ID A0A2D0R0Y5_ICTPU Unreviewed; 987 AA.
AC A0A2D0R0Y5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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|RefSeq:XP_017323691.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017323691.1};
RN [1] {ECO:0000313|RefSeq:XP_017323691.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017323691.1};
RG RefSeq;
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR RefSeq; XP_017323691.1; XM_017468202.2.
DR AlphaFoldDB; A0A2D0R0Y5; -.
DR STRING; 7998.ENSIPUP00000017611; -.
DR Ensembl; ENSIPUT00000018359; ENSIPUP00000017611; ENSIPUG00000011912.
DR GeneID; 108265645; -.
DR KEGG; ipu:108265645; -.
DR CTD; 8237; -.
DR OMA; TGQLVIM; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000221080; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR029346; USP_C.
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 Pfam; PF14533; USP7_C2; 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 ECO:0000313|RefSeq:XP_017323691.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 15..121
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 245..957
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 583..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..603
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..662
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 987 AA; 112691 MW; FCE2D89E986D4D04 CRC64;
MVMATSSTAA AAEPPGLETQ RQEIENLVQN QELRLGDCWY LLSRRWFELW NEYVKNGDQN
SPSYPGKVDN TELFNDLDSY RLKDRLVESE DFVLVPAEAW RKLLSWYGKM DGQPALERKV
IDLPSTLKVE IYPVEIMLCL HSDMDNVVTA QFSRADTILS IQKVMQKEFG VAEDAEPRLW
MKSSDNNCER LRNIHMTVLD ACLSTGVTVI MEMRNADGTW PSSRPQIMRN SMEEQDMYQG
QPGVCGLTNL GNTCFMNSAL QCLSNTPPLT EYFLRSLYID ELNFTNPLGM KGEIAEAYAD
VIKQMWSGRH YSVVPRVFKT KVGHFASQFL GYQQHDSQEL LSFLLDGLHE DLNRVKNKEY
IELKDADGRP DQEVADEAWC NHRRRNDSVI VDTFHGLFKS TLVCPECKKV SVTFDPFCYL
SIPLPVSTER AMEVFFISLD PLAKPMQYRV IVPKAGRVKD LCTALSKETN IPEKKMIVAD
VFNHRFYKIY HRDESLSLIL DRDDIFVYEL NSSITEDQDD KEVLLAVYMR ERSNYRDYGS
GGSNYSTSLF GHPLLMSLPR TQCNTDALYQ LFLQRLMRYV RQPDPTEEVE EEDEEENGSE
ENDEEDKIYT NQTNGLSGGE DEEEPEQAGP SKTEEPSQQN STQSEASPSS EEEEDEEETN
DEAAGESSTK EGQSACCSTD SNSQVTGDGT QAAAAQTSGK EDEDGEEDDG ELSETVAPAK
KTTMTTSRRR CTEKKKRPIF TIQAVNSNGT TDRGNGDGNG ALSFSNQLYV AIDWDPDMKK
KYYNDTEAEK YIKDKTMDVP QQQSTVHLQE CIELFTTMET LEEENPWYCP TCKKHQLATK
KLDLWSLPEV LIIHLKRFSY TKYSREKLDT IVDFPLRKLD FSDWLLRKTG SESEPPSRYD
LIAVSNHYGG LRDGHYTSYA RNKDNGQWYY FDDSKVTYAK EEQIMTNAAY LLFYQRQDKI
RHPTLAPPDN HVASTNHDGP GKAMETD
//
