ID   A0A452ITA7_9SAUR        Unreviewed;       809 AA.
AC   A0A452ITA7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 4 {ECO:0000256|ARBA:ARBA00040967};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE   AltName: Full=Deubiquitinating enzyme 4 {ECO:0000256|ARBA:ARBA00042237};
DE   AltName: Full=Ubiquitin thioesterase 4 {ECO:0000256|ARBA:ARBA00041731};
DE   AltName: Full=Ubiquitin-specific-processing protease 4 {ECO:0000256|ARBA:ARBA00042735};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000031275.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000031275.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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; Evidence={ECO:0000256|ARBA:ARBA00000707};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. USP4 subfamily.
CC       {ECO:0000256|ARBA:ARBA00037971}.
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DR   AlphaFoldDB; A0A452ITA7; -.
DR   Ensembl; ENSGAGT00000035475.1; ENSGAGP00000031275.1; ENSGAGG00000021693.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 3.30.2230.10; DUSP-like; 1.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR028135; Ub_USP-typ.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF45; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 4; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF14836; Ubiquitin_3; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   PROSITE; PS51283; DUSP; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020}.
FT   DOMAIN          11..122
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          255..809
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
SQ   SEQUENCE   809 AA;  92533 MW;  AC90F5C514E14C5A CRC64;
     MAAELDCGPR PDVGAQRAEL GPLLGIALRP GESWYLIDSR WFKQWKKYVG FDSWDMYNVG
     EPNLFPGPID NSGLFADPEI QTLKEHLIDE LDYVLVPTEA WNKLVNWYGC IEGQQPIVRK
     VVEYGLFVKH CKVEVYLLEL KLCENSDPTN VLTCHFSKAD TIATIEKEMR QLFNIPSEKE
     TRLWSRYMSN AYEEVNYLDS TVQDAGLYHG QVLLIEVKNE DGTWPRQSLP AKVSGFSYNS
     YSCRESPFQS QPGICGLSNL GNTCFMNSAL QCLSNTPPLT EYFLEDRYEA EINHNNPLGM
     RGEIAEAYAE LIKQMWSGRH SHVAPRMFKT QVGRFAPQFS GYQQQDSQEL LAFLLDGLHE
     DLNRVKKKPY LELKDANGRP DSVVAKEAWE NHRLRNDSII VDIFHGLFKS TLVCPKCSKV
     SVTFDPFCYL TLPLPLKTDR SMDVSLVLAD LHRRPTQYRL VVPMMGTISD LCEALSKLSK
     IPAENMVVTD VYNHRFHKIF QMDEGLSHIM PKDNIFSSED GAECIILSVY FREKRIRQSS
     TSLGTVLCGQ PLLISVPKHK LTLDHLYNVM EHQDRDEEGR EKASETDSCQ SEGCAHDLLG
     KEWQHHKKHL FTFSLVNSYG TSEINSITTQ GKLLKLNSYA TLAIDLDPDT RKLLFDEQES
     QAFEKDESML QSQKKKTTVA LKDCIELFTT METLGEHDPW YCPKCKKHQQ ATKKFDLWSL
     PRILVVHLKR FSYSRYWRDK LDTVVEFPIR DLSMSEFVCD PAAEPYVYDL IAVSNHYGAM
     GVGHCEAGPW LMKKLGWLIG LVGKLFGQH
//