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SFH5_PHANO
ID   SFH5_PHANO              Reviewed;         331 AA.
AC   Q0V0B0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Phosphatidylinositol transfer protein SFH5;
DE            Short=PITP SFH5;
GN   Name=SFH5; ORFNames=SNOG_02554;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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; CH445327; EAT90766.1; -; Genomic_DNA.
DR   RefSeq; XP_001793157.1; XM_001793105.1.
DR   AlphaFoldDB; Q0V0B0; -.
DR   SMR; Q0V0B0; -.
DR   STRING; 13684.SNOT_02554; -.
DR   EnsemblFungi; SNOT_02554; SNOT_02554; SNOG_02554.
DR   GeneID; 5970007; -.
DR   KEGG; pno:SNOG_02554; -.
DR   eggNOG; KOG1471; Eukaryota.
DR   HOGENOM; CLU_045138_0_1_1; -.
DR   InParanoid; Q0V0B0; -.
DR   OMA; MLQVHDY; -.
DR   OrthoDB; 1182715at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0032541; C:cortical endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008526; F:phosphatidylinositol transfer activity; IBA:GO_Central.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IBA:GO_Central.
DR   GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
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; IPR011074; CRAL/TRIO_N_dom.
DR   InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR   InterPro; IPR042938; Sfh5.
DR   PANTHER; PTHR47669; PTHR47669; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF03765; CRAL_TRIO_N; 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..331
FT                   /note="Phosphatidylinositol transfer protein SFH5"
FT                   /id="PRO_0000324985"
FT   DOMAIN          148..322
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         173
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         193
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         229
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         231
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         265
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
SQ   SEQUENCE   331 AA;  36669 MW;  396C3E9838B2A3C0 CRC64;
     MPVVESDEKV DDTAKDLSSL GLSDKETARG EEKEEKGTVA APSAPTVDTV QPTTGPSWPA
     TAPDHPLSKF YDIFEDVIKS AEHNEVYGIL LTKENPFQTK LILQKFLRAN QNDLDKAKQQ
     LLETLKWRKE FDPVKATGEK FDKTRFGGLG YVLEVQGVPE SKNEKDVVTF NIYGAVKDKK
     ATFGDLEGFL RWRVGLMEKS VQKLNLASAT TPVPNYGEGP DPYQGFQIHD YLQVSFLRQD
     PAVKAATSKT IEVLGRYYPE TLSRKFFVNV PVIMGWMYTA AKLIVAKETA KKFAVLSYGN
     QLAGELGVDI PAVYGGTKED LESVAEGMSL E
 
 
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