ID A0A7L2TJI6_POMRU Unreviewed; 766 AA.
AC A0A7L2TJI6;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 19.
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 Name=Usp10 {ECO:0000313|EMBL:NXS32884.1};
GN ORFNames=POSRUF_R05441 {ECO:0000313|EMBL:NXS32884.1};
OS Pomatostomus ruficeps (Chestnut-crowned babbler).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sylvioidea; Timaliidae; Pomatostomus.
OX NCBI_TaxID=9176 {ECO:0000313|EMBL:NXS32884.1, ECO:0000313|Proteomes:UP000583496};
RN [1] {ECO:0000313|EMBL:NXS32884.1, ECO:0000313|Proteomes:UP000583496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-002-71 {ECO:0000313|EMBL:NXS32884.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXS32884.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:NXS32884.1}.
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DR EMBL; VYZT01035943; NXS32884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L2TJI6; -.
DR OrthoDB; 429671at2759; -.
DR Proteomes; UP000583496; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005769; C:early endosome; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IEA:TreeGrafter.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IEA:TreeGrafter.
DR CDD; cd02257; Peptidase_C19; 1.
DR FunFam; 3.90.70.10:FF:000015; Ubiquitin specific peptidase 10; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR009818; PAM2_motif.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR050164; Peptidase_C19.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000583496};
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 382..763
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 96..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..549
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXS32884.1"
FT NON_TER 766
FT /evidence="ECO:0000313|EMBL:NXS32884.1"
SQ SEQUENCE 766 AA; 83423 MW; EF8CF5CFC69A3565 CRC64;
VQLPPYNETV SCGIKSTGKF HDGEEYQRIE FGVNEVIETQ SSVLNNTDYS ISSTLNPQAP
EFILSCAPAQ KTPDDALGDT NYNSIDCQFS DPTLALDSGS NADNDGLAGG LGQRERKKKK
KRPPGYYSYL EDVPDGVAAP EALVNGHATA AGLNSLSAED TELAGDLPSL ATPRTCSSPA
SSVDFLAAGA CAEPGAGAAA GGRTAGQPEV CRLPSSEQFC LPSEAVRDSP LRTAVVQSYA
GTDTTEPLGV TNGQTLESSG EDTAANGVEL HTVESTDSDQ AKPEEASPTT EATVPLAGSV
PVNQPAKSWA SLFHNSKPSA STSVVYVETK YTPPATSPLV PEKQVEVKEG PVPVSEDPVA
IKIAEILENV RLIHKPVSLQ PRGLINKGNW CYINATLQAL VACPPMYHLM KSIPMYSKSQ
RPCTSTPMLD SFVRLMNEFT NMPVPPKAKQ ALGDKIVRDI RPGAAFEPTY IYRLLTVIKS
SLSEKGRQED AEEYLGFILN GLHEEMLTLK KLLSPHNEKL SVSNGPEAQA VPREEEQEEQ
GEGSEDEWEQ VGPRNKSSVT RQADFVQTPI TDIFGGHIRS VVYQQSSKES ATLQLFFTLQ
LDIQSDKIRT VQDALESLVA RESVQGYTTK TKQEVEISRR LTLEKLPPVL VLHLKRFVYE
KTGGCQKLIK NIEYTVDLEI SKELLSPGVK SKISKGQRTY RLFAVVYHHG NSATGGHYTT
DVFQIGLNGW LRIDDQAVRV VHHSQVVKAS LERTAYLLYY RQVDLL
//
