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Protein

Mitochondrial import inner membrane translocase subunit TIM16

Gene

PAM16

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (SSC1) via its interaction with PAM18/TIM14. May act by positioning PAM18/TIM14 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation.3 Publications

Miscellaneous

Present with 3180 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

  • protein domain specific binding Source: SGD

GO - Biological processi

  • protein import into mitochondrial matrix Source: SGD

Keywordsi

Biological processProtein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-31558-MONOMER

Protein family/group databases

TCDBi3.A.8.1.1 the mitochondrial protein translocase (mpt) family

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial import inner membrane translocase subunit TIM16
Alternative name(s):
Presequence translocated-associated motor subunit PAM16
Gene namesi
Name:PAM16
Synonyms:TIM16
Ordered Locus Names:YJL104W
ORF Names:J0822
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL104W
SGDiS000003640 PAM16

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi88 – 90DKE → HPD: Does not confer ability to stimulate the ATPase activity of mtHSP70. 1 Publication3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002140981 – 149Mitochondrial import inner membrane translocase subunit TIM16Add BLAST149

Proteomic databases

MaxQBiP42949
PaxDbiP42949
PRIDEiP42949

Interactioni

Subunit structurei

Homodimer and heterodimer with PAM18. Homodimerization may not be relevant in vivo, while heterodimerization is essential for activity regulation of mtHSP70. Component of the PAM complex, at least composed of mtHsp70, MGE1, TIM44, PAM16, PAM17 and PAM18. Interacts with MDJ2.6 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein domain specific binding Source: SGD

Protein-protein interaction databases

BioGridi33652, 417 interactors
IntActiP42949, 11 interactors
MINTiP42949
STRINGi4932.YJL104W

Structurei

Secondary structure

1149
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi55 – 61Combined sources7
Helixi66 – 68Combined sources3
Helixi73 – 86Combined sources14
Helixi89 – 91Combined sources3
Helixi95 – 116Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GUZX-ray2.00B/D/F/H/J/L/N/P54-117[»]
ProteinModelPortaliP42949
SMRiP42949
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42949

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni57 – 113J-likeAdd BLAST57

Domaini

The J-like region, although related to the J domain does not stimulate ATPase activity of mtHSP70. It nevertheless mediates the heterodimerization with the J domain of PAM18 and is therefore essential for PAM complex function.1 Publication

Sequence similaritiesi

Belongs to the TIM16/PAM16 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000012037
HOGENOMiHOG000180095
InParanoidiP42949
KOiK17805
OMAiYLMEAND
OrthoDBiEOG092C5SDV

Family and domain databases

Gene3Di1.10.287.110, 1 hit
InterProiView protein in InterPro
IPR036869 J_dom_sf
IPR005341 Tim16
PANTHERiPTHR12388 PTHR12388, 1 hit

Sequencei

Sequence statusi: Complete.

P42949-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHRAFIQVI ITGTQVFGKA FAEAYRQAAS QSVKQGATNA SRRGTGKGEY
60 70 80 90 100
GGITLDESCK ILNIEESKGD LNMDKINNRF NYLFEVNDKE KGGSFYLQSK
110 120 130 140
VYRAAERLKW ELAQREKNAK AKAGDASTAK PPPNSTNSSG ADNSASSNQ
Length:149
Mass (Da):16,216
Last modified:November 1, 1995 - v1
Checksum:i42BB69D746264B47
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti114Q → H in AAT92626 (PubMed:17322287).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85021 Genomic DNA Translation: CAA59390.1
Z49379 Genomic DNA Translation: CAA89399.1
AY692607 Genomic DNA Translation: AAT92626.1
BK006943 Genomic DNA Translation: DAA08696.1
PIRiS53383
RefSeqiNP_012431.1, NM_001181537.1

Genome annotation databases

EnsemblFungiiYJL104W; YJL104W; YJL104W
GeneIDi853340
KEGGisce:YJL104W

Similar proteinsi

Entry informationi

Entry nameiTIM16_YEAST
AccessioniPrimary (citable) accession number: P42949
Secondary accession number(s): D6VW80, Q6B2X3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 28, 2018
This is version 144 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health