ID A0A3Q0QZS7_AMPCI Unreviewed; 809 AA.
AC A0A3Q0QZS7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000003552.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000003552.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3Q0QZS7; -.
DR STRING; 61819.ENSACIP00000003552; -.
DR Ensembl; ENSACIT00000003668.1; ENSACIP00000003552.1; ENSACIG00000002757.1.
DR GeneTree; ENSGT00940000157719; -.
DR OMA; STWIVWC; -.
DR Proteomes; UP000261340; Unplaced.
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 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 36..153
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 193..808
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 809 AA; 88899 MW; 620290CDB1ED2F17 CRC64;
MRLKDPFSLK AAEMTKRTNK PRKPRDEESS DEVSGLTCQH VSRAVDLNSV KKSVLSSVWS
VCSECLKERT MIDGEPAASH DILVCLKCGF QGCNQSGIQH VVKHHQAFHP ESHCITISLS
TWKAWCFECN EELSTHCNKK ALAQSLDFLQ KHSVRATSAV SPKIIKLREE PPDYADPPRG
KSSAINSALV PVKGINNLGN TCFFNAVMQN LSQTHMLIDL IQEVKEKGYK LRICPPPETN
LSPLTVVLPS PEPLTAAMFA FLQSMKEPGK GPINPKILFN QLCQKAPCFK GYQQQDSQEL
LHYLMDSIRV EETKRVKAGI LKAFNNPTEK TADEETKRQV KAYGKEGVKM NFVDRIFVGE
LTNTIMCEEC EHISTVKEAF IDISLPIIEE RISKPSNPGR LGKGGREQDS HTAHSDHVPS
AAHAVNRNTR KPSTQKQQSR RSSSSVEDKG ATFGGDRPEE EGVAGGSSHG VSVCKMAAAG
SLSDGSERDS GAQDSSNDAD SEASESEWAP RSASHSQSHG HMSTPSSTST LTPSPTPVSA
SSPSSSSSTK QGGAVEQIVS AVAKVNLSFS SGDSASAHCP PEEHGESQSR DNLHHQHHQG
AFQALSHSYT PSSKECSIQS CLHQFTSVEL LMGNNRLLCE SCTERRQKQL RKSSSADKKM
EKVYTSARKQ MLISSLPPVI TLHLKRFHQA GMNLRKVNRH VDFPLILDLA PFCSASCKNL
AAGERVLYSL YGIVEHSGSM RGGHYTAYVK VRAPQRKTEQ HHKNLSGARD ACSISHSQWV
YVSDTTVQVV PESRVLNSQA YLLFYEEML
//
