UBP10_CHICK
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 03-AUG-2022, entry version 91.
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. Acts as an essential regulator of p53/TP53
CC stability: in unstressed cells, specifically deubiquitinates p53/TP53
CC in the cytoplasm, leading to counteracts MDM2 action and stabilize
CC p53/TP53. Following DNA damage, translocates to the nucleus and
CC deubiquitinates p53/TP53, leading to regulate the p53/TP53-dependent
CC DNA damage response. Component of a regulatory loop that controls
CC autophagy and p53/TP53 levels (By similarity).
CC {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.ENSGALP00000009085; -.
DR MEROPS; C19.018; -.
DR PaxDb; Q5ZJN4; -.
DR GeneID; 415817; -.
DR KEGG; gga:415817; -.
DR CTD; 9100; -.
DR VEuPathDB; HostDB:geneid_415817; -.
DR eggNOG; KOG1871; Eukaryota.
DR InParanoid; Q5ZJN4; -.
DR OrthoDB; 1078977at2759; -.
DR PhylomeDB; Q5ZJN4; -.
DR PRO; PR:Q5ZJN4; -.
DR Proteomes; UP000000539; Unplaced.
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:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; 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 I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028767; USP10.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR13328:SF5; PTHR13328:SF5; 1.
DR Pfam; PF07145; PAM2; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 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
