P07213 (TOM70_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitochondrial import receptor subunit TOM70

Alternative name(s):
70 kDa mitochondrial outer membrane protein
Translocase of outer membrane 70 kDa subunit

Gene names

Name:	TOM70
Synonyms:	MAS70, OMP1
Ordered Locus Names:	YNL121C
ORF Names:	N1905

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	617 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the TOM (translocase of outer membrane) receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM20 and TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore. Ref.11
Subunit structure	Forms part of the TOM (translocase of outer membrane) complex that consists of at least 7 different proteins (TOM5, TOM6, TOM7, TOM20, TOM22, TOM40 and TOM70). In the complex interacts with TOM22. Interacts with TOM37. Ref.9 Ref.10
Subcellular location	Mitochondrion outer membrane; Single-pass membrane protein Ref.12.
Miscellaneous	Present with 45300 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the Tom70 family. Contains 9 TPR repeats.

Ontologies

Keywords
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Domain	Repeat TPR repeat Transmembrane Transmembrane helix
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein import into mitochondrial inner membrane Inferred from mutant phenotype PubMed 2177474. Source: SGD protein import into mitochondrial matrix Inferred from mutant phenotype PubMed 8132642. Source: SGD
Cellular_component	integral to mitochondrial outer membrane Inferred from direct assay PubMed 16689936. Source: SGD mitochondrial outer membrane translocase complex Inferred from direct assay Ref.9. Source: SGD
Molecular_function	P-P-bond-hydrolysis-driven protein transmembrane transporter activity Inferred from electronic annotation. Source: InterPro mitochondrion targeting sequence binding Inferred from mutant phenotype Ref.11. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 617

617

Mitochondrial import receptor subunit TOM70

PRO_0000106340

Regions

Topological domain

1 – 10

10

Mitochondrial intermembrane Potential

Transmembrane

11 – 30

20

Helical; Potential

Topological domain

31 – 617

587

Cytoplasmic Potential

Repeat

99 – 132

34

TPR 1

Repeat

134 – 165

32

TPR 2

Repeat

281 – 315

35

TPR 3

Repeat

363 – 396

34

TPR 4

Repeat

397 – 430

34

TPR 5

Repeat

432 – 464

33

TPR 6

Repeat

465 – 498

34

TPR 7

Repeat

505 – 541

37

TPR 8

Repeat

542 – 575

34

TPR 9

Amino acid modifications

Modified residue

78

1

Phosphoserine Ref.16

Modified residue

174

1

Phosphoserine Ref.14 Ref.15 Ref.16

Modified residue

232

1

Phosphothreonine Ref.16

Modified residue

234

1

Phosphothreonine Ref.16

Natural variations

Natural variant

30

1

N → S in strain: SK1, V1-09, YJM339 and YJM627. Ref.2

Natural variant

68

1

P → S in strain: V1-09 and YJM627. Ref.2

Natural variant

277

1

N → H in strain: YJM1129. Ref.2

Natural variant

359

1

L → S in strain: SK1. Ref.2

Natural variant

364

1

N → I in strain: YJM269 and YJM270. Ref.2

Natural variant

385

1

Y → H in strain: YJM1129. Ref.2

Natural variant

429

1

E → G in ytrain: V1-09. Ref.2

Experimental info

Sequence conflict

185

1

A → R in CAA29085. Ref.1

Secondary structure

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617

Helix Strand Turn

Details...

Helix

95 – 111

17

Helix

115 – 128

14

Helix

132 – 145

14

Helix

148 – 161

14

Helix

166 – 178

13

Helix

182 – 194

13

Beta strand

195 – 197

3

Helix

200 – 202

3

Helix

204 – 219

16

Helix

254 – 261

8

Helix

278 – 290

13

Helix

297 – 315

19

Turn

316 – 318

3

Helix

323 – 342

20

Helix

346 – 359

14

Helix

363 – 374

12

Helix

382 – 384

3

Helix

385 – 390

6

Helix

398 – 409

12

Helix

415 – 425

11

Helix

432 – 440

9

Turn

441 – 445

5

Helix

447 – 460

14

Helix

466 – 477

12

Helix

481 – 496

16

Beta strand

498 – 500

3

Helix

506 – 516

11

Helix

523 – 537

15

Helix

542 – 554

13

Helix

558 – 571

14

Helix

575 – 594

20

Helix

598 – 605

8

Sequences

	Sequence		Length	Mass (Da)
	P07213 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 664B8FC32CCE39A2	FASTA	617	70,123
	10 20 30 40 50 60 MKSFITRNKT AILATVAATG TAIGAYYYYN QLQQQQQRGK KNTINKDEKK DTKDSQKETE 70 80 90 100 110 120 GAKKSTAPSN PPIYPVSSNG EPDFSNKANF TAEEKDKYAL ALKDKGNQFF RNKKYDDAIK 130 140 150 160 170 180 YYNWALELKE DPVFYSNLSA CYVSVGDLKK VVEMSTKALE LKPDYSKVLL RRASANEGLG 190 200 210 220 230 240 KFADAMFDLS VLSLNGDFND ASIEPMLERN LNKQAMSKLK EKFGDIDTAT ATPTELSTQP 250 260 270 280 290 300 AKERKDKQEN LPSVTSMASF FGIFKPELTF ANYDESNEAD KELMNGLSNL YKRSPESYDK 310 320 330 340 350 360 ADESFTKAAR LFEEQLDKNN EDEKLKEKLA ISLEHTGIFK FLKNDPLGAH EDIKKAIELF 370 380 390 400 410 420 PRVNSYIYMA LIMADRNDST EYYNYFDKAL KLDSNNSSVY YHRGQMNFIL QNYDQAGKDF 430 440 450 460 470 480 DKAKELDPEN IFPYIQLACL AYRENKFDDC ETLFSEAKRK FPEAPEVPNF FAEILTDKND 490 500 510 520 530 540 FDKALKQYDL AIELENKLDG IYVGIAPLVG KATLLTRNPT VENFIEATNL LEKASKLDPR 550 560 570 580 590 600 SEQAKIGLAQ MKLQQEDIDE AITLFEESAD LARTMEEKLQ AITFAEAAKV QQRIRSDPVL 610 AKKIQETLAK LREQGLM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Import of proteins into mitochondria: nucleotide sequence of the gene for a 70-kd protein of the yeast mitochondrial outer membrane." Hase T., Riezman H., Suda K., Schatz G. EMBO J. 2:2169-2172(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequential elimination of major-effect contributors identifies additional quantitative trait loci conditioning high-temperature growth in yeast." Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S., Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H., Steinmetz L.M. Genetics 180:1661-1670(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-30; SER-68; HIS-277; SER-359; ILE-364; HIS-385 AND GLY-429. Strain: ATCC 200060 / W303, S103, SK1, V1-09, YJM 1129, YJM 269, YJM 270, YJM 320, YJM 326, YJM 339, YJM 627 and YJM230.
[3]	"The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces cerevisiae reveals an unusually high number of overlapping open reading frames." de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D., Pallavicini A., Lanfranchi G., Valle G. Yeast 13:261-266(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Expanding family." Boguski M.S., Sikorski R.S., Hieter P.A., Goebl M. Nature 346:114-114(1990) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAINS TPR REPEATS.
[7]	"Protein import into yeast mitochondria is accelerated by the outer membrane protein MAS70." Hines V., Brandt A., Griffiths G., Horstmann H., Brutsch H., Schatz G. EMBO J. 9:3191-3200(1990) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Precursor binding to yeast mitochondria. A general role for the outer membrane protein Mas70p." Hines V., Schatz G. J. Biol. Chem. 268:449-454(1993) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[9]	"Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex." Dekker P.J.T., Ryan M.T., Brix J., Mueller H., Hoenlinger A., Pfanner N. Mol. Cell. Biol. 18:6515-6524(1998) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE TOM COMPLEX.
[10]	"Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase." van Wilpe S., Ryan M.T., Hill K., Maarse A.C., Meisinger C., Brix J., Dekker P.J.T., Moczko M., Wagner R., Meijer M., Guiard B., Hoenlinger A., Pfanner N. Nature 401:485-489(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TOM22.
[11]	"The mitochondrial import receptor Tom70: identification of a 25 kDa core domain with a specific binding site for preproteins." Brix J., Ziegler G.A., Dietmeier K., Schneider-Mergener J., Schulz G.E., Pfanner N. J. Mol. Biol. 303:479-488(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex." Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M. Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[13]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[14]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, MASS SPECTROMETRY.
[15]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, MASS SPECTROMETRY.
[16]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-174; THR-232 AND THR-234, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X05585 Genomic DNA. Translation: CAA29085.1.
EF125216 Genomic DNA. Translation: ABN58537.1.
EF125217 Genomic DNA. Translation: ABN58546.1.
EF125218 Genomic DNA. Translation: ABN58555.1.
EF125219 Genomic DNA. Translation: ABN58564.1.
EF125220 Genomic DNA. Translation: ABN58573.1.
EF125221 Genomic DNA. Translation: ABN58582.1.
EF125222 Genomic DNA. Translation: ABN58591.1.
EF125223 Genomic DNA. Translation: ABN58600.1.
EF125224 Genomic DNA. Translation: ABN58609.1.
EF125225 Genomic DNA. Translation: ABN58618.1.
EF125226 Genomic DNA. Translation: ABN58627.1.
EF125228 Genomic DNA. Translation: ABN58645.1.
Z69382 Genomic DNA. Translation: CAA93386.1.
Z71397 Genomic DNA. Translation: CAA96002.1.
BK006947 Genomic DNA. Translation: DAA10428.1.

PIR

MMBYO. S63062.

RefSeq

NP_014278.3. NM_001182959.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GW1	X-ray	3.00	A/B	94-607	[»]

ProteinModelPortal

P07213.

SMR

P07213. Positions 94-607.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2301N.

IntAct

P07213. 9 interactions.

MINT

MINT-508943.

STRING

4932.YNL121C.

Protein family/group databases

TCDB

3.A.8.1.1. mitochondrial protein translocase (MPT) family.

Proteomic databases

PaxDb

P07213.

PeptideAtlas

P07213.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YNL121C; YNL121C; YNL121C.

GeneID

855602.

KEGG

sce:YNL121C.

Organism-specific databases

CYGD

YNL121c.

SGD

S000005065. TOM70.

Phylogenomic databases

eggNOG

NOG290605.

GeneTree

ENSGT00700000104258.

OMA

WKQDLDK.

OrthoDB

EOG4SBJ6K.

Enzyme and pathway databases

BioCyc

YEAST:G3O-33142-MONOMER.

Reactome

REACT_118590. Mitochondrial Protein Import (yeast).
REACT_85873. Metabolism of proteins.

Gene expression databases

Genevestigator

P07213.

GermOnline

YNL121C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.25.40.10. 3 hits.

InterPro

IPR005687. Tom70.
IPR001440. TPR-1.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]

Pfam

PF00515. TPR_1. 2 hits.
[Graphical view]

SMART

SM00028. TPR. 6 hits.
[Graphical view]

TIGRFAMs

TIGR00990. 3a0801s09. 1 hit.

PROSITE

PS50005. TPR. 6 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P07213.

NextBio

979768.

Entry information

Entry name

TOM70_YEAST

Accession

Primary (citable) accession number: P07213
Secondary accession number(s): B0KZR5 , B0KZS4, B0KZU2, B0KZY7, B0KZZ6, B0L005, B0L023, D6W162

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 152 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program