ZIM17_YEAST
ID ZIM17_YEAST Reviewed; 174 AA.
AC P42844; D6W0N5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Mitochondrial protein import protein ZIM17;
DE AltName: Full=Mitochondrial import inner membrane translocase subunit TIM15;
DE AltName: Full=mtHsp70 escort protein 1;
DE AltName: Full=mtHsp70-associated motor and chaperone protein TIM15/ZIM17;
DE Short=MMC;
DE Flags: Precursor;
GN Name=ZIM17; Synonyms=FMP28, HEP1, TIM15; OrderedLocusNames=YNL310C;
GN ORFNames=N0381;
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].
RC STRAIN=S288c / FY1676;
RX PubMed=7502583; DOI=10.1002/yea.320111109;
RA Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.;
RT "Sequencing analysis of a 24.7 kb fragment of yeast chromosome XIV
RT identifies six known genes, a new member of the hexose transporter family
RT and ten new open reading frames.";
RL Yeast 11:1077-1085(1995).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP PROTEIN SEQUENCE OF 48-52, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH SSC1.
RX PubMed=15719019; DOI=10.1038/sj.emboj.7600580;
RA Sichting M., Mokranjac D., Azem A., Neupert W., Hell K.;
RT "Maintenance of structure and function of mitochondrial Hsp70 chaperones
RT requires the chaperone Hep1.";
RL EMBO J. 24:1046-1056(2005).
RN [6]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [7]
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 [8]
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 [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION OF START CODON.
RX PubMed=15383543; DOI=10.1074/jbc.m409194200;
RA Burri L., Vascotto K., Fredersdorf S., Tiedt R., Hall M.N., Lithgow T.;
RT "Zim17, a novel zinc finger protein essential for protein import into
RT mitochondria.";
RL J. Biol. Chem. 279:50243-50249(2004).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SSC1.
RX PubMed=15642367; DOI=10.1016/j.febslet.2004.12.018;
RA Yamamoto H., Momose T., Yatsukawa Y., Ohshima C., Ishikawa D., Sato T.,
RA Tamura Y., Ohwa Y., Endo T.;
RT "Identification of a novel member of yeast mitochondrial Hsp70-associated
RT motor and chaperone proteins that facilitates protein translocation across
RT the inner membrane.";
RL FEBS Lett. 579:507-511(2005).
RN [12]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15992824; DOI=10.1016/j.jmb.2005.05.068;
RA Sanjuan Szklarz L.K., Guiard B., Rissler M., Wiedemann N., Kozjak V.,
RA van der Laan M., Lohaus C., Marcus K., Meyer H.E., Chacinska A.,
RA Pfanner N., Meisinger C.;
RT "Inactivation of the mitochondrial heat shock protein Zim17 leads to
RT aggregation of matrix Hsp70s followed by pleiotropic effects on morphology
RT and protein biogenesis.";
RL J. Mol. Biol. 351:206-218(2005).
RN [13]
RP STRUCTURE BY NMR OF 64-159, INTERACTION WITH SSC1, AND MUTAGENESIS OF
RP 106-ARG-HIS-107; ASP-111; 133-GLN--ASP-137 AND 140-ASP--ASP-148.
RX PubMed=17571076; DOI=10.1038/sj.embor.7400990;
RA Momose T., Ohshima C., Maeda M., Endo T.;
RT "Structural basis of functional cooperation of Tim15/Zim17 with yeast
RT mitochondrial Hsp70.";
RL EMBO Rep. 8:664-670(2007).
CC -!- FUNCTION: Involved in protein import into mitochondria. Acts as a
CC Hsp70-specific chaperone that prevents self-aggregation of the matrix
CC Hsp70 chaperones SSC1 (mtHSP70) and SSQ1, thereby maintaining their
CC function in mitochondrial protein import and Fe/S protein biosynthesis.
CC May act together with PAM18 as co-chaperone to facilitate recognition
CC and folding of imported proteins by SSC1 in the mitochondrial matrix.
CC {ECO:0000269|PubMed:15383543, ECO:0000269|PubMed:15642367,
CC ECO:0000269|PubMed:15719019, ECO:0000269|PubMed:15992824}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- SUBUNIT: Interacts with SSC1; binds to the nucleotide-free state as
CC well as to the ADP- or ATP-bound state of SSC1.
CC {ECO:0000269|PubMed:15642367, ECO:0000269|PubMed:15719019,
CC ECO:0000269|PubMed:17571076}.
CC -!- INTERACTION:
CC P42844; P0CS91: SSC1; Xeno; NbExp=2; IntAct=EBI-28366, EBI-7276682;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:15383543, ECO:0000269|PubMed:15642367,
CC ECO:0000269|PubMed:15719019, ECO:0000269|PubMed:15992824}; Peripheral
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15383543,
CC ECO:0000269|PubMed:15642367, ECO:0000269|PubMed:15719019,
CC ECO:0000269|PubMed:15992824}; Matrix side {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15383543,
CC ECO:0000269|PubMed:15642367, ECO:0000269|PubMed:15719019,
CC ECO:0000269|PubMed:15992824}. Note=Soluble matrix protein loosely
CC associated with the inner membrane.
CC -!- INDUCTION: By heat shock (at protein level).
CC {ECO:0000269|PubMed:15992824}.
CC -!- MISCELLANEOUS: Present with 1520 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS56692.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA86385.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA96239.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z46259; CAA86385.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z71586; CAA96239.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY558366; AAS56692.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006947; DAA10251.1; -; Genomic_DNA.
DR PIR; S51301; S51301.
DR RefSeq; NP_014089.2; NM_001183148.1.
DR PDB; 2E2Z; NMR; -; A=64-159.
DR PDBsum; 2E2Z; -.
DR AlphaFoldDB; P42844; -.
DR SMR; P42844; -.
DR BioGRID; 35529; 15.
DR IntAct; P42844; 18.
DR MINT; P42844; -.
DR STRING; 4932.YNL310C; -.
DR MaxQB; P42844; -.
DR PaxDb; P42844; -.
DR PRIDE; P42844; -.
DR DNASU; 855406; -.
DR EnsemblFungi; YNL310C_mRNA; YNL310C; YNL310C.
DR GeneID; 855406; -.
DR KEGG; sce:YNL310C; -.
DR SGD; S000005254; ZIM17.
DR VEuPathDB; FungiDB:YNL310C; -.
DR eggNOG; KOG3277; Eukaryota.
DR GeneTree; ENSGT00390000008220; -.
DR HOGENOM; CLU_093902_1_0_1; -.
DR InParanoid; P42844; -.
DR OMA; MIPRTRT; -.
DR BioCyc; YEAST:G3O-33297-MON; -.
DR EvolutionaryTrace; P42844; -.
DR PRO; PR:P42844; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P42844; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0051087; F:chaperone binding; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
DR GO; GO:0006457; P:protein folding; IMP:SGD.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:SGD.
DR GO; GO:0050821; P:protein stabilization; IMP:SGD.
DR GO; GO:0006986; P:response to unfolded protein; IMP:SGD.
DR InterPro; IPR024158; Mt_import_TIM15.
DR InterPro; IPR007853; Znf_DNL-typ.
DR PANTHER; PTHR20922; PTHR20922; 1.
DR Pfam; PF05180; zf-DNL; 1.
DR PROSITE; PS51501; ZF_DNL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Direct protein sequencing; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Protein transport; Reference proteome; Transit peptide; Transport; Zinc;
KW Zinc-finger.
FT TRANSIT 1..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:15719019"
FT CHAIN 48..174
FT /note="Mitochondrial protein import protein ZIM17"
FT /id="PRO_0000203367"
FT ZN_FING 64..159
FT /note="DNL-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT MUTAGEN 106..107
FT /note="RH->AA: In TIM15-2RH; Abolishes interaction with
FT SSC1, and leads to self-aggregation of mtHSP70 and
FT accumulation of uncleaved precursor proteins."
FT /evidence="ECO:0000269|PubMed:17571076"
FT MUTAGEN 111
FT /note="D->A: Abolishes interaction with SSC1, and leads to
FT self-aggregation of mtHSP70 and accumulation of uncleaved
FT precursor proteins."
FT /evidence="ECO:0000269|PubMed:17571076"
FT MUTAGEN 133..137
FT /note="Missing: Temperature sensitive; only partly prevents
FT self-aggregation of mtHSP70 and leads to accumulation of
FT uncleaved precursor proteins at high temperatures."
FT /evidence="ECO:0000269|PubMed:17571076"
FT MUTAGEN 140..148
FT /note="DLEFEDIPD->ALAFAAIPA: In TIM15-5DE; no effect."
FT /evidence="ECO:0000269|PubMed:17571076"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:2E2Z"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:2E2Z"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:2E2Z"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:2E2Z"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:2E2Z"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:2E2Z"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2E2Z"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:2E2Z"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:2E2Z"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:2E2Z"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:2E2Z"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:2E2Z"
SQ SEQUENCE 174 AA; 19855 MW; 4707DD1CA1490691 CRC64;
MIPRTRTLLQ SKIPITRYFA RCWAPRVRYN VCRTLPAAAL HTNIIAHNEV KKDDKKVHLG
SFKVDKPKMM IAFTCKKCNT RSSHTMSKQA YEKGTVLISC PHCKVRHLIA DHLKIFHDHH
VTVEQLMKAN GEQVSQDVGD LEFEDIPDSL KDVLGKYAKN NSENASQLPH PSQK
