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Mitochondrial protein import protein MAS5 (Yeast dnaJ protein 1)

 MAS5_YEAST              Reviewed;         409 AA.
P25491; D6W1B6;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
25-OCT-2017, entry version 179.
RecName: Full=Mitochondrial protein import protein MAS5;
AltName: Full=Yeast dnaJ protein 1;
Flags: Precursor;
Name=YDJ1; Synonyms=MAS5; OrderedLocusNames=YNL064C;
ORFNames=N2418, YNL2418C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
PubMed=1869583; DOI=10.1083/jcb.114.4.609;
Caplan A.J., Douglas M.G.;
"Characterization of YDJ1: a yeast homologue of the bacterial dnaJ
protein.";
J. Cell Biol. 114:609-621(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1729605; DOI=10.1128/MCB.12.1.283;
Atencio D.P., Yaffe M.P.;
"MAS5, a yeast homolog of DnaJ involved in mitochondrial protein
import.";
Mol. Cell. Biol. 12:283-291(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=S288c / FY1676;
PubMed=8533472; DOI=10.1002/yea.320111008;
Bergez P., Doignon F., Crouzet M.;
"The sequence of a 44 420 bp fragment located on the left arm of
chromosome XIV from Saccharomyces cerevisiae.";
Yeast 11:967-974(1995).
[4]
ERRATUM.
PubMed=8904343;
DOI=10.1002/(SICI)1097-0061(19960315)12:3<297::AID-YEA940>3.0.CO;2-D;
Bergez P., Doignon F., Crouzet M.;
Yeast 12:297-297(1996).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[6]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[7]
ISOPRENYLATION AT CYS-406.
PubMed=1527016;
Caplan A.J., Tsai J., Casey P.J., Douglas M.G.;
"Farnesylation of YDJ1p is required for function at elevated growth
temperatures in Saccharomyces cerevisiae.";
J. Biol. Chem. 267:18890-18895(1992).
[8]
FUNCTION, AND SUBUNIT.
PubMed=11689685; DOI=10.1128/MCB.21.23.7923-7932.2001;
Hon T., Lee H.C., Hach A., Johnson J.L., Craig E.A.,
Erdjument-Bromage H., Tempst P., Zhang L.;
"The Hsp70-Ydj1 molecular chaperone represses the activity of the heme
activator protein Hap1 in the absence of heme.";
Mol. Cell. Biol. 21:7923-7932(2001).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[12]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-198, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[13]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 103-350 IN COMPLEX WITH
SUBSTRATE ANALOGS, SUBUNIT, AND MUTAGENESIS OF PHE-335.
PubMed=14656432; DOI=10.1016/j.str.2003.10.012;
Li J., Qian X., Sha B.;
"The crystal structure of the yeast Hsp40 Ydj1 complexed with its
peptide substrate.";
Structure 11:1475-1483(2003).
[14]
X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 258-378.
PubMed=15701512; DOI=10.1016/j.jmb.2004.12.040;
Wu Y., Li J., Jin Z., Fu Z., Sha B.;
"The crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1
reveals novel dimerization motif for Hsp40.";
J. Mol. Biol. 346:1005-1011(2005).
-!- FUNCTION: Probably involved in mitochondrial protein import. Is
also required for efficient translocation of pre-pro-alpha-factor.
Involved in heme regulation of HAP1, as a component of the high-
molecular-weight (HMC) complex. {ECO:0000269|PubMed:11689685}.
-!- SUBUNIT: Homodimer. Interacts with HAP1. Component of the HMC
including HAP1, SRO9 and YDJ1. {ECO:0000269|PubMed:11689685,
ECO:0000269|PubMed:14656432}.
-!- INTERACTION:
Q12285:MDY2; NbExp=2; IntAct=EBI-10420, EBI-34904;
Q12118:SGT2; NbExp=2; IntAct=EBI-10420, EBI-31784;
Q7LKB1:SUP35 (xeno); NbExp=3; IntAct=EBI-10420, EBI-8411471;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
Note=Concentrated in a perinuclear ring as well as in the
cytoplasm.
-!- INDUCTION: YDJ1 is a heat shock gene whose expression increases
moderately at elevated temperatures.
-!- MISCELLANEOUS: Present with 119000 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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EMBL; X56560; CAA39910.1; -; Genomic_DNA.
EMBL; S74758; AAB20771.1; -; Genomic_DNA.
EMBL; U12141; AAA99647.1; -; Genomic_DNA.
EMBL; Z71340; CAA95937.1; -; Genomic_DNA.
EMBL; BK006947; DAA10482.1; -; Genomic_DNA.
PIR; S26703; S26703.
RefSeq; NP_014335.1; NM_001182902.1.
PDB; 1NLT; X-ray; 2.70 A; A=103-350.
PDB; 1XAO; X-ray; 2.07 A; A/B=258-378.
PDBsum; 1NLT; -.
PDBsum; 1XAO; -.
ProteinModelPortal; P25491; -.
SMR; P25491; -.
BioGrid; 35759; 841.
DIP; DIP-2251N; -.
IntAct; P25491; 112.
MINT; MINT-603538; -.
STRING; 4932.YNL064C; -.
iPTMnet; P25491; -.
MaxQB; P25491; -.
PRIDE; P25491; -.
EnsemblFungi; YNL064C; YNL064C; YNL064C.
GeneID; 855661; -.
KEGG; sce:YNL064C; -.
EuPathDB; FungiDB:YNL064C; -.
SGD; S000005008; YDJ1.
GeneTree; ENSGT00860000133716; -.
HOGENOM; HOG000226718; -.
InParanoid; P25491; -.
KO; K09503; -.
OMA; CDGHGMK; -.
OrthoDB; EOG092C1UGR; -.
BioCyc; YEAST:G3O-33094-MONOMER; -.
Reactome; R-SCE-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
EvolutionaryTrace; P25491; -.
PRO; PR:P25491; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:SGD.
GO; GO:0072380; C:TRC complex; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0001671; F:ATPase activator activity; IDA:SGD.
GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
GO; GO:0006458; P:'de novo' protein folding; IMP:SGD.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:CAFA.
GO; GO:0042026; P:protein refolding; IDA:SGD.
GO; GO:0045047; P:protein targeting to ER; IMP:SGD.
GO; GO:0006626; P:protein targeting to mitochondrion; IMP:SGD.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:SGD.
GO; GO:0009408; P:response to heat; IEA:InterPro.
GO; GO:0035719; P:tRNA import into nucleus; IMP:SGD.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
CDD; cd06257; DnaJ; 1.
CDD; cd10719; DnaJ_zf; 1.
Gene3D; 1.10.287.110; -; 1.
HAMAP; MF_01152; DnaJ; 1.
InterPro; IPR012724; DnaJ.
InterPro; IPR002939; DnaJ_C.
InterPro; IPR036869; DnaJ_dom_sf.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR018253; DnaJ_domain_CS.
InterPro; IPR008971; HSP40/DnaJ_pept-bd.
InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
Pfam; PF00226; DnaJ; 1.
Pfam; PF01556; DnaJ_C; 1.
Pfam; PF00684; DnaJ_CXXCXGXG; 1.
PRINTS; PR00625; JDOMAIN.
SMART; SM00271; DnaJ; 1.
SUPFAM; SSF46565; SSF46565; 1.
SUPFAM; SSF49493; SSF49493; 3.
SUPFAM; SSF57938; SSF57938; 1.
PROSITE; PS00636; DNAJ_1; 1.
PROSITE; PS50076; DNAJ_2; 1.
PROSITE; PS51188; ZF_CR; 1.
1: Evidence at protein level;
3D-structure; Chaperone; Complete proteome; Cytoplasm;
Isopeptide bond; Lipoprotein; Metal-binding; Methylation; Prenylation;
Protein transport; Reference proteome; Repeat; Stress response;
Transport; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 406 Mitochondrial protein import protein
MAS5.
/FTId=PRO_0000071093.
PROPEP 407 409 Removed in mature form. {ECO:0000305}.
/FTId=PRO_0000396684.
DOMAIN 4 72 J.
REPEAT 143 150 CXXCXGXG motif.
REPEAT 159 166 CXXCXGXG motif.
REPEAT 185 192 CXXCXGXG motif.
REPEAT 201 208 CXXCXGXG motif.
ZN_FING 130 213 CR-type.
REGION 1 172 Necessary for HAP1 repression in the
absence of heme.
REGION 135 137 Substrate binding.
REGION 215 216 Substrate binding.
REGION 247 249 Substrate binding.
COMPBIAS 73 103 Gly-rich.
METAL 143 143 Zinc 1.
METAL 146 146 Zinc 1.
METAL 159 159 Zinc 2.
METAL 162 162 Zinc 2.
METAL 185 185 Zinc 2.
METAL 188 188 Zinc 2.
METAL 201 201 Zinc 1.
METAL 204 204 Zinc 1.
BINDING 116 116 Substrate; via amide nitrogen.
SITE 335 335 Involved in dimerization.
MOD_RES 406 406 Cysteine methyl ester. {ECO:0000305}.
LIPID 406 406 S-farnesyl cysteine.
{ECO:0000269|PubMed:1527016}.
CROSSLNK 198 198 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 335 335 F->D: Prevents dimerization.
{ECO:0000269|PubMed:14656432}.
STRAND 116 122 {ECO:0000244|PDB:1NLT}.
HELIX 126 129 {ECO:0000244|PDB:1NLT}.
STRAND 131 142 {ECO:0000244|PDB:1NLT}.
TURN 144 148 {ECO:0000244|PDB:1NLT}.
STRAND 150 152 {ECO:0000244|PDB:1NLT}.
TURN 153 155 {ECO:0000244|PDB:1NLT}.
STRAND 162 166 {ECO:0000244|PDB:1NLT}.
STRAND 168 182 {ECO:0000244|PDB:1NLT}.
STRAND 189 193 {ECO:0000244|PDB:1NLT}.
STRAND 202 204 {ECO:0000244|PDB:1NLT}.
STRAND 209 220 {ECO:0000244|PDB:1NLT}.
STRAND 229 232 {ECO:0000244|PDB:1NLT}.
STRAND 247 253 {ECO:0000244|PDB:1NLT}.
STRAND 260 262 {ECO:0000244|PDB:1XAO}.
STRAND 265 273 {ECO:0000244|PDB:1XAO}.
HELIX 274 279 {ECO:0000244|PDB:1XAO}.
STRAND 281 286 {ECO:0000244|PDB:1XAO}.
STRAND 288 290 {ECO:0000244|PDB:1NLT}.
STRAND 292 297 {ECO:0000244|PDB:1XAO}.
TURN 299 302 {ECO:0000244|PDB:1NLT}.
STRAND 308 311 {ECO:0000244|PDB:1XAO}.
STRAND 319 321 {ECO:0000244|PDB:1NLT}.
STRAND 327 334 {ECO:0000244|PDB:1XAO}.
HELIX 343 352 {ECO:0000244|PDB:1XAO}.
STRAND 367 371 {ECO:0000244|PDB:1XAO}.
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


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