ID A0A1A6FXT2_NEOLE Unreviewed; 777 AA.
AC A0A1A6FXT2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
DE Flags: Fragment;
GN ORFNames=A6R68_10160 {ECO:0000313|EMBL:OBS58726.1};
OS Neotoma lepida (Desert woodrat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Neotoma.
OX NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS58726.1, ECO:0000313|Proteomes:UP000092124};
RN [1] {ECO:0000313|EMBL:OBS58726.1, ECO:0000313|Proteomes:UP000092124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=417 {ECO:0000313|EMBL:OBS58726.1};
RC TISSUE=Liver {ECO:0000313|EMBL:OBS58726.1};
RA Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT lepida.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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. USP10 subfamily.
CC {ECO:0000256|ARBA:ARBA00005427}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBS58726.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LZPO01110810; OBS58726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A6FXT2; -.
DR STRING; 56216.A0A1A6FXT2; -.
DR Proteomes; UP000092124; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02257; Peptidase_C19; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR009818; Ataxin-2_C.
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:SF687; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10; 1.
DR Pfam; PF07145; PAM2; 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 Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000092124};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 403..774
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 126..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OBS58726.1"
SQ SEQUENCE 777 AA; 85635 MW; 56E07F3F87965C80 CRC64;
YIFGDFSPDE FNQFFVTPRS SVELPPYSGT LCGIQAEDEL PDGQEHQRIE FGVDEVIKPS
DGLPRTPSYS ISSTLNPQAP EFILGCTTSK KTSDGVEKDE NYSSIDQYPG SALALENSSN
VEAEALENDG GAGGLGQRER KKKKKRPPGY YSYLKDGGDE SVSPAALVNG HASSAVTNSV
GVEDAEFMVD MLPSVMPRTC DSPRNPMDFI SDPVPDSPFP RTLGGDARTA GLLEGCHGTD
FEQPCLPADS LLRTAVTQPY VGTDTTENLA VANGKILESL GEDTAANGIE LHTEESTDLD
LAKPESQSPP ADSMLSASGA IPISQPTKSW ASLFHDSKPS SSSPMAYVET KCSPPVPSPL
ASEKQVEVKE GLVPVSEDPV AIKIAELLET VTLIHKPVSL QPRGLINKGN WCYINATLQA
LVACPPMYHL MKFIPLYSKV QRPCTSTPMI DSFVRLMNEF TNMPVPPKPR QALGDKIVRD
IRPGAAFEPT YIYRLLTGRQ EDAEEYLGFI LNGLHEEMLS LKKLLSPTHE KLTVSNGPRS
HLIEDEEQED TGEGSEEEWE QVGPRNKTSV TRQADFVQTP ITGIFGGHIR SVVYQQSSKE
SATLQPFFTL QLDIQSDKIR TVQDALESLV ARESVQGYTT KTKQEVEVSR RVTLEKLPPV
LVLHLKRFVY EKTGGCQKLV KNIDYPVDLE ISKELLSPGV KNKNFKCHRT YRLFAVVYHH
GNSATGGHYT TDVFQIGLNG WLRIDDQTVK VINQYQVVKP TADRTAYLLY YRRVDLL
//
