ID A0A3Q1F576_9TELE Unreviewed; 972 AA.
AC A0A3Q1F576;
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};
GN Name=USP11 {ECO:0000313|Ensembl:ENSAPOP00000002495.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000002495.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000002495.1}
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; A0A3Q1F576; -.
DR Ensembl; ENSAPOT00000013348.1; ENSAPOP00000002495.1; ENSAPOG00000003900.1.
DR GeneTree; ENSGT00940000160485; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
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:SF29; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 11; 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; 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:UP000257200};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 1..83
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 207..929
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 543..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..563
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 110273 MW; D49D990CC29D531C CRC64;
MYVVDRRWFE QWKEFVETGD QNSSSFPGQI DNTELFEDLD SYHLKERLVE NEDFVLVPAE
AWHKLLAWYG MVDDQPPLER KVVDLPSTLK VEVYPVEIFL CLHSNMENVI TAQFSRADNI
HSIQRAMCQA FSVPPGSECR LWMKSSDSSC ERLRNVHMSV LDACLSSGMT VIMETRNADG
TWPSSRPQIM RNSVEDQDSY RGQPGVCGLT NLGNTCFMNS ALQCLSNTPP LTEYFLQSSY
LEELNFTNPL GMKGEIAEAY ADVIKQMWSG RHYSVVPRVF KTKVGHFASQ FLGYQQHDSQ
ELLSFLLDGL HEDLNRVKNK EYIELRDADG RPDQEVAEEA WRNHRRRNDS VIVDTFHGLF
KSTLVCPECH KVSVTFDPFC YLSVPLPVSK ERVMEVFFVS LDPYAKPVQH RVVVPKAGKV
SDLCTALSEM TNVPPTRMVV ADVFNHRFYK IYNTEESLSC ILDRDDIFVY ELSVLEEQQE
EQVLLALYLR ERSHYRDYGS GSSSYSTTLF GHPLLLNVLR SSCSREALYN LFLQRLARYV
RPPDPSEELE EEEEEEDDEE ELDKTQTNGI SDDEEQEDVE NPGPSQTEPC CSDPSPSSQS
DDTVTAEPQP EVNHTQSSMD HSDTETTNGS MNQTEPVCSA DTNSSNSTGD SGSIAGTGAA
SEPPAEQPQQ PCETTEEESE EGKQEEACSP SPPANEHPAK RRACRKKRKS LFTIQAVNSN
GTTERGMGEG GSAVSFSSQP YVAIDWDPDM KKRFYNENEA EKYVKHASME VPQQQTTVQL
QECIELFTTV ETLEEENPWY CPVCKKHQLA TKKLDLWSLP EVLIIHLKRF SYTKFTREKL
DSIVDFPLRD LDFSGCLLRK TVSSEEPPSR YDLIAVSNHY GGLRDGHYTS YARNKDNGQW
YYFDDSKVTY AREDQIMTNA AYVLFYHRQD KIRIPTLPAP NTSPASSTQS DITSCKDDEA
AGLGASSYVA ME
//
