ID A0A2Y9T2R0_PHYMC Unreviewed; 945 AA.
AC A0A2Y9T2R0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, 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};
GN Name=USP26 {ECO:0000313|RefSeq:XP_023983842.1};
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_023983842.1};
RN [1] {ECO:0000313|RefSeq:XP_023983842.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023983842.1};
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|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 RefSeq; XP_023983842.1; XM_024128074.1.
DR AlphaFoldDB; A0A2Y9T2R0; -.
DR STRING; 9755.ENSPCTP00005026520; -.
DR Ensembl; ENSPCTT00005029198; ENSPCTP00005026520; ENSPCTG00005019026.
DR KEGG; pcad:102979319; -.
DR InParanoid; A0A2Y9T2R0; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000248484; Chromosome 21.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02257; Peptidase_C19; 2.
DR CDD; cd13312; PH_USP37_like; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 2.30.29.180; Ubiquitin carboxyl-terminal hydrolase 26/29/37, pleckstrin homology-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR032069; USP37-like_PH.
DR InterPro; IPR038093; USP37-like_PH_sf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF23; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE USP2; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF16674; UCH_N; 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_023983842.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 299..911
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 182..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 945 AA; 106869 MW; 37C3FBC20B38D94F CRC64;
MDALMVHGFV QICSRKTRMS EVKEAFIEIV EKKRKVILVV YFSTGEYRTF QLNNNIKNIV
LRPCGEDQNF LYLIFQTNAF LSIERLSSRD AQNLKMFLDR VHQNHLHPPI RPDRDGSIFA
STTTQKAGGK TPSHKICKTS SKICKMSFRK ERNETPDYKE MSLFASELST FTCEELLENG
YGKRERRPSS GSEMNKNFLQ ENTSVKNRIA KMNPLRYVSH NEKGELRLKR LKKSNKLELG
ASLNINSTGN TYLDVTDLLQ RVSKKIYLAL LSESKYVEDD PEWGKLKMIF DFYPQKLWQG
LPNLGNSCYM NAVLQSLFSI PSFADDLLNQ GLSWGNMPPD ALSIFLAQLL ILNDIYNIKI
KEKLLVNIKN AISAVAEIFS GNMQNDAYEF LGHCLDQMKE NTGKFNTVCK TESESEEENS
PQQVSAGSAD TKVPVCPVAS NFDFELLRSI ICKACGHIVL KKEVDDSLSI NLPQGAQALP
LSIQSSFDLF FEAEELEYKC EKCKHRSSTA VHNFSRLPRV LIVHLKRYKF NESGSLRKDD
REVIISKYLK LSSHCNETTK PPLPLSKNAP LRDFQVLKVF PKFNSKTISS LTDSTKQTSE
SKDSLAPHIR SDEESEPQEC QTLHKASSRK EQQQDLGKYS KLNIIESTLV NSGYGAAIAR
ELLAVGLMMN LEDCSLSLNG TPASSPDTYH KVSPDTYHKK IPKLKKNKRT NMSSDFRSMA
ETTKEFCKDN KTRISEESCQ VPEETQQCGA LRLCEQDLCL VLIRRFPPPN TQWHTEKCRR
HTELSFQGAK VNSLGALGSN KDSGDKGSSH VEEASHVEEA SHVEEASHVE EASAKKPNRE
AKMGDSHDYR LIGVISHLGK TPGSGHYVSD AYNFERQEWL TYSDLQISGI QEAPMQEARL
CTGYIFFYMH NEIFEDLLGK KENSQPHSTE EGVVKEVDSG SHTSP
//
