Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei26 – 261Phosphatidic acid1 Publication
Binding sitei58 – 581Phosphatidic acid1 Publication
Binding sitei148 – 1481Phosphatidic acid1 Publication
Binding sitei152 – 1521Phosphatidic acid2 Publications

GO - Molecular functioni

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

GO - Biological processi

  • cardiolipin metabolic process 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 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231F → D: Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication
Mutagenesisi25 – 251R → E: Nearly abolishes phosphatidic acid transfer activity. 1 Publication
Mutagenesisi25 – 251R → K: No effect on phosphatidic acid transfer activity. 1 Publication
Mutagenesisi33 – 331H → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-58; E-61; E-148 and E-155. 1 Publication
Mutagenesisi42 – 421R → D: Impairs interaction with MDM35. Reduces ability to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication
Mutagenesisi50 – 501L → D: Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication
Mutagenesisi54 – 541R → E: Decreases phosphatidic acid transfer activity and impairs cardiolipin biosynthesis. 1 Publication
Mutagenesisi58 – 581K → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-33; E-61; E-148 and E-155. 1 Publication
Mutagenesisi61 – 611K → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-33; E-58; E-148 and E-155. 1 Publication
Mutagenesisi61 – 611K → E: Nearly abolishes phosphatidic acid transfer activity; when associated with E-155. 1 Publication
Mutagenesisi62 – 621L → A: Decreases phosphatidic acid binding and impairs cardiolipin biosynthesis; when associated with A-65. 1 Publication
Mutagenesisi65 – 651W → A: Decreases phosphatidic acid binding and impairs cardiolipin biosynthesis; when associated with A-62. 1 Publication
Mutagenesisi77 – 771W → D: Impairs interaction with MDM35. Reduces ability to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication
Mutagenesisi78 – 781I → D: Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication
Mutagenesisi84 – 841V → E: Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication
Mutagenesisi96 – 961R → D: Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication
Mutagenesisi97 – 971N → A: Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication
Mutagenesisi104 – 1041M → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-144. 1 Publication
Mutagenesisi106 – 1061V → E: Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication
Mutagenesisi144 – 1441W → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-104. 1 Publication
Mutagenesisi148 – 1481K → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-33; E-58; E-61 and E-155. 1 Publication
Mutagenesisi155 – 1551K → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-33; E-58; E-61 and E-148. 1 Publication
Mutagenesisi155 – 1551K → E: Nearly abolishes phosphatidic acid transfer activity; when associated with E-61. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 175175Protein UPS1, mitochondrialPRO_0000271269Add
BLAST

Proteomic databases

MaxQBiQ05776.

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 interactions.
DIPiDIP-4798N.
IntActiQ05776. 1 interaction.
MINTiMINT-494469.

Structurei

Secondary structure

1
175
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1312Combined sources
Helixi15 – 239Combined sources
Beta strandi34 – 4411Combined sources
Beta strandi50 – 5910Combined sources
Turni64 – 696Combined sources
Beta strandi75 – 8511Combined sources
Turni86 – 894Combined sources
Beta strandi90 – 10011Combined sources
Turni101 – 1033Combined sources
Beta strandi105 – 11511Combined sources
Turni116 – 1194Combined sources
Beta strandi120 – 13011Combined sources
Helixi134 – 1363Combined sources
Helixi137 – 16731Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-170.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 172171PRELI/MSF1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 8080Required for mitochondrial targeting1 PublicationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00550000074825.
HOGENOMiHOG000185150.
InParanoidiQ05776.
OMAiHISESWI.
OrthoDBiEOG7W6WX6.

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
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. Positions 1-170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31463. 316 interactions.
DIPiDIP-4798N.
IntActiQ05776. 1 interaction.
MINTiMINT-494469.

Proteomic databases

MaxQBiQ05776.

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.
OMAiHISESWI.
OrthoDBiEOG7W6WX6.

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...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "Ups1p, a conserved intermembrane space protein, regulates mitochondrial shape and alternative topogenesis of Mgm1p."
    Sesaki H., Dunn C.D., Iijima M., Shepard K.A., Yaffe M.P., Machamer C.E., Jensen R.E.
    J. Cell Biol. 173:651-658(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  6. "The genetic interactome of prohibitins: coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria."
    Osman C., Haag M., Potting C., Rodenfels J., Dip P.V., Wieland F.T., Brugger B., Westermann B., Langer T.
    J. Cell Biol. 184:583-596(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria."
    Tamura Y., Endo T., Iijima M., Sesaki H.
    J. Cell Biol. 185:1029-1045(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "Mdm35p imports Ups proteins into the mitochondrial intermembrane space by functional complex formation."
    Tamura Y., Iijima M., Sesaki H.
    EMBO J. 29:2875-2887(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION MDM35.
  9. "Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35."
    Potting C., Wilmes C., Engmann T., Osman C., Langer T.
    EMBO J. 29:2888-2898(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MDM35.
  10. "Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes."
    Miliara X., Garnett J.A., Tatsuta T., Abid Ali F., Baldie H., Perez-Dorado I., Simpson P., Yague E., Langer T., Matthews S.
    EMBO Rep. 16:824-835(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MDM35, MUTAGENESIS OF ARG-54.
  11. "Structural basis of intramitochondrial phosphatidic acid transport mediated by Ups1-Mdm35 complex."
    Yu F., He F., Yao H., Wang C., Wang J., Li J., Qi X., Xue H., Ding J., Zhang P.
    EMBO Rep. 16:813-823(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-170 IN COMPLEX WITH PHOSPHATIDIC ACID AND MDM35, INTERACTION WITH MDM35, FUNCTION, MUTAGENESIS OF PHE-23; HIS-33; ARG-42; LEU-50; LYS-58; LYS-61; TRP-77; ILE-78; VAL-84; ARG-96; ASN-97; MET-104; VAL-106; TRP-144; LYS-148 AND LYS-155.
  12. "Structural and mechanistic insights into phospholipid transfer by Ups1-Mdm35 in mitochondria."
    Watanabe Y., Tamura Y., Kawano S., Endo T.
    Nat. Commun. 6:7922-7922(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 1-170 IN COMPLEX WITH PHOSPHATIDIC ACID AND MDM35, INTERACTION WITH MDM35, FUNCTION, MUTAGENESIS OF ARG-25; LYS-61 AND LYS-155, SUBCELLULAR LOCATION.

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: June 8, 2016
This is version 109 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.