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SFH5_PICGU
ID   SFH5_PICGU              Reviewed;         336 AA.
AC   A5DEQ9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Phosphatidylinositol transfer protein SFH5;
DE            Short=PITP SFH5;
GN   Name=SFH5; ORFNames=PGUG_01760;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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.
CC       {ECO:0000250|UniProtKB:P47008}.
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:0000250|UniProtKB:A6ZQI5};
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; CH408156; EDK37662.2; -; Genomic_DNA.
DR   RefSeq; XP_001486089.1; XM_001486039.1.
DR   AlphaFoldDB; A5DEQ9; -.
DR   SMR; A5DEQ9; -.
DR   STRING; 4929.XP_001486089.1; -.
DR   PRIDE; A5DEQ9; -.
DR   EnsemblFungi; EDK37662; EDK37662; PGUG_01760.
DR   GeneID; 5127890; -.
DR   KEGG; pgu:PGUG_01760; -.
DR   VEuPathDB; FungiDB:PGUG_01760; -.
DR   eggNOG; KOG1471; Eukaryota.
DR   HOGENOM; CLU_045138_0_1_1; -.
DR   InParanoid; A5DEQ9; -.
DR   OMA; RKEFNPL; -.
DR   OrthoDB; 1182715at2759; -.
DR   Proteomes; UP000001997; 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; IPR036273; CRAL/TRIO_N_dom_sf.
DR   InterPro; IPR042938; Sfh5.
DR   PANTHER; PTHR47669; PTHR47669; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF46938; SSF46938; 1.
DR   SUPFAM; SSF52087; SSF52087; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endoplasmic reticulum; Heme; Iron; Lipid transport; Membrane;
KW   Metal-binding; Microsome; Reference proteome; Transport.
FT   CHAIN           1..336
FT                   /note="Phosphatidylinositol transfer protein SFH5"
FT                   /id="PRO_0000324986"
FT   DOMAIN          144..308
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         158
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         188
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         213
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         215
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         249
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
SQ   SEQUENCE   336 AA;  38525 MW;  E2A91322A12C738D CRC64;
     MSEPIEKPVE KPGVEPVSDV KDTDPAKKDQ PVLVSTTKLT KTQSETLKKL IDELPQILEE
     TGDSSYDEIY GYRINKSGLE HVHDEIRNEI VLKFLIAEEY KFEEARTRLI NTFKWRKKFQ
     PLSAAYSETF DKELDDLGVI TKYDGTNENL HVVTWNLYGN LKSPKKLFQK FGQDDKAEKE
     GSPFLRWRIG LMERALSLID FTDKSNSKIA QVHDYNNVSM FRMDPGMKAA TKEIIKIFGD
     NYPELLSTKF FINVPTIMSW VFTFFRTIGL VSEDTWKKFQ VLNSGNLATW FGEKNLPKAY
     NGSNDSTVES LFASEAKTEA PEYAKIMIHK AALDID
 
 
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