ID B0Y2X5_ASPFC Unreviewed; 424 AA.
AC B0Y2X5;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 03-MAY-2023, entry version 64.
DE RecName: Full=Phosphatidylinositol transfer protein SFH5 {ECO:0000256|ARBA:ARBA00018320, ECO:0000256|RuleBase:RU367059};
DE Short=PITP SFH5 {ECO:0000256|RuleBase:RU367059};
GN ORFNames=AFUB_052200 {ECO:0000313|EMBL:EDP51216.1};
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP51216.1, ECO:0000313|Proteomes:UP000001699};
RN [1] {ECO:0000313|EMBL:EDP51216.1, ECO:0000313|Proteomes:UP000001699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC {ECO:0000313|Proteomes:UP000001699};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS499597; EDP51216.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y2X5; -.
DR EnsemblFungi; EDP51216; EDP51216; AFUB_052200.
DR VEuPathDB; FungiDB:AFUB_052200; -.
DR HOGENOM; CLU_045138_1_0_1; -.
DR PhylomeDB; B0Y2X5; -.
DR Proteomes; UP000001699; 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; IPR011074; CRAL/TRIO_N_dom.
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 Pfam; PF03765; CRAL_TRIO_N; 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 228..363
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 46200 MW; 3999874414C98519 CRC64;
MSVTMADQQP EKTTAPASDV ADSQPAVVSN TDTRKETTET AEPQSEDKTA TTTAQPAVET
TATQSGTAET PAEADKAPAE VQQPPQAEEE KPVAQQPEQP AYLAKNPALS QFFERLPAIV
SSSGHAEMWS VPLKDSNDAP TVNVLIKFLR ANEGNVKLAE EQLTKALKWR KETNPSALAE
STSYSATKFG GLGYLTTYKE ANGAETVVTW NIYGGVKDIN TTFGDMNEFV KWRVALMELA
VKELKMAEAT SVIDYDGEDP YQMIQVHDYQ NVSFLRLNPA IKAATKKTIE VFTTAYPELL
REKFFVNVPA IMGWMFAAMK VFLSKNTTRK FHPISNGANL AREFPSLKDQ FPKVYGGSAP
ALQEGARTVS LIQDESAPAA TEQSKEQANK EEAAQEESKP ESAPEQPKAD PDVIVQEAPA
ADAK
//
