ID   UCHL_DICDI              Reviewed;         255 AA.
AC   Q54T48;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase;
DE            EC=3.4.19.12;
DE   AltName: Full=Ubiquitin thioesterase;
GN   Name=uch1; Synonyms=uchl; ORFNames=DDB_G0282007;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Ubiquitin-protein hydrolase is involved both in the
CC       processing of ubiquitin precursors and of ubiquitinated proteins. This
CC       enzyme is a thiol protease that recognizes and hydrolyzes a peptide
CC       bond at the C-terminal glycine of either ubiquitin or nedd8 (By
CC       similarity). {ECO:0000250}.
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;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C12 family. {ECO:0000305}.
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DR   EMBL; AAFI02000044; EAL66425.1; -; Genomic_DNA.
DR   RefSeq; XP_640403.1; XM_635311.1.
DR   AlphaFoldDB; Q54T48; -.
DR   SMR; Q54T48; -.
DR   STRING; 44689.DDB0304593; -.
DR   MEROPS; C12.A11; -.
DR   PaxDb; Q54T48; -.
DR   EnsemblProtists; EAL66425; EAL66425; DDB_G0282007.
DR   GeneID; 8623358; -.
DR   KEGG; ddi:DDB_G0282007; -.
DR   dictyBase; DDB_G0282007; uch1.
DR   eggNOG; KOG1415; Eukaryota.
DR   HOGENOM; CLU_054406_1_1_1; -.
DR   InParanoid; Q54T48; -.
DR   OMA; YVCFVKG; -.
DR   PhylomeDB; Q54T48; -.
DR   Reactome; R-DDI-5689603; UCH proteinases.
DR   Reactome; R-DDI-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-DDI-8951664; Neddylation.
DR   PRO; PR:Q54T48; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.532.10; -; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001578; Peptidase_C12_UCH.
DR   InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR   PANTHER; PTHR10589; PTHR10589; 1.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..255
FT                   /note="Probable ubiquitin carboxyl-terminal hydrolase"
FT                   /id="PRO_0000331128"
FT   REGION          16..21
FT                   /note="Interaction with ubiquitin"
FT                   /evidence="ECO:0000250"
FT   REGION          227..232
FT                   /note="Interaction with ubiquitin"
FT                   /evidence="ECO:0000250"
FT   REGION          235..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        103
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        177
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            192
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   255 AA;  29106 MW;  A0B7E6B2540C24C3 CRC64;
     MSVDQELIET QKNWIPLEAN PEVLTTFMQS LGVSKDWEFC DIYGIDEGLL EMVPSPCVAV
     ILLFPITNEY EDKRYKLEKE IEEKGQVLSD KVYFMKQYIG NACGTIGVIH SVLNNANVIE
     FNENGFFKQF LDKTTSLSTE ERAISLLKNS EIEKSHEISA LQGQSNVPQE DEPVVLHFVS
     FVHVDGHLYE LDGRKPFAIN HGESSAETLL KDTANVLQKM IDEDPKEIRF NLMGLVKKPN
     EESEEEEEKE KEETK