OTU1_YEAST
ID OTU1_YEAST Reviewed; 301 AA.
AC P43558; D6VTI6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Ubiquitin thioesterase OTU1;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q5VVQ6};
DE AltName: Full=OTU domain-containing protein 1;
GN Name=OTU1; OrderedLocusNames=YFL044C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION.
RX PubMed=15755922; DOI=10.1128/ec.4.3.604-614.2005;
RA Gardocki M.E., Bakewell M., Kamath D., Robinson K., Borovicka K.,
RA Lopes J.M.;
RT "Genomic analysis of PIS1 gene expression.";
RL Eukaryot. Cell 4:604-614(2005).
RN [6]
RP FUNCTION, DOMAIN OTU, IDENTIFICATION IN A COMPLEX WITH NPL4; UFD1; CDC48;
RP DOA1 AND SHP1, INTERACTION WITH DOA1 AND CDC48, AND MUTAGENESIS OF CYS-120.
RX PubMed=16427015; DOI=10.1016/j.molcel.2005.12.014;
RA Rumpf S., Jentsch S.;
RT "Functional division of substrate processing cofactors of the ubiquitin-
RT selective Cdc48 chaperone.";
RL Mol. Cell 21:261-269(2006).
RN [7]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-160, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
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. Participates in the
CC regulation of the ubiquitin conjugation pathway involving CDC48 by
CC hindering multiubiquitination of substrates at the CDC48 chaperone. May
CC be indirectly involved in PIS1 gene expression.
CC {ECO:0000269|PubMed:15755922, ECO:0000269|PubMed:16427015}.
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 -!- SUBUNIT: Forms a complex composed of CDC48, NPL4, UFD1, DOA1, SHP1 and
CC deubiquitinase OTU1; within the complex interacts with CDC48 and
CC DOA1/UFD3. {ECO:0000269|PubMed:16427015}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The OTU domain mediates the hydrolase activity and the
CC interaction with CDC48. {ECO:0000269|PubMed:16427015}.
CC -!- MISCELLANEOUS: Present with 2770 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; D50617; BAA09197.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12396.1; -; Genomic_DNA.
DR PIR; S56211; S56211.
DR RefSeq; NP_116610.1; NM_001179923.1.
DR PDB; 3BY4; X-ray; 1.55 A; A=91-301.
DR PDB; 3C0R; X-ray; 2.31 A; A/C=91-301.
DR PDB; 4KDI; X-ray; 1.86 A; C/D=1-73.
DR PDB; 4KDL; X-ray; 1.81 A; B=1-73.
DR PDBsum; 3BY4; -.
DR PDBsum; 3C0R; -.
DR PDBsum; 4KDI; -.
DR PDBsum; 4KDL; -.
DR AlphaFoldDB; P43558; -.
DR SMR; P43558; -.
DR BioGRID; 31103; 107.
DR DIP; DIP-4672N; -.
DR IntAct; P43558; 13.
DR MINT; P43558; -.
DR STRING; 4932.YFL044C; -.
DR MEROPS; C85.006; -.
DR TCDB; 3.A.16.1.2; the endoplasmic reticular retrotranslocon (er-rt) family.
DR iPTMnet; P43558; -.
DR MaxQB; P43558; -.
DR PaxDb; P43558; -.
DR PRIDE; P43558; -.
DR EnsemblFungi; YFL044C_mRNA; YFL044C; YFL044C.
DR GeneID; 850500; -.
DR KEGG; sce:YFL044C; -.
DR SGD; S000001850; OTU1.
DR VEuPathDB; FungiDB:YFL044C; -.
DR eggNOG; KOG3288; Eukaryota.
DR GeneTree; ENSGT00390000009989; -.
DR HOGENOM; CLU_049327_0_0_1; -.
DR InParanoid; P43558; -.
DR OMA; NEEYCDW; -.
DR BioCyc; YEAST:G3O-30420-MON; -.
DR Reactome; R-SCE-5689896; Ovarian tumor domain proteases.
DR EvolutionaryTrace; P43558; -.
DR PRO; PR:P43558; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43558; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:SGD.
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; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR13312; PTHR13312; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Isopeptide bond; Metal-binding;
KW Nucleus; Protease; Reference proteome; Thiol protease; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..301
FT /note="Ubiquitin thioesterase OTU1"
FT /id="PRO_0000202672"
FT DOMAIN 109..229
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT ZN_FING 270..294
FT /note="C2H2-type"
FT REGION 4..80
FT /note="UBX-like"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 114..120
FT /note="Cys-loop"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 169..179
FT /note="Variable-loop"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 218..222
FT /note="His-loop"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 243..248
FT /note="S2 site"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT ACT_SITE 117
FT /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT ACT_SITE 120
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 222
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT ACT_SITE 294
FT /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT CROSSLNK 160
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 120
FT /note="C->S: Loss of function."
FT /evidence="ECO:0000269|PubMed:16427015"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:4KDL"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:4KDL"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:4KDL"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:4KDL"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:4KDL"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:4KDL"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:4KDL"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4KDL"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:4KDL"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:3BY4"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:3BY4"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:3BY4"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:3BY4"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:3BY4"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:3BY4"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:3BY4"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:3BY4"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:3BY4"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:3BY4"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:3BY4"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:3BY4"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:3BY4"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:3BY4"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:3BY4"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:3BY4"
FT HELIX 242..258
FT /evidence="ECO:0007829|PDB:3BY4"
SQ SEQUENCE 301 AA; 33510 MW; 32ABA3CFEA4BB5EB CRC64;
MKLKVTGAGI NQVVTLKQDA TLNDLIEHIN VDVKTMRFGY PPQRINLQGE DASLGQTQLD
ELGINSGEKI TIESSDSNES FSLPPPQPKP KRVLKSTEMS IGGSGENVLS VHPVLDDNSC
LFHAIAYGIF KQDSVRDLRE MVSKEVLNNP VKFNDAILDK PNKDYAQWIL KMESWGGAIE
IGIISDALAV AIYVVDIDAV KIEKFNEDKF DNYILILFNG IHYDSLTMNE FKTVFNKNQP
ESDDVLTAAL QLASNLKQTG YSFNTHKAQI KCNTCQMTFV GEREVARHAE STGHVDFGQN
R
