ID A0A455C037_PHYMC Unreviewed; 711 AA.
AC A0A455C037;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=USP36 {ECO:0000313|RefSeq:XP_028354715.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028354715.1};
RN [1] {ECO:0000313|RefSeq:XP_028354715.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028354715.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC from specific proteins to regulate different cellular processes.
CC {ECO:0000256|RuleBase:RU366025}.
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 RefSeq; XP_028354715.1; XM_028498914.2.
DR AlphaFoldDB; A0A455C037; -.
DR Proteomes; UP000248484; Chromosome 14.
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:SF653; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 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 ECO:0000313|RefSeq:XP_028354715.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 122..423
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 428..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..554
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 711 AA; 76877 MW; A3092150D2AD928F CRC64;
MPIVDKLKEA LKPGRRDSAD DGELGKLLAS SARKVLLQKL EFEPASKSFS YQLESLKSKY
VLLNPRTEGA GCHRSGDEPQ ARTQGGEHAY ESCGDGVPAP QKVLFPVERL SLRWGRVYRV
GAGLHNLGNT CFLNSTVQCL TYTPPLANYL LSKEHTRGCH QGSFCMLCVM QNHIIQAFAN
SGNAIKPVSF IRDLRKIARH FRFGNQEDAH EFLRYTIDAM QKACLSGCAK LDRQTQATTL
VHQIFGGYLR SRVKCSVCKS VSDTYDPYLD VALEIRQAAN IVRALELFVK PDVLSGENAY
MCAKCKKKVP ASKRFTVHRT SNVLTLSLKR FANFSGGKIT KDVGYPEFLN IRPYMSQSNG
EPVMYGLYAV LVHSGYSCHA GHYYCYVKAS SGQWYQMNDS FVHSSNIKVV LNQQAYVLFY
LRIPGSKKSP EGSICRTTSS LPGHPRVVPD HARKNISNGT TSSSVTGKRP DTVTMKKPQT
PEELGVPVAR NGSVSGLKSQ NGYTTPKPPL GSPSPKLCKT PTHAPTVLDE PGKKVKKPAP
PQHFSPPLKT SPGPPSAGEP GGSRCEGRRP GSWDSRATLS TSPRPPAART ANGLGPKVGV
EGPTAERRGS SPERPAGGGP ARPPPAPQSG AAPLGDSQGT HSAGPAKVLP AREDVELVKA
KCLDLSSASP EPANTMSPPP AKKLALSARK STKFLFMSIT AGQHPAEGNR Q
//