OSH6_YEAST
ID OSH6_YEAST Reviewed; 448 AA.
AC Q02201; D6VXT9;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Oxysterol-binding protein homolog 6 {ECO:0000303|PubMed:11238399};
DE AltName: Full=Lipid-transfer protein Osh6;
DE Short=LTP;
DE AltName: Full=Oxysterol-binding phosphatidylserine transferase;
DE AltName: Full=Oxysterol-binding protein-related protein 6;
DE Short=ORP 6;
DE Short=OSBP-related protein 6;
GN Name=OSH6 {ECO:0000303|PubMed:11238399}; OrderedLocusNames=YKR003W;
GN ORFNames=YK102;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1441752; DOI=10.1002/yea.320080908;
RA Duesterhoeft A., Philippsen P.;
RT "DNA sequencing and analysis of a 24.7 kb segment encompassing centromere
RT CEN11 of Saccharomyces cerevisiae reveals nine previously unknown open
RT reading frames.";
RL Yeast 8:749-759(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP GENETIC ANALYSIS.
RX PubMed=11238399; DOI=10.1093/genetics/157.3.1117;
RA Beh C.T., Cool L., Phillips J., Rine J.;
RT "Overlapping functions of the yeast oxysterol-binding protein homologues.";
RL Genetics 157:1117-1140(2001).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION.
RX PubMed=15173322; DOI=10.1242/jcs.01157;
RA Beh C.T., Rine J.;
RT "A role for yeast oxysterol-binding protein homologs in endocytosis and in
RT the maintenance of intracellular sterol-lipid distribution.";
RL J. Cell Sci. 117:2983-2996(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH VPS4.
RX PubMed=16096648; DOI=10.1038/sj.emboj.7600764;
RA Wang P., Zhang Y., Li H., Chieu H.K., Munn A.L., Yang H.;
RT "AAA ATPases regulate membrane association of yeast oxysterol binding
RT proteins and sterol metabolism.";
RL EMBO J. 24:2989-2999(2005).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16156791; DOI=10.1111/j.1742-4658.2005.04886.x;
RA Wang P., Duan W., Munn A.L., Yang H.;
RT "Molecular characterization of Osh6p, an oxysterol binding protein homolog
RT in the yeast Saccharomyces cerevisiae.";
RL FEBS J. 272:4703-4715(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=20008566; DOI=10.1083/jcb.200905007;
RA Schulz T.A., Choi M.G., Raychaudhuri S., Mears J.A., Ghirlando R.,
RA Hinshaw J.E., Prinz W.A.;
RT "Lipid-regulated sterol transfer between closely apposed membranes by
RT oxysterol-binding protein homologues.";
RL J. Cell Biol. 187:889-903(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH PHOSPHATIDYLSERINE,
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-69; THR-71; ILE-73;
RP LYS-126; ASN-129; HIS-157; HIS-158; LYS-182 AND LYS-351.
RX PubMed=23934110; DOI=10.1038/nature12430;
RA Maeda K., Anand K., Chiapparino A., Kumar A., Poletto M., Kaksonen M.,
RA Gavin A.C.;
RT "Interactome map uncovers phosphatidylserine transport by oxysterol-binding
RT proteins.";
RL Nature 501:257-261(2013).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN COMPLEX WITH PHOSPHATIDYLINOSITOL
RP 4-PHOSPHATE, FUNCTION, AND MUTAGENESIS OF LEU-69; 157-HIS-HIS-158 AND
RP LYS-351.
RX PubMed=26206936; DOI=10.1126/science.aab1346;
RA Moser von Filseck J., Copic A., Delfosse V., Vanni S., Jackson C.L.,
RA Bourguet W., Drin G.;
RT "Phosphatidylserine transport by ORP/Osh proteins is driven by
RT phosphatidylinositol 4-phosphate.";
RL Science 349:432-436(2015).
CC -!- FUNCTION: Lipid transport protein (LTP) involved in non-vesicular
CC transfer of lipids between membranes. Functions in phosphoinositide-
CC coupled directional transport of various lipids by carrying the lipid
CC molecule in a hydrophobic pocket and transfering it between membranes
CC through the cytosol. Involved in maintenance of intracellular sterol
CC distribution and homeostasis (PubMed:15173322, PubMed:16156791,
CC PubMed:23934110, PubMed:26206936). Catalyzes the lipid countertransport
CC between the endoplasmic reticulum (ER) and the plasma membrane (PM).
CC Specifically exchanges phosphatidylserine (PS) with
CC phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine
CC to the PM in exchange for PI4P, which is delivered to the ER-localized
CC PI4P phosphatase SAC1 for degradation. Thus, by maintaining a PI4P
CC gradient at the ER/PM interface, SAC1 drives PS transport
CC (PubMed:23934110, PubMed:26206936). Binds phosphatidylserine and PI4P
CC in a mutually exclusive manner (PubMed:26206936). Also binds
CC phosphatidic acid (PA) (PubMed:16156791). {ECO:0000269|PubMed:15173322,
CC ECO:0000269|PubMed:16156791, ECO:0000269|PubMed:23934110,
CC ECO:0000269|PubMed:26206936}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000269|PubMed:23934110};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38664;
CC Evidence={ECO:0000269|PubMed:23934110};
CC -!- SUBUNIT: Interacts with the AAA ATPase VPS4; regulates OSH6 membrane
CC association. VPS4 is required for membrane dissociation of OSH6.
CC {ECO:0000269|PubMed:16096648}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16096648,
CC ECO:0000269|PubMed:16156791}. Cell membrane
CC {ECO:0000269|PubMed:16156791, ECO:0000269|PubMed:20008566}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:20008566,
CC ECO:0000269|PubMed:23934110}. Note=Localizes to the cortical
CC endoplasmic reticulum at the endoplasmic reticulum-plasma membrane
CC contact sites. {ECO:0000269|PubMed:20008566,
CC ECO:0000269|PubMed:23934110}.
CC -!- DOMAIN: The OSBP-related domain (ORD) mediates binding of sterols and
CC phospholipids. It displays an incomplete beta-barrel containing a
CC central hydrophobic tunnel that can accommodate a single lipid molecule
CC with a flexible lid covering the tunnel entrance. The ORD can bind two
CC membranes simultaneously. It has at least two membrane-binding
CC surfaces; one near the mouth of the lipid-binding pocket and a distal
CC site that can bind a second membrane. These structural features
CC correlate with the phosphatidylinositol 4-phosphate (PI(4)P)-coupled
CC lipid transport optimized in closely apposed membranes, such as
CC organelle contact sites. The lipid transfer cycle starts from the
CC association of the LTP with a donor membrane, which accompanies
CC conformational changes that uncover the ligand-binding pocket. The
CC tunnel opening is generally mediated by displacement of the lid
CC covering the binding pocket allowing uptake or release of a lipid
CC molecule. The LTPs extract the lipid from the membrane by providing a
CC hydrophobic environment as well as specific interaction. Dissociation
CC from the donor membrane shifts the conformation to a closed form. Then,
CC the LTPs loaded with a cargo lipid diffuse through the aqueous phase.
CC Lid opening may be induced by the interaction of a hydrophobic side of
CC the lid with the target membranes. {ECO:0000305|PubMed:20008566}.
CC -!- MISCELLANEOUS: Present with 2550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
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DR EMBL; X65124; CAA46249.1; -; Genomic_DNA.
DR EMBL; Z28228; CAA82073.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09159.1; -; Genomic_DNA.
DR PIR; S25324; S25324.
DR RefSeq; NP_012928.1; NM_001179793.1.
DR PDB; 4B2Z; X-ray; 1.95 A; A/B=1-448.
DR PDB; 4PH7; X-ray; 2.55 A; A/B/C/D=1-448.
DR PDBsum; 4B2Z; -.
DR PDBsum; 4PH7; -.
DR AlphaFoldDB; Q02201; -.
DR SMR; Q02201; -.
DR BioGRID; 34135; 91.
DR IntAct; Q02201; 24.
DR MINT; Q02201; -.
DR STRING; 4932.YKR003W; -.
DR SwissLipids; SLP:000000525; -.
DR TCDB; 2.D.1.1.3; the pi4p/ps counter transporter (p/p-ct) family.
DR iPTMnet; Q02201; -.
DR MaxQB; Q02201; -.
DR PaxDb; Q02201; -.
DR PRIDE; Q02201; -.
DR EnsemblFungi; YKR003W_mRNA; YKR003W; YKR003W.
DR GeneID; 853872; -.
DR KEGG; sce:YKR003W; -.
DR SGD; S000001711; OSH6.
DR VEuPathDB; FungiDB:YKR003W; -.
DR eggNOG; KOG2210; Eukaryota.
DR GeneTree; ENSGT00940000154690; -.
DR HOGENOM; CLU_012334_4_2_1; -.
DR InParanoid; Q02201; -.
DR OMA; EISGKWS; -.
DR BioCyc; YEAST:G3O-31981-MON; -.
DR PRO; PR:Q02201; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; Q02201; protein.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IDA:SGD.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:SGD.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:SGD.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:SGD.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:SGD.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
DR GO; GO:0005548; F:phospholipid transporter activity; IDA:UniProtKB.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0120015; F:sterol transfer activity; IDA:SGD.
DR GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IGI:SGD.
DR GO; GO:0006887; P:exocytosis; IGI:SGD.
DR GO; GO:0030011; P:maintenance of cell polarity; IGI:SGD.
DR GO; GO:0015914; P:phospholipid transport; IDA:UniProtKB.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IGI:SGD.
DR GO; GO:0055092; P:sterol homeostasis; IMP:SGD.
DR GO; GO:0016125; P:sterol metabolic process; IGI:SGD.
DR GO; GO:0015918; P:sterol transport; IGI:SGD.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR PANTHER; PTHR10972; PTHR10972; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR SUPFAM; SSF144000; SSF144000; 1.
DR PROSITE; PS01013; OSBP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Endoplasmic reticulum;
KW Lipid transport; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..448
FT /note="Oxysterol-binding protein homolog 6"
FT /id="PRO_0000100390"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..391
FT /note="OSBP-related domain (ORD)"
FT /evidence="ECO:0000305"
FT COMPBIAS 12..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64..69
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000269|PubMed:26206936,
FT ECO:0007744|PDB:4PH7"
FT BINDING 64..69
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57262"
FT /evidence="ECO:0000269|PubMed:23934110,
FT ECO:0007744|PDB:4B2Z"
FT BINDING 126..129
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000269|PubMed:26206936,
FT ECO:0007744|PDB:4PH7"
FT BINDING 129
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57262"
FT /evidence="ECO:0000269|PubMed:23934110,
FT ECO:0007744|PDB:4B2Z"
FT BINDING 157..158
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000269|PubMed:26206936,
FT ECO:0007744|PDB:4PH7"
FT BINDING 183
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-L-serine"
FT /ligand_id="ChEBI:CHEBI:57262"
FT /evidence="ECO:0000269|PubMed:23934110,
FT ECO:0007744|PDB:4B2Z"
FT BINDING 351
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000269|PubMed:26206936,
FT ECO:0007744|PDB:4PH7"
FT BINDING 355
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000269|PubMed:26206936,
FT ECO:0007744|PDB:4PH7"
FT BINDING 359
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000269|PubMed:26206936,
FT ECO:0007744|PDB:4PH7"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MUTAGEN 69
FT /note="L->A,D: Strongly reduced binding to
FT phosphatidylserine."
FT /evidence="ECO:0000269|PubMed:23934110"
FT MUTAGEN 69
FT /note="L->D: Strongly reduced binding to phosphatidylserine
FT and phosphatidylinositol 4-phosphate (PI4P)."
FT /evidence="ECO:0000269|PubMed:26206936"
FT MUTAGEN 69
FT /note="L->F: Does not affect binding to
FT phosphatidylserine."
FT /evidence="ECO:0000269|PubMed:23934110"
FT MUTAGEN 71
FT /note="T->P: Abolished binding to phosphatidylserine."
FT /evidence="ECO:0000269|PubMed:23934110"
FT MUTAGEN 73
FT /note="I->D: Strongly reduced binding to
FT phosphatidylserine."
FT /evidence="ECO:0000269|PubMed:23934110"
FT MUTAGEN 126
FT /note="K->A: Strongly reduced binding to
FT phosphatidylserine."
FT /evidence="ECO:0000269|PubMed:23934110"
FT MUTAGEN 129
FT /note="N->A: Strongly reduced binding to
FT phosphatidylserine."
FT /evidence="ECO:0000269|PubMed:23934110"
FT MUTAGEN 157..158
FT /note="HH->AA: Strongly reduced binding to
FT phosphatidylinositol 4-phosphate (PI4P). Does not affect
FT binding to phosphatidylserine."
FT /evidence="ECO:0000269|PubMed:26206936"
FT MUTAGEN 157
FT /note="H->A: Does not affect binding to
FT phosphatidylserine."
FT /evidence="ECO:0000269|PubMed:23934110"
FT MUTAGEN 158
FT /note="H->A: Does not affect binding to
FT phosphatidylserine."
FT /evidence="ECO:0000269|PubMed:23934110"
FT MUTAGEN 182
FT /note="K->A: Does not affect binding to
FT phosphatidylserine."
FT /evidence="ECO:0000269|PubMed:23934110"
FT MUTAGEN 351
FT /note="K->A: Does not affect binding to
FT phosphatidylserine."
FT /evidence="ECO:0000269|PubMed:23934110"
FT MUTAGEN 351
FT /note="K->E: Strongly reduced binding to
FT phosphatidylinositol 4-phosphate (PI4P). Does not affect
FT binding to phosphatidylserine."
FT /evidence="ECO:0000269|PubMed:26206936"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:4B2Z"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:4B2Z"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:4B2Z"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:4B2Z"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:4B2Z"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:4B2Z"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 147..156
FT /evidence="ECO:0007829|PDB:4B2Z"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:4B2Z"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 197..206
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 263..271
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:4B2Z"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:4B2Z"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:4B2Z"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:4B2Z"
FT HELIX 333..340
FT /evidence="ECO:0007829|PDB:4B2Z"
FT HELIX 344..367
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:4B2Z"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:4B2Z"
FT HELIX 400..410
FT /evidence="ECO:0007829|PDB:4B2Z"
FT HELIX 421..424
FT /evidence="ECO:0007829|PDB:4B2Z"
FT HELIX 427..433
FT /evidence="ECO:0007829|PDB:4B2Z"
FT HELIX 436..440
FT /evidence="ECO:0007829|PDB:4PH7"
SQ SEQUENCE 448 AA; 51588 MW; 44C4E16CF320DB78 CRC64;
MGSKKLTVGS DSHRLSKSSF SSNKSSHSAT KDQPIDTDDI DEDDESGHNI ILNIISQLRP
GCDLTRITLP TFILEKKSML ERVTNQLQFP EFLLQAHSEK DPLKRFLYVM KWYLAGWHIA
PKAVKKPLNP VLGEYFTAYW DLPNKQQAYY ISEQTSHHPP ECAYFYMIPE SSIRVDGVVI
PKSRFLGNSS AAMMDGSTVL QFLDIKDGNG KPEKYVLTQP NVYVRGILFG KMRIELGDHM
IIKSPNFQAD IEFKTKGYVF GTYDAIEGTV KDYDGNAYYE ISGKWNDVMY LKDLKQPRSS
PKVFLDTHKE SPLRPKVRPL SEQGEYESRK LWKKVTDALA VRNHPVATEE KFQIEDHQRQ
LAKKRIEDGV EFHPKLFRRS KPGEDLDYCI YKNIPVDEDP EKQIRSILQI APILPGQQFT
DKFFIPAFEK IKSQKKMIEN EKQNPAKQ
