SFH5_SCLS1
ID SFH5_SCLS1 Reviewed; 413 AA.
AC A7EXH9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Phosphatidylinositol transfer protein sfh5;
DE Short=PITP sfh5;
GN Name=sfh5; ORFNames=SS1G_10044;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476634; EDN94171.1; -; Genomic_DNA.
DR RefSeq; XP_001589405.1; XM_001589355.1.
DR AlphaFoldDB; A7EXH9; -.
DR SMR; A7EXH9; -.
DR STRING; 665079.A7EXH9; -.
DR GeneID; 5485303; -.
DR KEGG; ssl:SS1G_10044; -.
DR VEuPathDB; FungiDB:sscle_01g003380; -.
DR InParanoid; A7EXH9; -.
DR OMA; LAACEFN; -.
DR Proteomes; UP000001312; 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..413
FT /note="Phosphatidylinositol transfer protein sfh5"
FT /id="PRO_0000324988"
FT DOMAIN 222..397
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 247
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT BINDING 267
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT BINDING 301
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT BINDING 303
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 337
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
SQ SEQUENCE 413 AA; 45780 MW; 602DBCB6BDDBEA28 CRC64;
MSAEVDTNIP KENVPEEVVE AKTTTTTTTM EPEPLIVEDL KSTTIESTPV KIGDPTSNEQ
IAREEPKPTI TEPSTTKSVA AEPTTEQHQE TAVKLESVKE ADAEAAARVE STEDADGEKA
LSTSQPSVSF DKTTKTHDGS PLSKFFSELP EILKVAGHNE MWGIILDPSE DHVQTSIVLE
KFLRANTKDV TKAKAQLTEA LKWRKAMQPQ KLLVDTEFDK VKFGKLGYVT SYPTSEGGKE
VITWNIYGAV KDTKKTFSDV PEFLRWRAAL MELSIRELDL ASATEKIPEN GPDPYRMIQV
HDYLNVSFLR MDPGIRAASK ETIQTFSMAY PELLKEKFFV NVPMVMGWVF TAMKIFLSAD
TIKKFHPLSY GSDLGAEIPG IAEKLPKEYG GKGEELESGF TVKYSGDDVP KSD
