ID   SFH5_YEAST              Reviewed;         294 AA.
AC   P47008; D6VW40; Q6Q535;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Phosphatidylinositol transfer protein SFH5;
DE            Short=PITP SFH5;
DE   AltName: Full=SEC14 homolog 5;
GN   Name=SFH5; OrderedLocusNames=YJL145W; ORFNames=J0644;
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 96604 / S288c / FY1679;
RX   PubMed=8813765;
RX   DOI=10.1002/(sici)1097-0061(19960630)12:8<787::aid-yea954>3.0.co;2-4;
RA   Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.;
RT   "Sequence analysis of a 40.7 kb segment from the left arm of yeast
RT   chromosome X reveals 14 known genes and 13 new open reading frames
RT   including homologues of genes clustered on the right arm of chromosome
RT   XI.";
RL   Yeast 12:787-797(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, PHOSPHATIDYLINOSITOL-BINDING, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=10848624; DOI=10.1091/mbc.11.6.1989;
RA   Li X., Routt S.M., Xie Z., Cui X., Fang M., Kearns M.A., Bard M.,
RA   Kirsch D.R., Bankaitis V.A.;
RT   "Identification of a novel family of nonclassic yeast phosphatidylinositol
RT   transfer proteins whose function modulates phospholipase D activity and
RT   Sec14p-independent cell growth.";
RL   Mol. Biol. Cell 11:1989-2005(2000).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12869188; DOI=10.1046/j.1432-1033.2003.03688.x;
RA   Schnabl M., Oskolkova O.V., Holic R., Brezna B., Pichler H., Zagorsek M.,
RA   Kohlwein S.D., Paltauf F., Daum G., Griac P.;
RT   "Subcellular localization of yeast Sec14 homologues and their involvement
RT   in regulation of phospholipid turnover.";
RL   Eur. J. Biochem. 270:3133-3145(2003).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [8]
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   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16709158; DOI=10.1042/bst0340346;
RA   Mousley C.J., Tyeryar K.R., Ryan M.M., Bankaitis V.A.;
RT   "Sec14p-like proteins regulate phosphoinositide homoeostasis and
RT   intracellular protein and lipid trafficking in yeast.";
RL   Biochem. Soc. Trans. 34:346-350(2006).
RN   [10]
RP   FUNCTION, AND HEME-BINDING.
RX   PubMed=32780017; DOI=10.7554/elife.57081;
RA   Khan D., Lee D., Gulten G., Aggarwal A., Wofford J., Krieger I.,
RA   Tripathi A., Patrick J.W., Eckert D.M., Laganowsky A., Sacchettini J.,
RA   Lindahl P., Bankaitis V.A.;
RT   "A Sec14-like phosphatidylinositol transfer protein paralog defines a novel
RT   class of heme-binding proteins.";
RL   Elife 9:0-0(2020).
CC   -!- FUNCTION: Non-classical phosphatidylinositol (PtdIns) transfer protein
CC       (PITP), which exhibits PtdIns-binding/transfer activity in the absence
CC       of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2
CC       homeostasis at the plasma membrane. Heme-binding protein that may play
CC       a role in organic oxidant-induced stress responses (PubMed:32780017).
CC       {ECO:0000269|PubMed:10848624, ECO:0000269|PubMed:12869188,
CC       ECO:0000269|PubMed:16709158, ECO:0000269|PubMed:32780017}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a
CC         1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out);
CC         Xref=Rhea:RHEA:38691, ChEBI:CHEBI:57880;
CC         Evidence={ECO:0000269|PubMed:10848624};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC         Evidence={ECO:0000269|PubMed:10848624};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000269|PubMed:32780017};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10848624,
CC       ECO:0000269|PubMed:12869188, ECO:0000269|PubMed:14562095}. Endoplasmic
CC       reticulum membrane {ECO:0000269|PubMed:16709158}; Peripheral membrane
CC       protein {ECO:0000269|PubMed:16709158}. Microsome membrane
CC       {ECO:0000269|PubMed:12869188, ECO:0000269|PubMed:16709158}; Peripheral
CC       membrane protein {ECO:0000269|PubMed:16709158}.
CC   -!- MISCELLANEOUS: Present with 6540 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SFH5 family. {ECO:0000305}.
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DR   EMBL; X87371; CAA60810.1; -; Genomic_DNA.
DR   EMBL; Z49420; CAA89440.1; -; Genomic_DNA.
DR   EMBL; AY558583; AAS56909.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08656.1; -; Genomic_DNA.
DR   PIR; S55168; S55168.
DR   RefSeq; NP_012390.1; NM_001181578.1.
DR   PDB; 6W32; X-ray; 2.90 A; A/B/C=1-294.
DR   PDBsum; 6W32; -.
DR   AlphaFoldDB; P47008; -.
DR   SMR; P47008; -.
DR   BioGRID; 33613; 67.
DR   IntAct; P47008; 2.
DR   MINT; P47008; -.
DR   STRING; 4932.YJL145W; -.
DR   SwissLipids; SLP:000000358; -.
DR   CarbonylDB; P47008; -.
DR   iPTMnet; P47008; -.
DR   MaxQB; P47008; -.
DR   PaxDb; 4932-YJL145W; -.
DR   PeptideAtlas; P47008; -.
DR   EnsemblFungi; YJL145W_mRNA; YJL145W; YJL145W.
DR   GeneID; 853296; -.
DR   KEGG; sce:YJL145W; -.
DR   AGR; SGD:S000003681; -.
DR   SGD; S000003681; SFH5.
DR   VEuPathDB; FungiDB:YJL145W; -.
DR   eggNOG; KOG1471; Eukaryota.
DR   HOGENOM; CLU_045138_0_1_1; -.
DR   InParanoid; P47008; -.
DR   OMA; KRVVTWN; -.
DR   OrthoDB; 53323at2759; -.
DR   BioCyc; YEAST:G3O-31589-MONOMER; -.
DR   BioGRID-ORCS; 853296; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P47008; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47008; Protein.
DR   GO; GO:0071944; C:cell periphery; IDA:SGD.
DR   GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008526; F:phosphatidylinositol transfer activity; IDA:SGD.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IGI:SGD.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IGI:SGD.
DR   GO; GO:0015914; P:phospholipid transport; IDA:SGD.
DR   GO; GO:2000114; P:regulation of establishment of cell polarity; IGI:SGD.
DR   GO; GO:0017157; P:regulation of exocytosis; IGI:SGD.
DR   CDD; cd00170; SEC14; 1.
DR   Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   InterPro; IPR042938; Sfh5.
DR   PANTHER; PTHR47669; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SFH5; 1.
DR   PANTHER; PTHR47669:SF1; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SFH5; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Endoplasmic reticulum; Heme; Iron;
KW   Lipid transport; Membrane; Metal-binding; Microsome; Reference proteome;
KW   Transport.
FT   CHAIN           1..294
FT                   /note="Phosphatidylinositol transfer protein SFH5"
FT                   /id="PRO_0000203033"
FT   DOMAIN          100..266
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   BINDING         128
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         148
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         173
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         175
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="proximal binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         209
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   CONFLICT        70
FT                   /note="F -> S (in Ref. 4; AAS56909)"
FT                   /evidence="ECO:0000305"
FT   HELIX           6..26
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   HELIX           47..49
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   HELIX           54..67
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   TURN            68..70
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   HELIX           72..88
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   HELIX           91..96
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   HELIX           102..105
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   STRAND          108..112
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   STRAND          121..126
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   HELIX           128..131
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   TURN            135..139
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   HELIX           141..156
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   STRAND          164..174
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   HELIX           185..201
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   STRAND          206..213
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   HELIX           216..218
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   HELIX           219..226
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   HELIX           231..234
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   STRAND          237..242
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   HELIX           243..248
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   HELIX           255..258
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   HELIX           267..270
FT                   /evidence="ECO:0007829|PDB:6W32"
FT   HELIX           279..288
FT                   /evidence="ECO:0007829|PDB:6W32"
SQ   SEQUENCE   294 AA;  34388 MW;  E75B80F3AB56EF70 CRC64;
     MKFDNDSEKQ VFDKLKKAIP GIIKEKCAGY DELYGYKLNP EGLTQEEVDK YYDEKIADRL
     TYKLCKAYQF EYSTIVQNLI DILNWRREFN PLSCAYKEVH NTELQNVGIL TFDANGDANK
     KAVTWNLYGQ LVKKKELFQN VDKFVRYRIG LMEKGLSLLD FTSSDNNYMT QVHDYKGVSV
     WRMDSDIKNC SKTVIGIFQK YYPELLYAKY FVNVPTVFGW VYDLIKKFVD ETTRKKFVVL
     TDGSKLGQYL KDCPYEGYGG KDKKNNLTKQ NVTNVHPTEY GLYILQKQII EDVE
//