P42844 (ZIM17_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitochondrial protein import protein ZIM17

Alternative name(s):
Mitochondrial import inner membrane translocase subunit TIM15
mtHsp70 escort protein 1
mtHsp70-associated motor and chaperone protein TIM15/ZIM17
Short name=MMC

Gene names

Name:	ZIM17
Synonyms:	FMP28, HEP1, TIM15
Ordered Locus Names:	YNL310C
ORF Names:	N0381

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	174 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in protein import into mitochondria. Acts as a Hsp70-specific chaperone that prevents self-aggregation of the matrix Hsp70 chaperones SSC1 (mtHSP70) and SSQ1, thereby maintaining their function in mitochondrial protein import and Fe/S protein biosynthesis. May act together with PAM18 as co-chaperone to facilitate recognition and folding of imported proteins by SSC1 in the mitochondrial matrix. Ref.5 Ref.10 Ref.11 Ref.12
Cofactor	Binds 1 zinc ion per subunit.
Subunit structure	Interacts with SSC1; binds to the nucleotide-free state as well as to the ADP- or ATP-bound state of SSC1. Ref.5 Ref.11 Ref.13
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. Note: Soluble matrix protein loosely associated with the inner membrane. Ref.5 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12
Induction	By heat shock (at protein level). Ref.12
Miscellaneous	Present with 1520 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Contains 1 DNL-type zinc finger.
Sequence caution	The sequence AAS56692.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA86385.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA96239.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chaperone
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from physical interaction Ref.5. Source: SGD protein import into mitochondrial matrix Inferred from mutant phenotype Ref.10. Source: SGD protein stabilization Inferred from mutant phenotype. Source: SGD response to unfolded protein Inferred from mutant phenotype Ref.12. Source: SGD
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial matrix Inferred from direct assay Ref.10Ref.12. Source: SGD
Molecular function	chaperone binding Inferred from direct assay Ref.5. Source: SGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 47

47

Mitochondrion Ref.5

Chain

48 – 174

127

Mitochondrial protein import protein ZIM17

PRO_0000203367

Regions

Zinc finger

64 – 159

96

DNL-type

Sites

Metal binding

75

1

Zinc

Metal binding

78

1

Zinc

Metal binding

100

1

Zinc

Metal binding

103

1

Zinc

Experimental info

Mutagenesis

106 – 107

2

RH → AA in TIM15-2RH; Abolishes interaction with SSC1, and leads to self-aggregation of mtHSP70 and accumulation of uncleaved precursor proteins.

Mutagenesis

111

1

D → A: Abolishes interaction with SSC1, and leads to self-aggregation of mtHSP70 and accumulation of uncleaved precursor proteins. Ref.13

Mutagenesis

133 – 137

5

Missing: Temperature sensitive; only partly prevents self-aggregation of mtHSP70 and leads to accumulation of uncleaved precursor proteins at high temperatures. Ref.13

Mutagenesis

140 – 148

9

DLEFEDIPD → ALAFAAIPA in TIM15-5DE; no effect. Ref.13

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

174

Helix Strand Turn

Details...

Beta strand

68 – 75

8

Turn

76 – 79

4

Beta strand

80 – 87

8

Helix

88 – 92

5

Beta strand

96 – 99

4

Beta strand

106 – 109

4

Helix

116 – 118

3

Helix

123 – 129

7

Helix

148 – 153

6

Sequences

	Sequence		Length	Mass (Da)
	P42844 [UniParc]. Last modified February 5, 2008. Version 2. Checksum: 4707DD1CA1490691	FASTA	174	19,855
	10 20 30 40 50 60 MIPRTRTLLQ SKIPITRYFA RCWAPRVRYN VCRTLPAAAL HTNIIAHNEV KKDDKKVHLG 70 80 90 100 110 120 SFKVDKPKMM IAFTCKKCNT RSSHTMSKQA YEKGTVLISC PHCKVRHLIA DHLKIFHDHH 130 140 150 160 170 VTVEQLMKAN GEQVSQDVGD LEFEDIPDSL KDVLGKYAKN NSENASQLPH PSQK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing analysis of a 24.7 kb fragment of yeast chromosome XIV identifies six known genes, a new member of the hexose transporter family and ten new open reading frames." Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C. Yeast 11:1077-1085(1995) [PubMed: 7502583] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / FY1676.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." 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. Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1." Sichting M., Mokranjac D., Azem A., Neupert W., Hell K. EMBO J. 24:1046-1056(2005) [PubMed: 15719019] [Abstract] Cited for: PROTEIN SEQUENCE OF 48-52, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SSC1.
[6]	"Sequencing and comparison of yeast species to identify genes and regulatory elements." Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S. Nature 423:241-254(2003) [PubMed: 12748633] [Abstract] Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[7]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"The proteome of Saccharomyces cerevisiae mitochondria." Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed: 14576278] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
[10]	"Zim17, a novel zinc finger protein essential for protein import into mitochondria." Burri L., Vascotto K., Fredersdorf S., Tiedt R., Hall M.N., Lithgow T. J. Biol. Chem. 279:50243-50249(2004) [PubMed: 15383543] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION OF START CODON.
[11]	"Identification of a novel member of yeast mitochondrial Hsp70-associated motor and chaperone proteins that facilitates protein translocation across the inner membrane." Yamamoto H., Momose T., Yatsukawa Y., Ohshima C., Ishikawa D., Sato T., Tamura Y., Ohwa Y., Endo T. FEBS Lett. 579:507-511(2005) [PubMed: 15642367] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SSC1.
[12]	"Inactivation of the mitochondrial heat shock protein Zim17 leads to aggregation of matrix Hsp70s followed by pleiotropic effects on morphology and protein biogenesis." Sanjuan Szklarz L.K., Guiard B., Rissler M., Wiedemann N., Kozjak V., van der Laan M., Lohaus C., Marcus K., Meyer H.E., Chacinska A., Pfanner N., Meisinger C. J. Mol. Biol. 351:206-218(2005) [PubMed: 15992824] [Abstract] Cited for: FUNCTION, INDUCTION, SUBCELLULAR LOCATION.
[13]	"Structural basis of functional cooperation of Tim15/Zim17 with yeast mitochondrial Hsp70." Momose T., Ohshima C., Maeda M., Endo T. EMBO Rep. 8:664-670(2007) [PubMed: 17571076] [Abstract] Cited for: STRUCTURE BY NMR OF 64-159, INTERACTION WITH SSC1, MUTAGENESIS OF 106-ARG-HIS-107; ASP-111; 133-GLN--ASP-137 AND 140-ASP--ASP-148.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z46259 Genomic DNA. Translation: CAA86385.1. Different initiation.
Z71586 Genomic DNA. Translation: CAA96239.1. Different initiation.
AY558366 Genomic DNA. Translation: AAS56692.1. Different initiation.
BK006947 Genomic DNA. Translation: DAA10251.1.

PIR

S51301.

RefSeq

NP_014089.2. NM_001183148.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E2Z	NMR	-	A	64-159	[»]

ProteinModelPortal

P42844.

SMR

P42844. Positions 60-159.

ModBase

Search...

Protein-protein interaction databases

IntAct

P42844. 17 interactions.

MINT

MINT-2492981.

STRING

P42844.

Proteomic databases

PeptideAtlas

P42844.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YNL310C; YNL310C; YNL310C.

GeneID

855406.

KEGG

sce:YNL310C.

NMPDR

fig|4932.3.peg.5151.

Organism-specific databases

SGD

S000005254. ZIM17.

Phylogenomic databases

eggNOG

fuNOG10120.

GeneTree

EFGT00050000006124.

HOGENOM

HBG448469.

OrthoDB

EOG4QJVXZ.

Gene expression databases

ArrayExpress

P42844.

Genevestigator

P42844.

GermOnline

YNL310C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR024158. Mt_import_TIM15.
IPR007853. Znf_DNL-typ.
[Graphical view]

PANTHER

PTHR20922. Znf_Zim17. 1 hit.

Pfam

PF05180. zf-DNL. 1 hit.
[Graphical view]

PROSITE

PS51501. ZF_DNL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

979241.

Entry information

Entry name

ZIM17_YEAST

Accession

Primary (citable) accession number: P42844
Secondary accession number(s): D6W0N5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	February 5, 2008
Last modified:	December 14, 2011
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program