SFH5_CHAGB
ID SFH5_CHAGB Reviewed; 436 AA.
AC Q2GLX8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Phosphatidylinositol transfer protein SFH5;
DE Short=PITP SFH5;
GN Name=SFH5; ORFNames=CHGG_11078;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408038; EAQ82902.1; -; Genomic_DNA.
DR RefSeq; XP_001230254.1; XM_001230253.1.
DR AlphaFoldDB; Q2GLX8; -.
DR SMR; Q2GLX8; -.
DR STRING; 38033.XP_001230254.1; -.
DR PRIDE; Q2GLX8; -.
DR EnsemblFungi; EAQ82902; EAQ82902; CHGG_11078.
DR GeneID; 4397379; -.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_045138_1_1_1; -.
DR InParanoid; Q2GLX8; -.
DR OMA; CAYTASI; -.
DR OrthoDB; 1182715at2759; -.
DR Proteomes; UP000001056; 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: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; Reference proteome; Transport.
FT CHAIN 1..436
FT /note="Phosphatidylinositol transfer protein SFH5"
FT /id="PRO_0000324975"
FT DOMAIN 248..427
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 60..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 273
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT BINDING 293
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT BINDING 326
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT BINDING 328
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 362
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
SQ SEQUENCE 436 AA; 47069 MW; 3B4FE74FB274BC96 CRC64;
MYGRSVQDCA YTASIGMIAQ GQNDFAANGR IWLGLLAPHD RGRGLGLGCE CLRPIKMSAV
EQKPSEQPAP TTVAPDTVST PEPAVAAAAD NATAAPAPSE TPATPAAPAA PDASGAQDTP
ATAGADSEVP APTETKELVE TKEPAEKKEP AETKEAPVEK APVDDKTPIT QLWATAKATG
HPEIWGVTLA DPETHVPTRI ILQKYLNAND ADLDKAKDQL TKTLEWRAKT KPLELVKKAF
SKTKFDGLGY VTKYVQDGST EPEAKEVFTW NIYGGVKSID ETFGKLEEFL DWRVALMELA
LQELDLASAT KLITAEYDPY KIFQVHDYKS ISFLRQSPQV KSASAETIKV FAQNYPELLK
EKFFVNVPAI MGFVYAFMKL FVAPKTIKKF HPMSNGGSLA VEFADSKVAA LGEKLPANYG
GKGAELEEQG KGPLLE
