ID   A0A383ZEI5_BALAS        Unreviewed;       587 AA.
AC   A0A383ZEI5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   Name=LOC103005697 {ECO:0000313|RefSeq:XP_007173600.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007173600.1};
RN   [1] {ECO:0000313|RefSeq:XP_007173600.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007173600.1};
RG   RefSeq;
RL   Submitted (JAN-2023) to UniProtKB.
CC   -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC       from specific proteins to regulate different cellular processes.
CC       {ECO:0000256|RuleBase:RU366025}.
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|RuleBase:RU366025};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025}.
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DR   RefSeq; XP_007173600.1; XM_007173538.1.
DR   AlphaFoldDB; A0A383ZEI5; -.
DR   STRING; 310752.A0A383ZEI5; -.
DR   GeneID; 103005697; -.
DR   KEGG; bacu:103005697; -.
DR   InParanoid; A0A383ZEI5; -.
DR   OrthoDB; 4944670at2759; -.
DR   Proteomes; UP000261681; Unplaced.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02661; Peptidase_C19E; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 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   PANTHER; PTHR24006:SF651; INACTIVE UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 17-LIKE PROTEIN 4-RELATED; 1.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU366025,
KW   ECO:0000313|RefSeq:XP_007173600.1};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          123..418
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          68..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          554..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..568
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   587 AA;  64693 MW;  80708CBC6E0CA5D4 CRC64;
     MADGSVPGCH LQTDCLREGG IVVLLEHQME NLVDLVCRDV EAASLDWGDE CPLQFDIFPK
     LHSPQPSATG VDAHWGSPRP EEPSPPSQMV WCSQRGDLTP VSAGLACAQK LLLPWRLPFV
     VGAGLQNVGN TCYMNAALQC LTHTPPLASS MLSQQHSTIC PNQTFCMLCA MQTHITRALL
     HPGEVIRPRK DLVASFHRHK QEDAHEFLMF TLDAMQQACL SAYELLGHPS EDTTLVHRIF
     GGSWRCQIQC LHCLRVSDTL DPYLDITLDI TAAQSVVQAL NELGKPEKLD GENAYHCSVC
     LKKVPATKRL TLHSASQVLI VVLKRFTEVT GVKMVQKVHY PECLDLRPYV SEQKAGPLDY
     ALYAVLVHAG WSGHQGHYFC YVKAGNGQWY KVDDAMVTAC DVTSALSQSA YVLFYVQNSA
     LEGDCGRVSP GGARTPLGAE PTRTVTAHRE PERDVSIGVP GSEEPLEGTD VQEVSLEQWR
     RLQAPNRPKP EFNLRKIESA LPADAVVIHP SNYEGGMSTK LCEQENYQFN RASGDTAPKR
     PINIGSNIPC LSRRARASRK KNKKKQRSVG ALQKGLMHIL ADTHTSN
//