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P32830 (TIM12_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial import inner membrane translocase subunit TIM12
Alternative name(s):
Mitochondrial regulator of splicing 5
Gene names
Name:TIM12
Synonyms:MRS5
Ordered Locus Names:YBR091C
ORF Names:YBR0812
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length109 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as external driving force. In the TIM22 complex, it acts as a docking point for the soluble TIM9-TIM10 heterohexamer that guides the target proteins in transit through the aqueous mitochondrial intermembrane space. Ref.1 Ref.7 Ref.8 Ref.9 Ref.11

Subunit structure

Component of the TIM22 complex, whose core is composed of TIM18, TIM22 and TIM54, associated with the peripheral proteins MRS5/TIM12 and the 70 kDa heterohexamer composed of TIM9 and TIM10 (or TIM8 and TIM13). Interacts directly with both the TIM22 protein and the TIM9-TIM10 heterohexamer. Interacts with multi-pass transmembrane proteins in transit. Ref.6 Ref.7 Ref.8 Ref.10 Ref.12 Ref.13

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein Ref.1 Ref.7.

Domain

The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIM12 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane By similarity.

Sequence similarities

Belongs to the small Tim family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FUS3P168922EBI-11303,EBI-7193
TIM10P871082EBI-11303,EBI-9115

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 109108Mitochondrial import inner membrane translocase subunit TIM12
PRO_0000096581

Regions

Motif40 – 6627Twin CX3C motif

Amino acid modifications

Modified residue21N-acetylserine Ref.15
Disulfide bond40 ↔ 66 By similarity
Disulfide bond44 ↔ 62 By similarity

Sequences

Sequence LengthMass (Da)Tools
P32830 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 2C4B7DEE9695866D

FASTA10912,284
        10         20         30         40         50         60 
MSFFLNSLRG NQEVSQEKLD VAGVQFDAMC STFNNILSTC LEKCIPHEGF GEPDLTKGEQ 

        70         80         90        100 
CCIDRCVAKM HYSNRLIGGF VQTRGFGPEN QLRHYSRFVA KEIADDSKK 

« Hide

References

« Hide 'large scale' references
[1]"Mrs5p, an essential protein of the mitochondrial intermembrane space, affects protein import into yeast mitochondria."
Jarosch E., Tuller G., Daum G., Waldherr M., Voskova A., Schweyen R.J.
J. Biol. Chem. 271:17219-17225(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[2]"Analysis of a 70 kb region on the right arm of yeast chromosome II."
Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.
Yeast 10:1363-1381(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
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.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22."
Sirrenberg C., Bauer M.D., Guiard B., Neupert W., Brunner M.
Nature 384:582-585(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TIM10 AND TIM22.
[7]"Carrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11 and Tim12/Mrs5."
Sirrenberg C., Endres M., Foelsch H., Stuart R.A., Neupert W., Brunner M.
Nature 391:912-915(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PROBABLE ZINC-BINDING, INTERACTION WITH TIM10 AND TIM22.
[8]"Import of mitochondrial carriers mediated by essential proteins of the intermembrane space."
Koehler C.M., Jarosch E., Tokatlidis K., Schmid K., Schweyen R.J., Schatz G.
Science 279:369-373(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TIM10 AND TIM22.
[9]"Two intermembrane space TIM complexes interact with different domains of Tim23p during its import into mitochondria."
Davis A.J., Sepuri N.B., Holder J., Johnson A.E., Jensen R.E.
J. Cell Biol. 150:1271-1282(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Tim9, a new component of the TIM22.54 translocase in mitochondria."
Adam A., Endres M., Sirrenberg C., Lottspeich F., Neupert W., Brunner M.
EMBO J. 18:313-319(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TIM9 AND TIM10.
[11]"Transport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complex."
Endres M., Neupert W., Brunner M.
EMBO J. 18:3214-3221(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Tim18p, a new subunit of the TIM22 complex that mediates insertion of imported proteins into the yeast mitochondrial inner membrane."
Koehler C.M., Murphy M.P., Bally N.A., Leuenberger D., Oppliger W., Dolfini L., Junne T., Schatz G., Or E.
Mol. Cell. Biol. 20:1187-1193(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A THE TIM22 COMPLEX WITH TIM18; TIM22 AND TIM54.
[13]"Protein insertion into the mitochondrial inner membrane by a twin-pore translocase."
Rehling P., Model K., Brandner K., Kovermann P., Sickmann A., Meyer H.E., Kuehlbrandt W., Wagner R., Truscott K.N., Pfanner N.
Science 299:1747-1751(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE TIM22 COMPLEX WITH TIM10; TIM18; TIM22 AND TIM54.
[14]Erratum
Rehling P., Model K., Brandner K., Kovermann P., Sickmann A., Meyer H.E., Kuehlbrandt W., Wagner R., Truscott K.N., Pfanner N.
Science 300:251-251(2003)
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M90689 Genomic DNA. Translation: AAC37483.1.
X78993 Genomic DNA. Translation: CAA55596.1.
Z35960 Genomic DNA. Translation: CAA85044.1.
AY558529 Genomic DNA. Translation: AAS56855.1.
BK006936 Genomic DNA. Translation: DAA07212.1.
PIRS30793.
RefSeqNP_009649.1. NM_001178439.1.

3D structure databases

ProteinModelPortalP32830.
SMRP32830. Positions 22-69.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32797. 20 interactions.
DIPDIP-1140N.
IntActP32830. 5 interactions.
MINTMINT-522035.
STRING4932.YBR091C.

Proteomic databases

MaxQBP32830.
PaxDbP32830.
PeptideAtlasP32830.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR091C; YBR091C; YBR091C.
GeneID852388.
KEGGsce:YBR091C.

Organism-specific databases

CYGDYBR091c.
SGDS000000295. TIM12.

Phylogenomic databases

eggNOGNOG291835.
HOGENOMHOG000211421.
KOK17793.
OMAGEQECID.
OrthoDBEOG7VHT9C.

Enzyme and pathway databases

BioCycYEAST:G3O-29057-MONOMER.
ReactomeREACT_118590. Mitochondrial Protein Import (yeast).

Gene expression databases

GenevestigatorP32830.

Family and domain databases

Gene3D1.10.287.810. 1 hit.
InterProIPR004217. Tim10/DDP_fam_Znf.
IPR027247. Tim10/Tim12.
IPR027102. Tim12.
[Graphical view]
PANTHERPTHR11038. PTHR11038. 1 hit.
PTHR11038:SF15. PTHR11038:SF15. 1 hit.
PfamPF02953. zf-Tim10_DDP. 1 hit.
[Graphical view]
SUPFAMSSF144122. SSF144122. 1 hit.
ProtoNetSearch...

Other

NextBio971201.

Entry information

Entry nameTIM12_YEAST
AccessionPrimary (citable) accession number: P32830
Secondary accession number(s): D6VQ92
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 11, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families