MAS5_YEAST
ID MAS5_YEAST Reviewed; 409 AA.
AC P25491; D6W1B6;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Mitochondrial protein import protein MAS5;
DE AltName: Full=Yeast dnaJ protein 1;
DE Flags: Precursor;
GN Name=YDJ1; Synonyms=MAS5; OrderedLocusNames=YNL064C;
GN ORFNames=N2418, YNL2418C;
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 [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=1869583; DOI=10.1083/jcb.114.4.609;
RA Caplan A.J., Douglas M.G.;
RT "Characterization of YDJ1: a yeast homologue of the bacterial dnaJ
RT protein.";
RL J. Cell Biol. 114:609-621(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1729605; DOI=10.1128/mcb.12.1.283-291.1992;
RA Atencio D.P., Yaffe M.P.;
RT "MAS5, a yeast homolog of DnaJ involved in mitochondrial protein import.";
RL Mol. Cell. Biol. 12:283-291(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1676;
RX PubMed=8533472; DOI=10.1002/yea.320111008;
RA Bergez P., Doignon F., Crouzet M.;
RT "The sequence of a 44 420 bp fragment located on the left arm of chromosome
RT XIV from Saccharomyces cerevisiae.";
RL Yeast 11:967-974(1995).
RN [4]
RP ERRATUM OF PUBMED:8533472.
RX PubMed=8904343;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<297::aid-yea940>3.0.co;2-d;
RA Bergez P., Doignon F., Crouzet M.;
RL Yeast 12:297-297(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [6]
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 [7]
RP ISOPRENYLATION AT CYS-406.
RX PubMed=1527016; DOI=10.1016/s0021-9258(19)37044-9;
RA Caplan A.J., Tsai J., Casey P.J., Douglas M.G.;
RT "Farnesylation of YDJ1p is required for function at elevated growth
RT temperatures in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 267:18890-18895(1992).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11689685; DOI=10.1128/mcb.21.23.7923-7932.2001;
RA Hon T., Lee H.C., Hach A., Johnson J.L., Craig E.A., Erdjument-Bromage H.,
RA Tempst P., Zhang L.;
RT "The Hsp70-Ydj1 molecular chaperone represses the activity of the heme
RT activator protein Hap1 in the absence of heme.";
RL Mol. Cell. Biol. 21:7923-7932(2001).
RN [9]
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 [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-198, 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).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 103-350 IN COMPLEX WITH SUBSTRATE
RP ANALOGS, SUBUNIT, AND MUTAGENESIS OF PHE-335.
RX PubMed=14656432; DOI=10.1016/j.str.2003.10.012;
RA Li J., Qian X., Sha B.;
RT "The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide
RT substrate.";
RL Structure 11:1475-1483(2003).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 258-378.
RX PubMed=15701512; DOI=10.1016/j.jmb.2004.12.040;
RA Wu Y., Li J., Jin Z., Fu Z., Sha B.;
RT "The crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1
RT reveals novel dimerization motif for Hsp40.";
RL J. Mol. Biol. 346:1005-1011(2005).
CC -!- FUNCTION: Probably involved in mitochondrial protein import. Is also
CC required for efficient translocation of pre-pro-alpha-factor. Involved
CC in heme regulation of HAP1, as a component of the high-molecular-weight
CC (HMC) complex. {ECO:0000269|PubMed:11689685}.
CC -!- SUBUNIT: Homodimer. Interacts with HAP1. Component of the HMC including
CC HAP1, SRO9 and YDJ1. {ECO:0000269|PubMed:11689685,
CC ECO:0000269|PubMed:14656432}.
CC -!- INTERACTION:
CC P25491; Q12285: MDY2; NbExp=2; IntAct=EBI-10420, EBI-34904;
CC P25491; Q12118: SGT2; NbExp=2; IntAct=EBI-10420, EBI-31784;
CC P25491; Q7LKB1: SUP35; Xeno; NbExp=3; IntAct=EBI-10420, EBI-8411471;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC Note=Concentrated in a perinuclear ring as well as in the cytoplasm.
CC -!- INDUCTION: YDJ1 is a heat shock gene whose expression increases
CC moderately at elevated temperatures.
CC -!- MISCELLANEOUS: Present with 119000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; X56560; CAA39910.1; -; Genomic_DNA.
DR EMBL; S74758; AAB20771.1; -; Genomic_DNA.
DR EMBL; U12141; AAA99647.1; -; Genomic_DNA.
DR EMBL; Z71340; CAA95937.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10482.1; -; Genomic_DNA.
DR PIR; S26703; S26703.
DR RefSeq; NP_014335.1; NM_001182902.1.
DR PDB; 1NLT; X-ray; 2.70 A; A=103-350.
DR PDB; 1XAO; X-ray; 2.07 A; A/B=258-378.
DR PDB; 5VSO; NMR; -; A=1-70.
DR PDBsum; 1NLT; -.
DR PDBsum; 1XAO; -.
DR PDBsum; 5VSO; -.
DR AlphaFoldDB; P25491; -.
DR SMR; P25491; -.
DR BioGRID; 35759; 933.
DR ComplexPortal; CPX-1276; HMC complex.
DR ComplexPortal; CPX-1882; HAP1 transcriptional repressor complex, SSA1 variant.
DR ComplexPortal; CPX-1883; HAP1 transcriptional repressor complex, SSA2 variant.
DR DIP; DIP-2251N; -.
DR IntAct; P25491; 113.
DR MINT; P25491; -.
DR STRING; 4932.YNL064C; -.
DR iPTMnet; P25491; -.
DR MaxQB; P25491; -.
DR PaxDb; P25491; -.
DR PRIDE; P25491; -.
DR EnsemblFungi; YNL064C_mRNA; YNL064C; YNL064C.
DR GeneID; 855661; -.
DR KEGG; sce:YNL064C; -.
DR SGD; S000005008; YDJ1.
DR VEuPathDB; FungiDB:YNL064C; -.
DR eggNOG; KOG0712; Eukaryota.
DR GeneTree; ENSGT00940000154688; -.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; P25491; -.
DR OMA; RVCPTCV; -.
DR BioCyc; YEAST:G3O-33094-MON; -.
DR Reactome; R-SCE-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR EvolutionaryTrace; P25491; -.
DR PRO; PR:P25491; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P25491; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:SGD.
DR GO; GO:0017053; C:transcription repressor complex; IC:ComplexPortal.
DR GO; GO:0072380; C:TRC complex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0001671; F:ATPase activator activity; IDA:SGD.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0006458; P:'de novo' protein folding; IMP:SGD.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:CAFA.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042026; P:protein refolding; IDA:SGD.
DR GO; GO:0045047; P:protein targeting to ER; IMP:SGD.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IMP:SGD.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR GO; GO:0070482; P:response to oxygen levels; IC:ComplexPortal.
DR GO; GO:0035719; P:tRNA import into nucleus; IMP:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR HAMAP; MF_01152; DnaJ; 1.
DR InterPro; IPR012724; DnaJ.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR044713; DNJA1/2-like.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR43888; PTHR43888; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR SUPFAM; SSF57938; SSF57938; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Isopeptide bond; Lipoprotein;
KW Metal-binding; Methylation; Prenylation; Protein transport;
KW Reference proteome; Repeat; Stress response; Transport; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..406
FT /note="Mitochondrial protein import protein MAS5"
FT /id="PRO_0000071093"
FT PROPEP 407..409
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000396684"
FT DOMAIN 4..72
FT /note="J"
FT REPEAT 143..150
FT /note="CXXCXGXG motif"
FT REPEAT 159..166
FT /note="CXXCXGXG motif"
FT REPEAT 185..192
FT /note="CXXCXGXG motif"
FT REPEAT 201..208
FT /note="CXXCXGXG motif"
FT ZN_FING 130..213
FT /note="CR-type"
FT REGION 1..172
FT /note="Necessary for HAP1 repression in the absence of
FT heme"
FT REGION 382..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 116
FT /ligand="substrate"
FT BINDING 135..137
FT /ligand="substrate"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 215..216
FT /ligand="substrate"
FT BINDING 247..249
FT /ligand="substrate"
FT SITE 335
FT /note="Involved in dimerization"
FT MOD_RES 406
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 406
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:1527016"
FT CROSSLNK 198
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 335
FT /note="F->D: Prevents dimerization."
FT /evidence="ECO:0000269|PubMed:14656432"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:5VSO"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:5VSO"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:5VSO"
FT HELIX 41..57
FT /evidence="ECO:0007829|PDB:5VSO"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:5VSO"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:1NLT"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:1NLT"
FT STRAND 131..142
FT /evidence="ECO:0007829|PDB:1NLT"
FT TURN 144..148
FT /evidence="ECO:0007829|PDB:1NLT"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1NLT"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:1NLT"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1NLT"
FT STRAND 168..182
FT /evidence="ECO:0007829|PDB:1NLT"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:1NLT"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1NLT"
FT STRAND 209..220
FT /evidence="ECO:0007829|PDB:1NLT"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:1NLT"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:1NLT"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:1XAO"
FT STRAND 265..273
FT /evidence="ECO:0007829|PDB:1XAO"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:1XAO"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:1XAO"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:1NLT"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:1XAO"
FT TURN 299..302
FT /evidence="ECO:0007829|PDB:1NLT"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:1XAO"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:1NLT"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:1XAO"
FT HELIX 343..352
FT /evidence="ECO:0007829|PDB:1XAO"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:1XAO"
SQ SEQUENCE 409 AA; 44671 MW; E4539F3618DD9CF2 CRC64;
MVKETKFYDI LGVPVTATDV EIKKAYRKCA LKYHPDKNPS EEAAEKFKEA SAAYEILSDP
EKRDIYDQFG EDGLSGAGGA GGFPGGGFGF GDDIFSQFFG AGGAQRPRGP QRGKDIKHEI
SASLEELYKG RTAKLALNKQ ILCKECEGRG GKKGAVKKCT SCNGQGIKFV TRQMGPMIQR
FQTECDVCHG TGDIIDPKDR CKSCNGKKVE NERKILEVHV EPGMKDGQRI VFKGEADQAP
DVIPGDVVFI VSERPHKSFK RDGDDLVYEA EIDLLTAIAG GEFALEHVSG DWLKVGIVPG
EVIAPGMRKV IEGKGMPIPK YGGYGNLIIK FTIKFPENHF TSEENLKKLE EILPPRIVPA
IPKKATVDEC VLADFDPAKY NRTRASRGGA NYDSDEEEQG GEGVQCASQ
