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Protein

Oxysterol-binding protein homolog 4

Gene

KES1

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

Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1 phosphatase in the endoplasmic reticulum (PubMed:16136145, PubMed:22162133). Displays a similar affinity for PI4P and sterols (PubMed:22162133). Binds sterol and PI4P in a mutually exclusive manner (Probable).Curated2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei96 – 961SterolCombined sources2 Publications
Binding sitei336 – 3361Phosphatidylinositol 4-phosphateCombined sources1 Publication
Binding sitei340 – 3401Phosphatidylinositol 4-phosphateCombined sources1 Publication
Binding sitei344 – 3441Phosphatidylinositol 4-phosphateCombined sources1 Publication

GO - Molecular functioni

  • lipid binding Source: SGD
  • oxysterol binding Source: SGD
  • phosphatidic acid binding Source: SGD
  • phosphatidylinositol-4,5-bisphosphate binding Source: SGD
  • phosphatidylinositol-4-phosphate binding Source: UniProtKB
  • sterol transporter activity Source: UniProtKB

GO - Biological processi

  • endocytosis Source: SGD
  • ER to Golgi ceramide transport Source: SGD
  • exocytosis Source: SGD
  • maintenance of cell polarity Source: SGD
  • piecemeal microautophagy of nucleus Source: SGD
  • positive regulation of phosphatase activity Source: SGD
  • post-Golgi vesicle-mediated transport Source: SGD
  • sphingolipid metabolic process Source: SGD
  • sterol biosynthetic process Source: UniProtKB-KW
  • sterol transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Lipid transport, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34042-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Oxysterol-binding protein homolog 4
Alternative name(s):
Protein KES1
Gene namesi
Name:KES1Imported
Synonyms:OSH4
Ordered Locus Names:YPL145C
ORF Names:LPI3C, P2614
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL145C.
SGDiS000006066. KES1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • extrinsic component of membrane Source: SGD
  • Golgi membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi97 – 971Y → F: Abolishes both cholesterol binding and biological function. 1 Publication
Mutagenesisi109 – 1091K → A: Strong reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. 2 Publications
Mutagenesisi111 – 1111L → D: Abolishes both cholesterol binding and biological function. 1 Publication
Mutagenesisi112 – 1121N → E: Abolishes binding to phosphatidylinositol 4-phosphate. 1 Publication
Mutagenesisi117 – 1171E → A: Abolishes both cholesterol binding and biological function. 1 Publication
Mutagenesisi143 – 1442HH → AA: Reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. 3 Publications
Mutagenesisi168 – 1681K → A: Slight reduction in cholesterol transport. 1 Publication
Mutagenesisi168 – 1681K → A: Strong reduction in cholesterol transport. 1 Publication
Mutagenesisi202 – 2043HIE → AIA: Strong reduction in cholesterol binding without affecting phosphatidylinositol 4-phosphate binding. 1 Publication
Mutagenesisi336 – 3361K → A: Strong reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. 2 Publications
Mutagenesisi340 – 3401E → A: Abolishes binding to phosphatidylinositol 4-phosphate. 1 Publication
Mutagenesisi344 – 3441R → A: Slight reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Oxysterol-binding protein homolog 4PRO_0000100386Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei370 – 3701PhosphothreonineCombined sources
Modified residuei389 – 3891PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP35844.
PeptideAtlasiP35844.

PTM databases

iPTMnetiP35844.

Interactioni

Protein-protein interaction databases

BioGridi36038. 176 interactions.
DIPiDIP-2867N.
IntActiP35844. 10 interactions.
MINTiMINT-1678684.

Structurei

Secondary structure

1
434
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 63Combined sources
Helixi8 – 158Combined sources
Turni16 – 194Combined sources
Helixi24 – 263Combined sources
Helixi31 – 333Combined sources
Beta strandi34 – 385Combined sources
Helixi39 – 468Combined sources
Beta strandi47 – 493Combined sources
Helixi50 – 545Combined sources
Helixi55 – 584Combined sources
Turni61 – 633Combined sources
Helixi64 – 663Combined sources
Helixi77 – 10428Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi118 – 1236Combined sources
Turni129 – 1313Combined sources
Beta strandi134 – 1429Combined sources
Turni143 – 1464Combined sources
Beta strandi147 – 1548Combined sources
Turni155 – 1584Combined sources
Beta strandi159 – 17113Combined sources
Beta strandi173 – 1753Combined sources
Beta strandi177 – 1826Combined sources
Beta strandi185 – 1895Combined sources
Beta strandi192 – 1976Combined sources
Beta strandi201 – 2044Combined sources
Turni206 – 2094Combined sources
Beta strandi212 – 2154Combined sources
Beta strandi217 – 2237Combined sources
Beta strandi228 – 2347Combined sources
Beta strandi236 – 2394Combined sources
Beta strandi241 – 25313Combined sources
Helixi256 – 2583Combined sources
Helixi260 – 2623Combined sources
Beta strandi264 – 2707Combined sources
Beta strandi273 – 2797Combined sources
Helixi283 – 2853Combined sources
Beta strandi287 – 2915Combined sources
Turni292 – 2943Combined sources
Helixi305 – 3073Combined sources
Helixi313 – 3164Combined sources
Helixi318 – 3269Combined sources
Helixi329 – 35325Combined sources
Helixi357 – 3593Combined sources
Beta strandi360 – 3667Combined sources
Beta strandi368 – 3703Combined sources
Helixi383 – 3919Combined sources
Beta strandi396 – 3994Combined sources
Helixi407 – 4104Combined sources
Beta strandi417 – 4215Combined sources
Helixi423 – 4275Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZHTX-ray1.90A2-434[»]
1ZHWX-ray1.70A2-434[»]
1ZHXX-ray1.50A2-434[»]
1ZHYX-ray1.60A2-434[»]
1ZHZX-ray1.90A2-434[»]
1ZI7X-ray2.50A/B/C30-434[»]
3SPWX-ray2.60A/B1-434[»]
4F4BX-ray1.87A/B2-434[»]
4FESX-ray2.00A/B2-434[»]
4JCHX-ray1.70A/B2-434[»]
ProteinModelPortaliP35844.
SMRiP35844. Positions 2-434.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35844.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 296Phosphatidylinositol 4-phosphate bindingCombined sources1 Publication
Regioni109 – 1124Phosphatidylinositol 4-phosphate bindingCombined sources1 Publication
Regioni143 – 1442Phosphatidylinositol 4-phosphate bindingCombined sources1 Publication

Domaini

Consists of a beta-barrel forming a sterol-binding pocket. When empty, the N-terminal lid (29 residues) is unfolded and leaves the pocket open. Upon sterol binding, this segment forms a lid that blocks the sterol molecule in the pocket (PubMed:16136145). Phosphatidylinositol 4-phosphate (PI4P) binding sites are roughly the same as for sterol. First, the sterol-binding pocket accommodates the PI4P acyl chains. Second, a shallow pocket at the entrance of the tunnel, which contains critical residues such as Lys-336, His-143 and His-144, selects the polar head of PI4P with high specificity. This interaction is probably essential for compensating loose binding of the PI4P acyl chains. Third, the N-terminal lid secures the bound PI4P molecule by wrapping its glycerol moiety (PubMed:22162133).2 Publications

Sequence similaritiesi

Belongs to the OSBP family.Curated

Phylogenomic databases

HOGENOMiHOG000197950.
InParanoidiP35844.
OMAiKSQYCSR.
OrthoDBiEOG74FF95.

Family and domain databases

InterProiIPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
[Graphical view]
PANTHERiPTHR10972. PTHR10972. 2 hits.
PfamiPF01237. Oxysterol_BP. 1 hit.
[Graphical view]
PROSITEiPS01013. OSBP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35844-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQYASSSSW TSFLKSIASF NGDLSSLSAP PFILSPISLT EFSQYWAEHP
60 70 80 90 100
ELFLEPSFIN DDNYKEHCLI DPEVESPELA RMLAVTKWFI STLKSQYCSR
110 120 130 140 150
NESLGSEKKP LNPFLGELFV GKWENKEHPE FGETVLLSEQ VSHHPPVTAF
160 170 180 190 200
SIFNDKNKVK LQGYNQIKAS FTKSLMLTVK QFGHTMLDIK DESYLVTPPP
210 220 230 240 250
LHIEGILVAS PFVELEGKSY IQSSTGLLCV IEFSGRGYFS GKKNSFKARI
260 270 280 290 300
YKDSKDSKDK EKALYTISGQ WSGSSKIIKA NKKEESRLFY DAARIPAEHL
310 320 330 340 350
NVKPLEEQHP LESRKAWYDV AGAIKLGDFN LIAKTKTELE ETQRELRKEE
360 370 380 390 400
EAKGISWQRR WFKDFDYSVT PEEGALVPEK DDTFLKLASA LNLSTKNAPS
410 420 430
GTLVGDKEDR KEDLSSIHWR FQRELWDEEK EIVL
Length:434
Mass (Da):49,492
Last modified:June 1, 1994 - v1
Checksum:i360E4A46ABE2D87B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti355 – 3551I → T in AAS56373 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03913 Unassigned DNA. Translation: AAA17736.1.
U43703 Genomic DNA. Translation: AAB68217.1.
X96770 Genomic DNA. Translation: CAA65548.1.
Z73501 Genomic DNA. Translation: CAA97849.1.
AY558047 Genomic DNA. Translation: AAS56373.1.
BK006949 Genomic DNA. Translation: DAA11290.1.
PIRiS42676.
RefSeqiNP_015180.1. NM_001183959.1.

Genome annotation databases

EnsemblFungiiYPL145C; YPL145C; YPL145C.
GeneIDi855958.
KEGGisce:YPL145C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03913 Unassigned DNA. Translation: AAA17736.1.
U43703 Genomic DNA. Translation: AAB68217.1.
X96770 Genomic DNA. Translation: CAA65548.1.
Z73501 Genomic DNA. Translation: CAA97849.1.
AY558047 Genomic DNA. Translation: AAS56373.1.
BK006949 Genomic DNA. Translation: DAA11290.1.
PIRiS42676.
RefSeqiNP_015180.1. NM_001183959.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZHTX-ray1.90A2-434[»]
1ZHWX-ray1.70A2-434[»]
1ZHXX-ray1.50A2-434[»]
1ZHYX-ray1.60A2-434[»]
1ZHZX-ray1.90A2-434[»]
1ZI7X-ray2.50A/B/C30-434[»]
3SPWX-ray2.60A/B1-434[»]
4F4BX-ray1.87A/B2-434[»]
4FESX-ray2.00A/B2-434[»]
4JCHX-ray1.70A/B2-434[»]
ProteinModelPortaliP35844.
SMRiP35844. Positions 2-434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36038. 176 interactions.
DIPiDIP-2867N.
IntActiP35844. 10 interactions.
MINTiMINT-1678684.

PTM databases

iPTMnetiP35844.

Proteomic databases

MaxQBiP35844.
PeptideAtlasiP35844.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL145C; YPL145C; YPL145C.
GeneIDi855958.
KEGGisce:YPL145C.

Organism-specific databases

EuPathDBiFungiDB:YPL145C.
SGDiS000006066. KES1.

Phylogenomic databases

HOGENOMiHOG000197950.
InParanoidiP35844.
OMAiKSQYCSR.
OrthoDBiEOG74FF95.

Enzyme and pathway databases

BioCyciYEAST:G3O-34042-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP35844.
NextBioi980753.
PROiP35844.

Family and domain databases

InterProiIPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
[Graphical view]
PANTHERiPTHR10972. PTHR10972. 2 hits.
PfamiPF01237. Oxysterol_BP. 1 hit.
[Graphical view]
PROSITEiPS01013. OSBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A new family of yeast genes implicated in ergosterol synthesis is related to the human oxysterol binding protein."
    Jiang B., Brown J.L., Sheraton J., Fortin N., Bussey H.
    Yeast 10:341-353(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a small nuclear RNA, a new putative protein kinase and two new putative regulators."
    Purnelle B., Coster F., Goffeau A.
    Yeast 12:1483-1492(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204511 / S288c / AB972.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Overlapping functions of the yeast oxysterol-binding protein homologues."
    Beh C.T., Cool L., Phillips J., Rine J.
    Genetics 157:1117-1140(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENETIC ANALYSIS.
  7. "Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex."
    Li X., Rivas M.P., Fang M., Marchena J., Mehrotra B., Chaudhary A., Feng L., Prestwich G.D., Bankaitis V.A.
    J. Cell Biol. 157:63-77(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "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-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Phosphatidylserine transport by ORP/Osh proteins is driven by phosphatidylinositol 4-phosphate."
    Moser von Filseck J., Copic A., Delfosse V., Vanni S., Jackson C.L., Bourguet W., Drin G.
    Science 349:432-436(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 143-HIS-HIS-144.
  12. "Structural mechanism for sterol sensing and transport by OSBP-related proteins."
    Im Y.J., Raychaudhuri S., Prinz W.A., Hurley J.H.
    Nature 437:154-158(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 2-434 IN COMPLEX WITH STEROL, FUNCTION, DOMAIN, MUTAGENESIS OF TYR-97; LYS-109; LEU-111; GLU-117; 143-HIS-HIS-144; LYS-168; LYS-336 AND ARG-344.
  13. "Osh4p exchanges sterols for phosphatidylinositol 4-phosphate between lipid bilayers."
    de Saint-Jean M., Delfosse V., Douguet D., Chicanne G., Payrastre B., Bourguet W., Antonny B., Drin G.
    J. Cell Biol. 195:965-978(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH PHOSPHATIDYLINOSITOL 4-PHOSPHATE, FUNCTION, MUTAGENESIS OF LYS-109; ASN-112; 143-HIS-HIS-144; 202-HIS--GLU-204; LYS-336; GLU-340 AND ARG-344.
  14. "Synthesis and structure of 16,22-diketocholesterol bound to oxysterol-binding protein Osh4."
    Koag M.C., Cheun Y., Kou Y., Ouzon-Shubeita H., Min K., Monzingo A.F., Lee S.
    Steroids 78:938-944(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 2-434 IN COMPLEX WITH STEROL.

Entry informationi

Entry nameiKES1_YEAST
AccessioniPrimary (citable) accession number: P35844
Secondary accession number(s): D6W3M4, E9P8U8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 11, 2016
This is version 146 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 32200 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.