ID A0A3Q1CLT1_AMPOC Unreviewed; 637 AA.
AC A0A3Q1CLT1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000026524.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000026524.1}
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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR AlphaFoldDB; A0A3Q1CLT1; -.
DR STRING; 80972.ENSAOCP00000026524; -.
DR Ensembl; ENSAOCT00000017682.1; ENSAOCP00000026524.1; ENSAOCG00000014861.1.
DR GeneTree; ENSGT00940000154596; -.
DR Proteomes; UP000257160; 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; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF727; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 42; 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 Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 54..331
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 347..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 73106 MW; 32DA0636BEE97CC9 CRC64;
QIASFYFKRP SEKSDHESVC PVISSSDGID LPQKVLFSPE RLVLKWTQVH RIGAGLQNMG
NTCFLNSALQ CLTYTPPLAN YMLTQEHSKT CHEPGFCMMC TMQNHIIQVF ANSGKVIKPT
GHLRYGSQED AHEFLRYTVD AMQKSCLPGT NCNNTVLCFA VECLNCKAVS DTFDPFLDIF
LSMQTASSVS KALKQFVKPE QLGDENAYKC TKCKEMVTAS KRFTIHRSSN VLTLSLKRFA
NFNGGKIRKN VKYAEYLDLR PFMSQSQGEP QLYRLYAVLV HSGFSCHAGH YFCYIKASNG
QWYQMNDSSV SVSDIRSVLN QQSYALFYIN SPPPATATKT HSVAIESAAS SGHQGNPAAL
STQPDCSQST SGPSVTPQKV SISKIEAKDL PQSNGPSAVT EGRPDTKEQH QSKPSYRVNE
RQSSRDRERD RLYSDTCRDR ERHYRDRSPE WLRRDYRDNS NYLPYRDRSP PQKRSKRDWD
SERRQEQTVH LPRDCDRDRS SYNYNYYPQR SREDVDRGRR GYDYYCEESH NHRRWHKESG
DSRAMKDRSS GRKRDYYPSK EGTSFPATMS ETSKFKGFPP RVLLSTSESA LNREDQNHRR
TADHPSKERD DSSEACRSEK HRKSQKSKDE DRHRESG
//
