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Oxysterol-binding protein homolog 7

 OSH7_YEAST              Reviewed;         437 AA.
P38755; D3DKR7;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
12-SEP-2018, entry version 138.
RecName: Full=Oxysterol-binding protein homolog 7;
Name=OSH7; OrderedLocusNames=YHR001W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8091229; DOI=10.1126/science.8091229;
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J.,
Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
Vaudin M.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
VIII.";
Science 265:2077-2082(1994).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
GENETIC ANALYSIS.
PubMed=11238399;
Beh C.T., Cool L., Phillips J., Rine J.;
"Overlapping functions of the yeast oxysterol-binding protein
homologues.";
Genetics 157:1117-1140(2001).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
SUBCELLULAR LOCATION.
PubMed=20008566; DOI=10.1083/jcb.200905007;
Schulz T.A., Choi M.G., Raychaudhuri S., Mears J.A., Ghirlando R.,
Hinshaw J.E., Prinz W.A.;
"Lipid-regulated sterol transfer between closely apposed membranes by
oxysterol-binding protein homologues.";
J. Cell Biol. 187:889-903(2009).
[7]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-276, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23934110; DOI=10.1038/nature12430;
Maeda K., Anand K., Chiapparino A., Kumar A., Poletto M., Kaksonen M.,
Gavin A.C.;
"Interactome map uncovers phosphatidylserine transport by oxysterol-
binding proteins.";
Nature 501:257-261(2013).
[9]
FUNCTION.
PubMed=26206936; DOI=10.1126/science.aab1346;
Moser von Filseck J., Copic A., Delfosse V., Vanni S., Jackson C.L.,
Bourguet W., Drin G.;
"Phosphatidylserine transport by ORP/Osh proteins is driven by
phosphatidylinositol 4-phosphate.";
Science 349:432-436(2015).
-!- FUNCTION: Lipid transporter involved in lipid countertransport
between the endoplasmic reticulum and the plasma membrane:
specifically exchanges phosphatidylserine with
phosphatidylinositol 4-phosphate (PI4P), delivering
phosphatidylserine to the plasma membrane in exchange for PI4P,
which is degraded by the SAC1 phosphatase in the endoplasmic
reticulum. Binds phosphatidylserine and PI4P in a mutually
exclusive manner. {ECO:0000269|PubMed:23934110,
ECO:0000269|PubMed:26206936}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:20008566, ECO:0000269|PubMed:23934110}.
Note=Localizes to the cortical endoplasmic reticulum at the
endoplasmic reticulum-plasma membrane contact sites.
{ECO:0000269|PubMed:20008566, ECO:0000269|PubMed:23934110}.
-!- MISCELLANEOUS: Present with 2350 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U10555; AAB68425.1; -; Genomic_DNA.
EMBL; AY692903; AAT92922.1; -; Genomic_DNA.
EMBL; BK006934; DAA06687.1; -; Genomic_DNA.
PIR; S46796; S46796.
RefSeq; NP_011863.1; NM_001179131.1.
ProteinModelPortal; P38755; -.
SMR; P38755; -.
BioGrid; 36425; 112.
DIP; DIP-6363N; -.
IntAct; P38755; 19.
MINT; P38755; -.
STRING; 4932.YHR001W; -.
TCDB; 2.D.1.1.4; the pi4p/ps counter transporter (p/p-ct) family.
iPTMnet; P38755; -.
MaxQB; P38755; -.
PaxDb; P38755; -.
PRIDE; P38755; -.
EnsemblFungi; YHR001W; YHR001W; YHR001W.
GeneID; 856389; -.
KEGG; sce:YHR001W; -.
EuPathDB; FungiDB:YHR001W; -.
SGD; S000001043; OSH7.
GeneTree; ENSGT00550000074515; -.
HOGENOM; HOG000233871; -.
InParanoid; P38755; -.
KO; K22285; -.
OMA; LSGWHIR; -.
OrthoDB; EOG092C2XNN; -.
BioCyc; YEAST:YHR001W-MONOMER; -.
Reactome; R-SCE-1482801; Acyl chain remodelling of PS.
Reactome; R-SCE-192105; Synthesis of bile acids and bile salts.
PRO; PR:P38755; -.
Proteomes; UP000002311; Chromosome VIII.
GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0008289; F:lipid binding; IDA:SGD.
GO; GO:0008142; F:oxysterol binding; ISS:SGD.
GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
GO; GO:0005548; F:phospholipid transporter activity; IDA:UniProtKB.
GO; GO:0006897; P:endocytosis; IGI:SGD.
GO; GO:0006887; P:exocytosis; IGI:SGD.
GO; GO:0045324; P:late endosome to vacuole transport; IMP:SGD.
GO; GO:0030011; P:maintenance of cell polarity; IGI:SGD.
GO; GO:0015914; P:phospholipid transport; IDA:UniProtKB.
GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IGI:SGD.
GO; GO:0016125; P:sterol metabolic process; IGI:SGD.
GO; GO:0015918; P:sterol transport; IGI:SGD.
InterPro; IPR037239; OSBP_sf.
InterPro; IPR000648; Oxysterol-bd.
InterPro; IPR018494; Oxysterol-bd_CS.
PANTHER; PTHR10972; PTHR10972; 1.
Pfam; PF01237; Oxysterol_BP; 1.
SUPFAM; SSF144000; SSF144000; 1.
PROSITE; PS01013; OSBP; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Isopeptide bond;
Lipid transport; Lipid-binding; Membrane; Reference proteome;
Transport; Ubl conjugation.
CHAIN 1 437 Oxysterol-binding protein homolog 7.
/FTId=PRO_0000100391.
REGION 64 69 Phosphatidylinositol 4-phosphate binding.
{ECO:0000250|UniProtKB:Q02201}.
REGION 64 69 Phosphatidylserine binding.
{ECO:0000250|UniProtKB:Q02201}.
REGION 126 129 Phosphatidylinositol 4-phosphate binding.
{ECO:0000250|UniProtKB:Q02201}.
REGION 157 158 Phosphatidylinositol 4-phosphate binding.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 129 129 Phosphatidylserine.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 183 183 Phosphatidylserine.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 351 351 Phosphatidylinositol 4-phosphate.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 355 355 Phosphatidylinositol 4-phosphate.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 359 359 Phosphatidylinositol 4-phosphate.
{ECO:0000250|UniProtKB:Q02201}.
CROSSLNK 276 276 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
SEQUENCE 437 AA; 49805 MW; 1C972ED6517D529B CRC64;
MALNKLKNIP SLTNSSHSSI NGIASNAANS KPSGADTDDI DENDESGQSI LLNIISQLKP
GCDLSRITLP TFILEKKSML ERITNQLQFP DVLLEAHSNK DGLQRFVKVV AWYLAGWHIG
PRAVKKPLNP ILGEHFTAYW DLPNKQQAFY IAEQTSHHPP ESAYFYMIPE SNIRVDGVVV
PKSKFLGNSS AAMMEGLTVL QFLDIKDANG KPEKYTLSQP NVYARGILFG KMRIELGDHM
VIMGPKYQVD IEFKTKGFIS GTYDAIEGTI KDYDGKEYYQ ISGKWNDIMY IKDLREKSSK
KTVLFDTHQH FPLAPKVRPL EEQGEYESRR LWKKVTDALA VRDHEVATEE KFQIENRQRE
LAKKRAEDGV EFHSKLFRRA EPGEDLDYYI YKHIPEGTDK HEEQIRSILE TAPILPGQTF
TEKFSIPAYK KHGIQKN


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