ID UCHL5_DICDI Reviewed; 343 AA.
AC Q54N38;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 24-JAN-2024, entry version 101.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase isozyme L5;
DE Short=UCH-L5;
DE EC=3.4.19.12;
DE AltName: Full=Ubiquitin thioesterase L5;
GN Name=uch2; Synonyms=uchl5; ORFNames=DDB_G0285527;
OS Dictyostelium discoideum (Social amoeba).
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: Protease that specifically cleaves 'Lys-48'-linked
CC polyubiquitin chains. Deubiquitinating enzyme associated with the 19S
CC regulatory subunit of the 26S proteasome (By similarity).
CC {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 -!- SUBUNIT: Component of the 19S (PA700) regulatory complex of the 26S
CC proteasome. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C12 family. {ECO:0000305}.
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; AAFI02000079; EAL64601.1; -; Genomic_DNA.
DR RefSeq; XP_638105.1; XM_633013.1.
DR AlphaFoldDB; Q54N38; -.
DR SMR; Q54N38; -.
DR STRING; 44689.Q54N38; -.
DR MEROPS; C12.005; -.
DR PaxDb; 44689-DDB0233072; -.
DR EnsemblProtists; EAL64601; EAL64601; DDB_G0285527.
DR GeneID; 8625153; -.
DR KEGG; ddi:DDB_G0285527; -.
DR dictyBase; DDB_G0285527; uch2.
DR eggNOG; KOG2778; Eukaryota.
DR HOGENOM; CLU_018316_0_1_1; -.
DR InParanoid; Q54N38; -.
DR OMA; YIQYEIQ; -.
DR PhylomeDB; Q54N38; -.
DR Reactome; R-DDI-5689603; UCH proteinases.
DR PRO; PR:Q54N38; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd09617; Peptidase_C12_UCH37_BAP1; 1.
DR Gene3D; 1.20.58.860; -; 1.
DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR InterPro; IPR017390; Ubiquitinyl_hydrolase_UCH37.
DR InterPro; IPR041507; UCH_C.
DR PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR10589:SF16; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L5; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR Pfam; PF18031; UCH_C; 1.
DR PIRSF; PIRSF038120; Ubiquitinyl_hydrolase_UCH37; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Nucleus; Protease; Proteasome; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..343
FT /note="Ubiquitin carboxyl-terminal hydrolase isozyme L5"
FT /id="PRO_0000331127"
FT REGION 242..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 157
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT SITE 172
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 343 AA; 39325 MW; CAE23E5DB3EBE169 CRC64;
MSENEGWCTI ESDPGVFTEL ITKIGVKDIQ VEELYTLDSS EYDRLKPVLG LIFLFKWEKE
EENRTISDNE NIFFANQVIQ NACATQAILS VLLNSEGIEL GEELSNFKSF VGDFPPMMKG
EAIGNSELIK ETHNSFTVQD PFIFSKKKNR KPSDAFHFIS FIPFQGKVYE LDGLKKGPYC
LGDCTPDNWL EIATPFIQKR MEKYSQGEIR FNLMAVIKNR QTTLQEKILT LEKKKNDLEI
KLSELNSGSG GDNKEESGGA TPTTKEDLNF MINVVNNDIE EANNEILMEQ EKFRNWKDEN
IRRKHNFTPL ILNLIKGLAE KDNLQPLIQK AKDQISQKQQ QHK
//
