ID G3NMQ7_GASAC Unreviewed; 793 AA.
AC G3NMQ7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
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:ENSGACP00000006620.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000006620.1, 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:ENSGACP00000006620.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR AlphaFoldDB; G3NMQ7; -.
DR STRING; 69293.ENSGACP00000006620; -.
DR Ensembl; ENSGACT00000006637.1; ENSGACP00000006620.1; ENSGACG00000005006.1.
DR eggNOG; KOG1873; Eukaryota.
DR GeneTree; ENSGT00940000157719; -.
DR InParanoid; G3NMQ7; -.
DR OMA; STWIVWC; -.
DR TreeFam; TF326075; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000005006; Expressed in head kidney and 8 other cell types or tissues.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0003407; P:neural retina development; IEA:Ensembl.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02667; Peptidase_C19K; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
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:SF34; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 45; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 39..156
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 196..792
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 87560 MW; 2B4FB99A7B7EFA31 CRC64;
MRLKDPFSLK AADMTKRTNK PRKPRDEESS DEVSEMSGLT CQHVSKAVDL SSVKKSVLSN
VWLVCAECLK ERTLIDGEPA ASHDILVCLK CGFQGCNQSG IQHAVRHHQA FHPESHCITI
SLSTWKAWCF ECNEELSTHC NKKALAQTLD FLQKHSVKAT SGASPKTIKL QEEPSEYGDS
PKGKSPAANS TLVPVKGINN LGNTCFFNAV MQNLSQTHML IDLIQEVKDK GYKLRISPTV
DATVSPLTVT LSSPEPLTAA MFLFLHNMKE PGKGPINPKI LFNQLCQKAP RFKGYQQQDS
QELLHYLLDS IRVEETKRVK AGILKAFNNP TEKTADEETK RQVKAYGKEG VKMNFVDRIF
VGELTNTIMC EECEHISTVK EAFIDISLPI IEERISKPWH PGRVGKGGRE QDPPPGLQGG
ASFSGTRRPQ KTQEAEWTAN LINTLSKKQQ SRRSLSSVEE KVAGCSAERQ EEDGVAAGSA
CGVSVCKMAA AGSLSDGSER DSAPQDSSND ADSEASESEW APRPFSSSHG HARQGGAVKQ
LVTAVSKVNI AFTAGEVAPL THRSPEEPGE TQSRDNLHHQ HHQGAFQALS HSYTPSSKEC
SIQSCLHQFT SVELLMGNNK LLCESCTERR QKQLRKSSSA DKKVEKIYTS ARKQMLISSL
PPVITLHLKR FHQAGMNLRK VNRHVDFPLI LDLAPFCSAS CKNLAAGERV LYSLYGIVEH
SGSMRGGHYT AYVKVRAPQR KTEQLQKNLS GTRDAGSSFQ GQWVYISDTT VQTVPESRVL
NSQAYLLFYE ELL
//
