   H3CPM5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   18-SEP-2019, entry version 58.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   Name=USP22 {ECO:0000313|Ensembl:ENSTNIP00000010208};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae;
OC   Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000010208, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Ensembl:ENSTNIP00000010208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A.,
RA   Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B.,
RA   Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S.,
RA   Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B.,
RA   Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V.,
RA   Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J.,
RA   Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S.,
RA   Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J.,
RA   Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M.,
RA   Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C.,
RA   Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals
RT   the early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000010208}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide,
CC         peptide and isopeptide bonds formed by the C-terminal Gly of
CC         ubiquitin (a 76-residue protein attached to proteins as an
CC         intracellular targeting signal).; EC=3.4.19.12;
CC         Evidence={ECO:0000256|RuleBase:RU366025,
CC         ECO:0000256|SAAS:SAAS01117307};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025, ECO:0000256|SAAS:SAAS01045498}.
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DR   Ensembl; ENSTNIT00000010389; ENSTNIP00000010208; ENSTNIG00000007402.
DR   eggNOG; KOG1867; Eukaryota.
DR   eggNOG; ENOG410XQQ0; LUCA.
DR   GeneTree; ENSGT00940000156623; -.
DR   InParanoid; H3CPM5; -.
DR   OMA; TMSPAGC; -.
DR   TreeFam; TF323554; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
DR   GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 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   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SUPFAM; SSF54001; SSF54001; 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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007303};
KW   Hydrolase {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044238};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01044152};
KW   Protease {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044292};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044269};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000256|SAAS:SAAS01044331}; Zinc {ECO:0000256|SAAS:SAAS01044373};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS01044352}.
FT   DOMAIN       61    121       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      176    519       USP. {ECO:0000259|PROSITE:PS50235}.
FT   ZN_FING      61    121       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
SQ   SEQUENCE   524 AA;  60087 MW;  083F0029FCE5E69C CRC64;
     RTGFAAQRTQ KPDAVTTMSP AGCPHVNSFK VDNWKQNLRV IYQCFVWSGS AETRKRKAKS
     CICHMCGAHL NRLHSCLHCV FFACFAKKHI HEHAKSKRHN LAIDLLYGGI YCFMCQDYIY
     DKDMEQIAKD EQRKAWKMQG IGEKYSTWEP TKRELELLRH NPKRRRITSN CTIGLRGLIN
     LGNTCFMNCI VQALTHTPLL RDFFLSDRHK CEMQSNSCLV CEMSQLFQEF YSGHRSPHIP
     FRLLHLVWTH ARHLAGYEQQ DAHEFLIAAL DVLHRHCKAD DNGKKANNPN HCNCIIDQIF
     TGGLQSDVTC QVCHGVSTTI DPFWDISLDL PGSSTPFWPL SPGGDASALN GESHATGATT
     LTDCLRRFTR PEHLGSSAKI KCSGCHSYQE STKQLTMKKL PIVACFHLKR FEHSAKLRRK
     ITTYVSFPLE LDMTPFMASS KESRMNGQYQ QIVDPFNNDN KYSLFAVVNH QGTLESGHYT
     TFIRQHKDQW FKCDDAIITK ASIKDVLDSE GYLLFYHKQF LEYE
//
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