SFH5_YEAS7
ID SFH5_YEAS7 Reviewed; 294 AA.
AC A6ZQI5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Phosphatidylinositol transfer protein SFH5;
DE Short=PITP SFH5;
DE AltName: Full=SEC14 homolog 5;
GN Name=SFH5; ORFNames=SCY_3146;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH HEME, AND FUNCTION.
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 (By similarity). Heme-binding
CC protein that may play a role in organic oxidant-induced stress
CC responses (PubMed:32780017). {ECO:0000250|UniProtKB:P47008,
CC 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:0000250|UniProtKB:P47008};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC Evidence={ECO:0000250|UniProtKB:P47008};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:32780017};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47008}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P47008};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P47008}. Microsome
CC membrane {ECO:0000250|UniProtKB:P47008}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P47008}.
CC -!- SIMILARITY: Belongs to the SFH5 family. {ECO:0000305}.
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DR EMBL; AAFW02000044; EDN63237.1; -; Genomic_DNA.
DR PDB; 6W32; X-ray; 2.90 A; A/B=1-294.
DR PDBsum; 6W32; -.
DR AlphaFoldDB; A6ZQI5; -.
DR SMR; A6ZQI5; -.
DR PRIDE; A6ZQI5; -.
DR EnsemblFungi; EDN63237; EDN63237; SCY_3146.
DR HOGENOM; CLU_045138_0_1_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IEA:InterPro.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR042938; Sfh5.
DR PANTHER; PTHR47669; PTHR47669; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; SSF52087; 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; Transport.
FT CHAIN 1..294
FT /note="Phosphatidylinositol transfer protein SFH5"
FT /id="PRO_0000324991"
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:0000269|PubMed:32780017"
FT BINDING 148
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:32780017"
FT BINDING 173
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:32780017"
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:0000269|PubMed:32780017"
FT BINDING 209
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:32780017"
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
