ID   UBP10_CHICK             Reviewed;         785 AA.
AC   Q5ZJN4;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 97.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 10;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q14694};
DE   AltName: Full=Deubiquitinating enzyme 10;
DE   AltName: Full=Ubiquitin thioesterase 10;
DE   AltName: Full=Ubiquitin-specific-processing protease 10;
GN   Name=USP10; ORFNames=RCJMB04_16o18;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from target
CC       proteins such as p53/TP53, RPS2/us5, RPS3/us3, RPS10/eS10, BECN1, SNX3
CC       and CFTR. Acts as an essential regulator of p53/TP53 stability: in
CC       unstressed cells, specifically deubiquitinates p53/TP53 in the
CC       cytoplasm, leading to counteracts MDM2 action and stabilize p53/TP53.
CC       Following DNA damage, translocates to the nucleus and deubiquitinates
CC       p53/TP53, leading to regulate the p53/TP53-dependent DNA damage
CC       response. Component of a regulatory loop that controls autophagy and
CC       p53/TP53 levels. Plays a key role in 40S ribosome subunit recycling
CC       when a ribosome has stalled during translation: acts both by inhibiting
CC       formation of stress granules, which store stalled translation pre-
CC       initiation complexes, and mediating deubiquitination of 40S ribosome
CC       subunits. Deubiquitinates CFTR in early endosomes, enhancing its
CC       endocytic recycling. {ECO:0000250|UniProtKB:Q14694}.
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:0000250|UniProtKB:Q14694};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14694}. Nucleus
CC       {ECO:0000250|UniProtKB:Q14694}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. USP10 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ720400; CAG32059.1; -; mRNA.
DR   RefSeq; NP_001006130.1; NM_001006130.1.
DR   AlphaFoldDB; Q5ZJN4; -.
DR   SMR; Q5ZJN4; -.
DR   BioGRID; 677409; 1.
DR   STRING; 9031.ENSGALP00000056499; -.
DR   MEROPS; C19.018; -.
DR   PaxDb; 9031-ENSGALP00000009085; -.
DR   GeneID; 415817; -.
DR   KEGG; gga:415817; -.
DR   CTD; 9100; -.
DR   VEuPathDB; HostDB:geneid_415817; -.
DR   eggNOG; KOG1871; Eukaryota.
DR   InParanoid; Q5ZJN4; -.
DR   PhylomeDB; Q5ZJN4; -.
DR   PRO; PR:Q5ZJN4; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISS:UniProtKB.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB.
DR   GO; GO:0006974; P:DNA damage response; ISS:UniProtKB.
DR   GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; ISS:UniProtKB.
DR   GO; GO:0062030; P:negative regulation of stress granule assembly; ISS:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR   GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB.
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; PS50235; USP_3; 1.
PE   2: Evidence at transcript level;
KW   Autophagy; Cytoplasm; DNA damage; DNA repair; Hydrolase; Nucleus; Protease;
KW   Reference proteome; Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..785
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 10"
FT                   /id="PRO_0000393001"
FT   DOMAIN          401..782
FT                   /note="USP"
FT   REGION          113..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..565
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        410
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092"
FT   ACT_SITE        736
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092"
SQ   SEQUENCE   785 AA;  86556 MW;  97AB9EAE92AE32AB CRC64;
     MAVNGAQYIF GEFSPDEFNQ FFVTPRCSVE LPPYNETVSC GIKSTNEEYQ RIEFGVNEVI
     ETESSVLNNT DYSISSTLNP QAPEFILSCA PAQKTPDETN YNSIDCQFSD PTLTLDSGSN
     AENDGLSGGL GQRERKKKKK RPPGYYSYLE DVSDGVAPTE ALVNGHANSS GLNSIGTEDT
     ELTGDIPSLA TPRTCNSPDN SVDFVHEAVS DDSVSSALDN TRTAGQPEVC RVTNSEQFCI
     PSETGRDSPL RTAVVQPYAG TDTTESLGVT NGQTLESSGE DTAANGVELH TVESTDSDQA
     KPEEASPTTE ATATVAGSVP VNQPAKSWAS LFHNSKPSAS TSVVYVETKY TPPATSTLVP
     EKQVEVKEGP VPVSEDPVAI KIAELLENVK LVHKPVSLQP RGLINKGNWC YINATLQALV
     ACPPMYHLMK SIPMYSKSQR PCTSTPMIDS FVRLMNEFTN MPVPPKAKQA LGDKIVRDIR
     PGAAFEPTYI YRLLTVIKSS LSEKGRQEDA EEYLGFILNG LHEEMLTLKK LLSPHNEKLS
     VSNGPEVQTV REEEEQDEQG EGSEDEWEQV GPRNKSSVTR QADFVQTPIT DIFGGHIRSV
     VYQQSSKESA TLQPFFTLQL DIQSDKIRTV QDALESLVAR ESVQGYTTKT KQEVEISRRV
     TLEELPPVLV LHLKRFVYEK TGGCQKLIKN IEYPVDLEIS KELLSPGVKS KIFKGQRTYR
     LFAVVYHHGN SATGDHYTTD VFQIGLNGWL RIDDQAVKVI NQYQVVKPSA ERTAYLLYYR
     RVDLL
//