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Protein

Oxysterol-binding protein homolog 1

Gene

SWH1

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-binding protein involved in maintenance of intracellular sterol distribution and homeostasis. Binds to phosphoinositides. May be involved in formation of PMN vesicles by altering the membrane lipid composition.1 Publication

GO - Molecular functioni

  • 1-phosphatidylinositol binding Source: SGD
  • lipid binding Source: SGD
  • oxysterol binding Source: SGD
  • sterol transporter activity Source: SGD

GO - Biological processi

  • endocytosis Source: SGD
  • exocytosis Source: SGD
  • maintenance of cell polarity Source: SGD
  • piecemeal microautophagy of nucleus Source: SGD
  • sterol transport Source: SGD

Keywordsi

Biological processLipid transport, Transport
LigandLipid-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-28883-MONOMER.
ReactomeiR-SCE-192105. Synthesis of bile acids and bile salts.

Names & Taxonomyi

Protein namesi
Recommended name:
Oxysterol-binding protein homolog 1
Gene namesi
Name:SWH1
Synonyms:OSH1
Ordered Locus Names:YAR042W
ORF Names:YAR044W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:YAR042W.
SGDiS000000081. SWH1.

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

Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi719D → A: Abolishes function. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001003871 – 1188Oxysterol-binding protein homolog 1Add BLAST1188

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei394PhosphoserineCombined sources1
Modified residuei490PhosphoserineCombined sources1
Modified residuei500PhosphoserineCombined sources1
Modified residuei678PhosphoserineCombined sources1
Modified residuei683PhosphoserineCombined sources1
Modified residuei691PhosphoserineCombined sources1
Modified residuei692PhosphothreonineCombined sources1
Modified residuei694PhosphothreonineCombined sources1
Modified residuei708PhosphoserineCombined sources1
Modified residuei712PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP35845.
PRIDEiP35845.

PTM databases

iPTMnetiP35845.

Interactioni

Subunit structurei

Interacts with NVJ1.1 Publication

Protein-protein interaction databases

BioGridi31812. 122 interactors.
DIPiDIP-6839N.
ELMiP35845.
IntActiP35845. 26 interactors.
MINTiMINT-571501.
STRINGi4932.YAR042W.

Structurei

Secondary structure

11188
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 26Combined sources14
Helixi29 – 39Combined sources11
Helixi46 – 53Combined sources8
Helixi55 – 62Combined sources8
Helixi65 – 75Combined sources11
Helixi100 – 106Combined sources7
Helixi110 – 117Combined sources8
Helixi134 – 137Combined sources4
Helixi141 – 167Combined sources27
Helixi171 – 178Combined sources8
Helixi183 – 186Combined sources4
Turni194 – 196Combined sources3
Helixi200 – 207Combined sources8
Helixi210 – 218Combined sources9
Helixi233 – 236Combined sources4
Helixi249 – 251Combined sources3
Helixi252 – 267Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5H28X-ray1.50A12-274[»]
5H2CX-ray3.51A7-274[»]
ProteinModelPortaliP35845.
SMRiP35845.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati51 – 80ANK 1Add BLAST30
Repeati96 – 125ANK 2Add BLAST30
Repeati196 – 225ANK 3Add BLAST30
Domaini330 – 379PHPROSITE-ProRule annotationAdd BLAST50

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi716 – 722FFAT7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi434 – 472Asn/Asp-richAdd BLAST39

Domaini

The ankyrin repeats are required for targeting the protein to the NV junction.1 Publication
The PH domain is required for targeting the protein to the late Golgi.1 Publication
The FFAT motif is required for interaction with SCS2 and proper localization of the protein.1 Publication

Sequence similaritiesi

Belongs to the OSBP family.Curated

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

GeneTreeiENSGT00760000119155.
HOGENOMiHOG000186039.
InParanoidiP35845.
KOiK20456.
OMAiEINHTCR.
OrthoDBiEOG092C0GJ4.

Family and domain databases

CDDicd00204. ANK. 2 hits.
Gene3Di1.25.40.20. 1 hit.
2.30.29.30. 1 hit.
InterProiView protein in InterPro
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR036770. Ankyrin_rpt-contain_sf.
IPR037239. OSBP_sf.
IPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
IPR011993. PH-like_dom_sf.
IPR001849. PH_domain.
PANTHERiPTHR10972. PTHR10972. 1 hit.
PfamiView protein in Pfam
PF01237. Oxysterol_BP. 1 hit.
PF00169. PH. 1 hit.
SMARTiView protein in SMART
SM00248. ANK. 2 hits.
SM00233. PH. 1 hit.
SUPFAMiSSF144000. SSF144000. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiView protein in PROSITE
PS50297. ANK_REP_REGION. 2 hits.
PS50088. ANK_REPEAT. 2 hits.
PS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.

Sequencei

Sequence statusi: Complete.

P35845-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQPDLSSVA ISKPLLKLKL LDALRQGSFP NLQDLLKKQF QPLDDPNVQQ
60 70 80 90 100
VLHLMLHYAV QVAPMAVIKE IVHHWVSTTN TTFLNIHLDL NERDSNGNTP
110 120 130 140 150
LHIAAYQSRG DIVAFLLDQP TINDCVLNNS HLQAIEMCKN LNIAQMMQVK
160 170 180 190 200
RSTYVAETAQ EFRTAFNNRD FGHLESILSS PRNAELLDIN GMDPETGDTV
210 220 230 240 250
LHEFVKKRDV IMCRWLLEHG ADPFKRDRKG KLPIELVRKV NENDTATNTK
260 270 280 290 300
IAIDIELKKL LERATREQSV IDVTNNNLHE APTYKGYLKK WTNFAQGYKL
310 320 330 340 350
RWFILSSDGK LSYYIDQADT KNACRGSLNM SSCSLHLDSS EKLKFEIIGG
360 370 380 390 400
NNGVIRWHLK GNHPIETNRW VWAIQGAIRY AKDREILLHN GPYSPSLALS
410 420 430 440 450
HGLSSKVSNK ENLHATSKRL TKSPHLSKST LTQNDHDNDD DSTNNNNNKS
460 470 480 490 500
NNDYDDNNNN NNNDDDDYDD DDESRPLIEP LPLISSRSQS LSEITPGPHS
510 520 530 540 550
RKSTVSSTRA ADIPSDDEGY SEDDSDDDGN SSYTMENGGE NDGDEDLNAI
560 570 580 590 600
YGPYIQKLHM LQRSISIELA SLNELLQDKQ QHDEYWNTVN TSIETVSEFF
610 620 630 640 650
DKLNRLTSQR EKRMIAQMTK QRDVNNVWIQ SVKDLEMELV DKDEKLVALD
660 670 680 690 700
KERKNLKKML QKKLNNQPQV ETEANEESDD ANSMIKGSQE STNTLEEIVK
710 720 730 740 750
FIEATKESDE DSDADEFFDA EEAASDKKAN DSEDLTTNKE TPANAKPQEE
760 770 780 790 800
APEDESLIVI SSPQVEKKNQ LLKEGSFVGY EDPVRTKLAL DEDNRPKIGL
810 820 830 840 850
WSVLKSMVGQ DLTKLTLPVS FNEPTSLLQR VSEDIEYSHI LDQAATFEDS
860 870 880 890 900
SLRMLYVAAF TASMYASTTN RVSKPFNPLL GETFEYARTD GQYRFFTEQV
910 920 930 940 950
SHHPPISATW TESPKWDFYG ECNVDSSFNG RTFAVQHLGL WYITIRPDHN
960 970 980 990 1000
ISVPEETYSW KKPNNTVIGI LMGKPQVDNS GDVKVTNHTT GDYCMLHYKA
1010 1020 1030 1040 1050
HGWTSAGAYE VRGEVFNKDD KKLWVLGGHW NDSIYGKKVT ARGGELTLDR
1060 1070 1080 1090 1100
IKTANSATGG PKLDGSKFLI WKANERPSVP FNLTSFALTL NALPPHLIPY
1110 1120 1130 1140 1150
LAPTDSRLRP DQRAMENGEY DKAAAEKHRV EVKQRAAKKE REQKGEEYRP
1160 1170 1180
KWFVQEEHPV TKSLYWKFNG EYWNKRKNHD FKDCADIF
Length:1,188
Mass (Da):135,098
Last modified:December 6, 2005 - v4
Checksum:iB9DA826745CEB30B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti244D → Y in CAA52646 (PubMed:8086466).Curated1
Sequence conflicti248N → S (Ref. 3) Curated1
Sequence conflicti248N → S (PubMed:7731988).Curated1
Sequence conflicti424P → A in CAA52646 (PubMed:8086466).Curated1
Sequence conflicti464D → NNN (PubMed:8086466).Curated1
Sequence conflicti468 – 469YD → DY (PubMed:8086466).Curated2
Sequence conflicti495 – 496TP → AS in CAA52646 (PubMed:8086466).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74552 Genomic DNA. Translation: CAA52646.1.
AY241177 Genomic DNA. Translation: AAP31019.1.
L28920 Genomic DNA. Translation: AAC09496.2.
AY260892 Genomic DNA. Translation: AAP21760.1.
BK006935 Genomic DNA. Translation: DAA07006.1.
PIRiS47536.
RefSeqiNP_009421.3. NM_001178227.1.

Genome annotation databases

EnsemblFungiiYAR042W; YAR042W; YAR042W.
GeneIDi851286.
KEGGisce:YAR042W.

Similar proteinsi

Entry informationi

Entry nameiOSH1_YEAST
AccessioniPrimary (citable) accession number: P35845
Secondary accession number(s): D6VPN6
, P39555, P80234, Q86ZC4, Q86ZS1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 6, 2005
Last modified: November 22, 2017
This is version 175 of the entry and version 4 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

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