ID A0A2Y9SR76_PHYMC Unreviewed; 859 AA.
AC A0A2Y9SR76;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
GN Name=USP13 {ECO:0000313|RefSeq:XP_023979937.1};
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_023979937.1};
RN [1] {ECO:0000313|RefSeq:XP_023979937.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023979937.1};
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|PIRNR:PIRNR016308, ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|PIRNR:PIRNR016308,
CC ECO:0000256|RuleBase:RU366025}.
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DR RefSeq; XP_023979937.1; XM_024124169.3.
DR AlphaFoldDB; A0A2Y9SR76; -.
DR STRING; 9755.ENSPCTP00005003814; -.
DR Ensembl; ENSPCTT00005004213; ENSPCTP00005003814; ENSPCTG00005002736.
DR KEGG; pcad:102992461; -.
DR InParanoid; A0A2Y9SR76; -.
DR OrthoDB; 166948at2759; -.
DR Proteomes; UP000248484; Chromosome 1.
DR GO; GO:1904288; F:BAT3 complex binding; IEA:Ensembl.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:1990380; F:K48-linked deubiquitinase activity; IEA:Ensembl.
DR GO; GO:0070628; F:proteasome binding; IEA:Ensembl.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl.
DR GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0036506; P:maintenance of unfolded protein; IEA:Ensembl.
DR GO; GO:1904294; P:positive regulation of ERAD pathway; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:Ensembl.
DR CDD; cd02658; Peptidase_C19B; 1.
DR CDD; cd14384; UBA1_UBP13; 1.
DR CDD; cd14386; UBA2_UBP5; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR InterPro; IPR041432; UBP13_Znf-UBP_var.
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:SF10; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR Pfam; PF00627; UBA; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR Pfam; PF17807; zf-UBP_var; 1.
DR PIRSF; PIRSF016308; UBP; 1.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50030; UBA; 2.
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|PIRNR:PIRNR016308};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR016308};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR016308};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|PIRNR:PIRNR016308};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR016308};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR016308};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 187..295
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 336..857
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 652..693
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 723..763
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT ACT_SITE 345
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT ACT_SITE 819
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ SEQUENCE 859 AA; 97053 MW; A36A5BC602496054 CRC64;
MQRRGALFGM PGGSGNRKMA AGDIGELLVP HMPTIRVPRS GDRVYKNECA FSYDSPNSEG
GLYVCMNTFL AFGREHVERH FRKTGQSVYM YLKRHVHERV RGASGGALPK RRNSKIFLDL
DTDDDLNSDD YEYEDEAKLV IFPDHYEIAL PNIEELPALV TIACDAVLSS KSPYRKQDPD
TWENELPVSK YANKLTQLDN GVRIPPSGWK CARCDLRENL WLNLTDGSVL CGKWFFDSSG
GNGHALEHYR DLGYPLAVKL GTITPDGADV YSFQEEEPVL DPHLAKHLAH FGIDMLHMHG
TENGLQDNDS KPRISEWEVI QETGTKLKPM YGPGYTGLKN LGNSCYLSSV MQAIFSIPEF
QRAYVGNLPR IFDYSPLDPT QDFNTQMTKL GHGLLSGQYS KPPMKSELIE QVMKEEYKPQ
QNGISPRMFK AFVSKSHPEF SSNRQQDAQE FFLHLVNLVE RNRIGSENPS DVFRFLVEER
IQCCQTRKVR YVERVDYLMQ LPVAMEAATN KDELIAYELT RREAEANRRP LPELVRAKIP
FSACLQAFSE PENVDDFWSS ALQAKSAGVK TSRFASFPEY LVVQIKKFTF GLDWVPKKFD
VSIDMPDLLD INHLRARGLQ PGEEELPDIS PPVVIPDDSK DRLMNQLIDP SDIDESSVMQ
LAEMGFPLEA CRKAVYFTGN MGAEVAFNWI IVHMEEPDFA EPLTMPGYGG AATAGASAGL
DNQPPEETVA LITSMGFHRN QALQALRATN SNLERALDWI FSHPEFEEDS DFVIEMENNA
NANIISEAKP EGPRVKDGSG MYELFAFISH MGTSTMSGHY VCHIKKEGRW VIYNDHKVCA
SERPPKDLGY MYFYRRIPS
//
