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Protein

Protein UPS1, mitochondrial

Gene

UPS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for maintenance of normal mitochondrial morphology (PubMed:16754953, PubMed:26071601). Required for PCP1-dependent processing of MGM1 (PubMed:16754953). The UPS1:MDM35 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space (PubMed:26071602, PubMed:26071601, PubMed:26235513). Phosphatidic acid release requires dissociation of the UPS1:MDM35 complex (PubMed:26235513). Phosphatidic acid import is required for cardiolipin (CL) synthesis in the mitochondrial inner membrane (PubMed:26071602). With UPS2, controls the level of cardiolipin in mitochondria (PubMed:19506038). Cardiolipin is a unique phospholipid with four fatty acid chains and is present mainly in the mitochondrial inner membrane where it stabilizes the electron transport chain supercomplex between complexes III and IV through direct interaction of their subunits.6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei26Phosphatidic acid1 Publication1
Binding sitei58Phosphatidic acid1 Publication1
Binding sitei148Phosphatidic acid1 Publication1
Binding sitei152Phosphatidic acid2 Publications1

GO - Molecular functioni

  • lipid binding Source: UniProtKB-KW
  • phosphatidic acid transporter activity Source: SGD

GO - Biological processi

  • cardiolipin metabolic process Source: SGD
  • phospholipid translocation Source: SGD
  • phospholipid transport Source: SGD
  • positive regulation of phosphatidylcholine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32315-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein UPS1, mitochondrial
Alternative name(s):
Unprocessed MGM1 protein 1
Gene namesi
Name:UPS1
Ordered Locus Names:YLR193C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR193C.
SGDiS000004183. UPS1.

Subcellular locationi

  • Mitochondrion inner membrane 1 Publication; Peripheral membrane protein 1 Publication; Intermembrane side Curated
  • Mitochondrion intermembrane space 1 Publication

  • Note: Lacks the two major intermembrane space-targeting signals, bipartite presequences and cysteine motifs, and import is mediated by another IMS protein, MDM35.Curated

GO - Cellular componenti

  • extrinsic component of mitochondrial inner membrane Source: SGD
  • mitochondrial inner membrane Source: SGD
  • mitochondrial intermembrane space Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Disruption phenotypei

Cells show slow growth, fragmented mitochondria and have a 50-fold reduced level of s-MGM1. These defects can be complemented by human PRELI or bypassed by growth on a nonfermentable carbon source.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi23F → D: Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi25R → E: Nearly abolishes phosphatidic acid transfer activity. 1 Publication1
Mutagenesisi25R → K: No effect on phosphatidic acid transfer activity. 1 Publication1
Mutagenesisi33H → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-58; E-61; E-148 and E-155. 1 Publication1
Mutagenesisi42R → D: Impairs interaction with MDM35. Reduces ability to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi50L → D: Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi54R → E: Decreases phosphatidic acid transfer activity and impairs cardiolipin biosynthesis. 1 Publication1
Mutagenesisi58K → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-33; E-61; E-148 and E-155. 1 Publication1
Mutagenesisi61K → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-33; E-58; E-148 and E-155. 1 Publication1
Mutagenesisi61K → E: Nearly abolishes phosphatidic acid transfer activity; when associated with E-155. 1 Publication1
Mutagenesisi62L → A: Decreases phosphatidic acid binding and impairs cardiolipin biosynthesis; when associated with A-65. 1 Publication1
Mutagenesisi65W → A: Decreases phosphatidic acid binding and impairs cardiolipin biosynthesis; when associated with A-62. 1 Publication1
Mutagenesisi77W → D: Impairs interaction with MDM35. Reduces ability to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi78I → D: Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi84V → E: Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi96R → D: Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi97N → A: Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi104M → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-144. 1 Publication1
Mutagenesisi106V → E: Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi144W → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-104. 1 Publication1
Mutagenesisi148K → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-33; E-58; E-61 and E-155. 1 Publication1
Mutagenesisi155K → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-33; E-58; E-61 and E-148. 1 Publication1
Mutagenesisi155K → E: Nearly abolishes phosphatidic acid transfer activity; when associated with E-61. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002712691 – 175Protein UPS1, mitochondrialAdd BLAST175

Proteomic databases

MaxQBiQ05776.
PRIDEiQ05776.

Interactioni

Subunit structurei

Interacts with MDM35 (PubMed:20622808, PubMed:20657548, PubMed:26071602, PubMed:26071601, PubMed:26235513). Found associated with a 170 kDa complex.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MDM35O602005EBI-30337,EBI-2080774

Protein-protein interaction databases

BioGridi31463. 316 interactors.
DIPiDIP-4798N.
IntActiQ05776. 1 interactor.
MINTiMINT-494469.

Structurei

Secondary structure

1175
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 13Combined sources12
Helixi15 – 23Combined sources9
Beta strandi34 – 44Combined sources11
Beta strandi50 – 59Combined sources10
Turni64 – 69Combined sources6
Beta strandi75 – 85Combined sources11
Turni86 – 89Combined sources4
Beta strandi90 – 100Combined sources11
Turni101 – 103Combined sources3
Beta strandi105 – 115Combined sources11
Turni116 – 119Combined sources4
Beta strandi120 – 130Combined sources11
Helixi134 – 136Combined sources3
Helixi137 – 167Combined sources31

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XHRX-ray2.55A/B1-175[»]
4XIZX-ray2.00A/B1-170[»]
4YTWX-ray1.40B/D1-170[»]
4YTXX-ray3.20B/D/F/H/J/L/N/P1-170[»]
ProteinModelPortaliQ05776.
SMRiQ05776.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 172PRELI/MSF1PROSITE-ProRule annotationAdd BLAST171

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 80Required for mitochondrial targeting1 PublicationAdd BLAST80

Sequence similaritiesi

Belongs to the slowmo family.Curated
Contains 1 PRELI/MSF1 domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074825.
HOGENOMiHOG000185150.
InParanoidiQ05776.
OMAiVEEYTTY.
OrthoDBiEOG092C49GG.

Family and domain databases

InterProiIPR006797. PRELI/MSF1_dom.
[Graphical view]
PfamiPF04707. PRELI. 1 hit.
[Graphical view]
PROSITEiPS50904. PRELI_MSF1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q05776-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLLHKSTHI FPTDFASVSR AFFNRYPNPY SPHVLSIDTI SRNVDQEGNL
60 70 80 90 100
RTTRLLKKSG KLPTWVKPFL RGITETWIIE VSVVNPANST MKTYTRNLDH
110 120 130 140 150
TGIMKVEEYT TYQFDSATSS TIADSRVKFS SGFNMGIKSK VEDWSRTKFD
160 170
ENVKKSRMGM AFVIQKLEEA RNPQF
Length:175
Mass (Da):20,108
Last modified:November 1, 1996 - v1
Checksum:i5B9003B6A2323109
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14913 Genomic DNA. Translation: AAB67434.1.
BK006945 Genomic DNA. Translation: DAA09512.1.
PIRiS48546.
RefSeqiNP_013294.1. NM_001182080.1.

Genome annotation databases

EnsemblFungiiYLR193C; YLR193C; YLR193C.
GeneIDi850890.
KEGGisce:YLR193C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14913 Genomic DNA. Translation: AAB67434.1.
BK006945 Genomic DNA. Translation: DAA09512.1.
PIRiS48546.
RefSeqiNP_013294.1. NM_001182080.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XHRX-ray2.55A/B1-175[»]
4XIZX-ray2.00A/B1-170[»]
4YTWX-ray1.40B/D1-170[»]
4YTXX-ray3.20B/D/F/H/J/L/N/P1-170[»]
ProteinModelPortaliQ05776.
SMRiQ05776.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31463. 316 interactors.
DIPiDIP-4798N.
IntActiQ05776. 1 interactor.
MINTiMINT-494469.

Proteomic databases

MaxQBiQ05776.
PRIDEiQ05776.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR193C; YLR193C; YLR193C.
GeneIDi850890.
KEGGisce:YLR193C.

Organism-specific databases

EuPathDBiFungiDB:YLR193C.
SGDiS000004183. UPS1.

Phylogenomic databases

GeneTreeiENSGT00550000074825.
HOGENOMiHOG000185150.
InParanoidiQ05776.
OMAiVEEYTTY.
OrthoDBiEOG092C49GG.

Enzyme and pathway databases

BioCyciYEAST:G3O-32315-MONOMER.

Miscellaneous databases

PROiQ05776.

Family and domain databases

InterProiIPR006797. PRELI/MSF1_dom.
[Graphical view]
PfamiPF04707. PRELI. 1 hit.
[Graphical view]
PROSITEiPS50904. PRELI_MSF1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUPS1_YEAST
AccessioniPrimary (citable) accession number: Q05776
Secondary accession number(s): D6VYJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 704 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.