OTU1_DICDI
ID OTU1_DICDI Reviewed; 325 AA.
AC Q55BI3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Ubiquitin thioesterase OTU1;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q5VVQ6};
GN Name=yod1; ORFNames=DDB_G0271346;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
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: Hydrolase that can remove conjugated ubiquitin from proteins
CC and may therefore play an important regulatory role at the level of
CC protein turnover by preventing degradation.
CC {ECO:0000250|UniProtKB:Q5VVQ6}.
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:Q5VVQ6};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VVQ6}.
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DR EMBL; AAFI02000006; EAL71803.1; -; Genomic_DNA.
DR RefSeq; XP_645629.1; XM_640537.1.
DR AlphaFoldDB; Q55BI3; -.
DR SMR; Q55BI3; -.
DR STRING; 44689.DDB0266410; -.
DR MEROPS; C85.007; -.
DR PaxDb; Q55BI3; -.
DR EnsemblProtists; EAL71803; EAL71803; DDB_G0271346.
DR GeneID; 8617821; -.
DR KEGG; ddi:DDB_G0271346; -.
DR dictyBase; DDB_G0271346; yod1.
DR eggNOG; KOG3288; Eukaryota.
DR HOGENOM; CLU_049327_1_1_1; -.
DR InParanoid; Q55BI3; -.
DR OMA; NEEYCDW; -.
DR PhylomeDB; Q55BI3; -.
DR Reactome; R-DDI-5689896; Ovarian tumor domain proteases.
DR PRO; PR:Q55BI3; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; ISS:dictyBase.
DR GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR InterPro; IPR039138; OTU1_2_3.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR13312; PTHR13312; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Metal-binding; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..325
FT /note="Ubiquitin thioesterase OTU1"
FT /id="PRO_0000328367"
FT DOMAIN 123..246
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT ZN_FING 292..316
FT /note="C2H2-type"
FT REGION 7..86
FT /note="UBX-like"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 128..134
FT /note="Cys-loop"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 185..195
FT /note="Variable-loop"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 235..239
FT /note="His-loop"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 265..270
FT /note="S2 site"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT ACT_SITE 131
FT /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT ACT_SITE 134
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT ACT_SITE 239
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT ACT_SITE 316
FT /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
SQ SEQUENCE 325 AA; 36456 MW; DFB2AB7B181E4BDD CRC64;
MSLISIRIRS KTGVENIKLE SQLKLKELQN IIEEKTKIST DTQKILYGFP PKALDLSNQD
AVISGFLANG DTITIENVSS ISSNPGVDSV TNDKVTSSTN SFDRNIKSQP FISQEEEEDG
GYATRRVTDD DNSCLFSAVA YVLEDKNRLK GYSLRALIAQ NVKSDPFEYN EAVLGKSNEG
YCNWIQNPKN WGGAIELSIL SNHYKVEIAA FDISTQLMYC YGEDRKYTER VYLIYDGIHY
DALSICLTKN GPEDFDITRF SVDDKDSLAK MKVLIEKEFK AGKFTDTAKF SLICLNCNKT
LKGEKEAAIH ASTTGHGNFT EYKKR
