SFH5_ASPOR
ID SFH5_ASPOR Reviewed; 455 AA.
AC Q2UA18;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Phosphatidylinositol transfer protein sfh5;
DE Short=PITP sfh5;
GN Name=sfh5; ORFNames=AO090102000579;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007162; BAE61597.1; -; Genomic_DNA.
DR RefSeq; XP_001822730.1; XM_001822678.2.
DR AlphaFoldDB; Q2UA18; -.
DR SMR; Q2UA18; -.
DR STRING; 510516.Q2UA18; -.
DR EnsemblFungi; BAE61597; BAE61597; AO090102000579.
DR GeneID; 5994775; -.
DR KEGG; aor:AO090102000579; -.
DR VEuPathDB; FungiDB:AO090102000579; -.
DR HOGENOM; CLU_045138_1_0_1; -.
DR OMA; MLQVHDY; -.
DR Proteomes; UP000006564; Chromosome 4.
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; 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..455
FT /note="Phosphatidylinositol transfer protein sfh5"
FT /id="PRO_0000324970"
FT DOMAIN 179..367
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 216
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT BINDING 236
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT BINDING 270
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT BINDING 272
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 306
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
SQ SEQUENCE 455 AA; 49460 MW; 2BB20CF59453D363 CRC64;
MADQQEKTAS SAVPETQPPS QTAETTTQTT ATPAPEVQTE QTQPTESGPS AANTTTEQPT
NPPAAEASKE NAAPAPAPAA EDAPSEPAPA QEQQKEEKPA DNKPEYLAKN PALSQLFDRL
PTVLSNSGHD EMWGVPLRDS SDVPTVNVLI KFLRANEGNV KLAEDQLTKA LQWRKQTRPT
ALVEGRYSAK KFGGLGYLST YKDADGKETV ITWNIYGGVK DLGTTFGNVD EFINWRVALM
ELAVKDLKMD QATSVIDYEG EDPYQMIQVH DYLNVSFLRM NPSVKAATKK TIDVFATAYP
ELLREKFFVN VPSIMGWMFA AIKVFLSKNT TRKFHPISNG ANLAREFPPA VKEQFPKVYG
GSAPDLHEGA RTVALEEDNE PAPAPAAPAE PTEEAKPEQE APKQEPAPEA PKEEAIKEAL
VEAPKEEPKQ PAVEEPAKTD TAVTTQETVA PAEAK
