SFH5_BOTFB
ID SFH5_BOTFB Reviewed; 579 AA.
AC A6S3N2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Phosphatidylinositol transfer protein sfh5;
DE Short=PITP sfh5;
GN Name=sfh5; ORFNames=BC1G_07204;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
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; CH476881; EDN27419.1; -; Genomic_DNA.
DR RefSeq; XP_001554067.1; XM_001554017.1.
DR AlphaFoldDB; A6S3N2; -.
DR SMR; A6S3N2; -.
DR PRIDE; A6S3N2; -.
DR GeneID; 5434592; -.
DR KEGG; bfu:BCIN_07g04880; -.
DR OMA; LAACEFN; -.
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; Transport.
FT CHAIN 1..579
FT /note="Phosphatidylinositol transfer protein sfh5"
FT /id="PRO_0000324972"
FT DOMAIN 388..563
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 135..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 413
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT BINDING 433
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT BINDING 467
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT BINDING 469
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 503
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
SQ SEQUENCE 579 AA; 63764 MW; 22E7AD4F0E303209 CRC64;
MGYKNSVRKI LGNIFKPKIL KAKRQGAEGQ LNVVQRPRSV IFLKAGVRLS RTPDTCVQNI
AKERCDKVIG DKIPYGPSNQ ASSFAGQLGL KREKEINEEV GGWTKVVYKV EADLVEKEEE
KAGLAGWDGL GFESNTKMSA EPNNNQAKAD VPEEVVEPKP TTVEEPKSTT VEEPKSTTVE
ESKSTTVEEP KSTTAEQPKS TIEQDPKPST TESSPVQIDD STPIPQITTE EPKPTVAEPS
TTESVTAEPT TEQPQEAAVK LESVKEADAE AAAKLEATKD ADVEKAASTS QHSVSFDKAT
KTHDGSPLSK FYSELPAILE AAEYNEMWGI VLDPSETHVQ TSIVLEKFLR ANAKDVPKAK
AQLIEALKWR KTMQPQKLLE STEFDKVKFG NLGYVTSYNT TEGGKEVITW NIYGAVKDVK
KTFSDVPEFL KWRAALMELS IKELDLASAT EKIPENGPDP YRMIQVHDYL NVSFLRMDPS
IRAASKETIQ TFSMAYPELL KEKFFVNVPL VMGWVFTAMK IFLSADTIKK FHPLSYGSNL
GSEIPNVAEQ LPKEYGGKGG ELKSGLTVKY SEGEASKTA
