ID X0MSM4_FUSOX Unreviewed; 413 AA.
AC X0MSM4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Phosphatidylinositol transfer protein SFH5 {ECO:0000256|RuleBase:RU367059};
DE Short=PITP SFH5 {ECO:0000256|RuleBase:RU367059};
GN ORFNames=FOTG_09224 {ECO:0000313|EMBL:EXM23340.1};
OS Fusarium oxysporum f. sp. vasinfectum 25433.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089449 {ECO:0000313|EMBL:EXM23340.1};
RN [1] {ECO:0000313|EMBL:EXM23340.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=25433 {ECO:0000313|EMBL:EXM23340.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum Cotton.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXM23340.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=25433 {ECO:0000313|EMBL:EXM23340.1};
RG The Broad Institute Genomics Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Annotation of Fusarium oxysporum Cotton.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00024180}.
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:0000256|ARBA:ARBA00024146};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692;
CC Evidence={ECO:0000256|ARBA:ARBA00024146};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367059}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406,
CC ECO:0000256|RuleBase:RU367059}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004406, ECO:0000256|RuleBase:RU367059}.
CC Microsome membrane {ECO:0000256|RuleBase:RU367059}; Peripheral membrane
CC protein {ECO:0000256|RuleBase:RU367059}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the SFH5 family. {ECO:0000256|ARBA:ARBA00006667,
CC ECO:0000256|RuleBase:RU367059}.
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DR EMBL; KK035209; EXM23340.1; -; Genomic_DNA.
DR AlphaFoldDB; X0MSM4; -.
DR HOGENOM; CLU_045138_1_1_1; -.
DR Proteomes; UP000030701; 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:UniProtKB-UniRule.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 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; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SFH5; 1.
DR PANTHER; PTHR47669:SF1; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN SFH5; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU367059};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU367059}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055,
KW ECO:0000256|RuleBase:RU367059};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367059};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Microsome {ECO:0000256|ARBA:ARBA00022848, ECO:0000256|RuleBase:RU367059};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367059}.
FT DOMAIN 142..278
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 44487 MW; E3AE8AF2ED919ED7 CRC64;
MAAEQEKTVP AAVPAENPAT PEAPLTKLNA RLEDIFSKTL HKEMWGVQLT NIDHVPTKVV
LQKFLHANND DPVAAEKQLT QALEWRKKMN PTALVTQTFD KSKFGDLGYV TVHKGENGKE
TIITWNIYGA VKDNKATFGN VEEFIKWRAA IMELSVQKLK LDQVTEPIPE GGEDPYQMIQ
VHDYLNVSFF RMDPAVKAAS KETISVFSMA YPELLAHKYF VNVPAIMGWM FGAMKLFLTP
ATLRKFHPMT SGTTLATELK GIVSTLPKEY GGQGASVKEG MSVSLTEAGE SASGETSAEP
SPTEVPEQTA AADSTTAEKT VVTRESAPAT EKTLTAEPIV AAAAPAPALA AEAAPAPIPA
PVEAAKAETA EQAVEQAGEK PIEEALEKLS VNPAESEKKD TLATDVEKKE TAA
//
