SFH5_YEAST
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 03-AUG-2022, entry version 151.
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 AlphaFoldDB; P47008; -.
DR SMR; P47008; -.
DR BioGRID; 33613; 61.
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; P47008; -.
DR PRIDE; P47008; -.
DR EnsemblFungi; YJL145W_mRNA; YJL145W; YJL145W.
DR GeneID; 853296; -.
DR KEGG; sce:YJL145W; -.
DR SGD; S000003681; SFH5.
DR VEuPathDB; FungiDB:YJL145W; -.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_045138_0_1_1; -.
DR InParanoid; P47008; -.
DR OMA; RKEFNPL; -.
DR BioCyc; YEAST:G3O-31589-MON; -.
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; -; 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 Cytoplasm; Endoplasmic reticulum; Heme; Iron; Lipid transport; Membrane;
KW Metal-binding; Microsome; Reference proteome; 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"
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
