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 27-MAR-2024, entry version 221. 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}. 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; 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; 967. 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 TCDB; 8.A.192.1.6; the dnaj homolog (dnaj) family. DR iPTMnet; P25491; -. DR MaxQB; P25491; -. DR PaxDb; 4932-YNL064C; -. DR PeptideAtlas; P25491; -. DR EnsemblFungi; YNL064C_mRNA; YNL064C; YNL064C. DR GeneID; 855661; -. DR KEGG; sce:YNL064C; -. DR AGR; SGD:S000005008; -. 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 OrthoDB; 2785358at2759; -. DR BioCyc; YEAST:G3O-33094-MONOMER; -. DR Reactome; R-SCE-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand. DR BioGRID-ORCS; 855661; 0 hits in 10 CRISPR screens. 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; NAS: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:0030544; F:Hsp70 protein binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central. 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 DNA-templated transcription; NAS: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:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0009408; P:response to heat; IEA:InterPro. DR GO; GO:0070482; P:response to oxygen levels; NAS: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; cd10747; DnaJ_C; 1. DR CDD; cd10719; DnaJ_zf; 1. DR Gene3D; 1.10.287.110; DnaJ domain; 1. DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1. DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2. 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:SF10; DNAJ-LIKE-2, ISOFORM A; 1. DR PANTHER; PTHR43888; DNAJ-LIKE-2, ISOFORM A-RELATED; 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; Chaperone J-domain; 1. DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1. DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2. 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 //