ID G3P6B7_GASAC Unreviewed; 327 AA.
AC G3P6B7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU367139};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU367139};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000013140.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000013140.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000013140.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Hydrolase that can specifically remove 'Lys-48'-linked
CC conjugated ubiquitin from proteins. Has exodeubiquitinase activity and
CC has a preference for long polyubiquitin chains. May play a regulatory
CC role at the level of protein turnover. {ECO:0000256|RuleBase:RU367139}.
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 ECO:0000256|RuleBase:RU367139};
CC -!- SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM63
CC subfamily. {ECO:0000256|ARBA:ARBA00006616,
CC ECO:0000256|RuleBase:RU367139}.
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DR AlphaFoldDB; G3P6B7; -.
DR Ensembl; ENSGACT00000013165.1; ENSGACP00000013140.1; ENSGACG00000009933.2.
DR GeneTree; ENSGT00390000016607; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000009933; Expressed in spleen and 13 other cell types or tissues.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0140934; F:histone deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:1990380; F:K48-linked deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR007518; MINDY.
DR InterPro; IPR033979; MINDY_domain.
DR PANTHER; PTHR18063; NF-E2 INDUCIBLE PROTEIN; 1.
DR PANTHER; PTHR18063:SF7; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE MINDY-1; 1.
DR Pfam; PF04424; MINDY_DUB; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU367139};
KW Protease {ECO:0000256|RuleBase:RU367139};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Thiol protease {ECO:0000256|RuleBase:RU367139};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU367139}.
FT DOMAIN 1..128
FT /note="MINDY deubiquitinase"
FT /evidence="ECO:0000259|Pfam:PF04424"
FT REGION 307..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 327 AA; 36647 MW; 33F200785B660914 CRC64;
MNTLFLRWKA KLPAQTEVVT TEDLMAHLVY AHAGECVLSV TPRHKADGMD LNFQNMSDAM
AVLPKLSTGL DVNVRFTGVT DFEYTPECIV FDLLDIPLYH GWLVDPQSPE MEASVGKLSY
NQLVEKIIDY KHSSDTQLTN AGLLAEQFLE STATQLSYHG LCELNTTATE GEISVFFRNN
HFSTMIKHKG HLYLLVSDQG FLQEEGLVWE SLHNVEGDGN FCDSDFRLCH PPQRAPPTTT
LPPGAQDAQR QIDQDYLVAV SLQQQQGGAP GPLSDLELAQ QLQQEEHRRQ HRRPVLIMMS
PCFQVRGHGS QQGGARRREK DSDCVVL
//
