SFH5_CANAL
ID SFH5_CANAL Reviewed; 320 AA.
AC Q5AP66; A0A1D8PEV7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Phosphatidylinositol transfer protein SFH5;
DE Short=PITP SFH5;
GN Name=SFH5; OrderedLocusNames=CAALFM_C110270CA;
GN ORFNames=CaO19.12362, CaO19.4897;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017623; AOW26657.1; -; Genomic_DNA.
DR RefSeq; XP_723579.1; XM_718486.2.
DR AlphaFoldDB; Q5AP66; -.
DR SMR; Q5AP66; -.
DR STRING; 237561.Q5AP66; -.
DR PRIDE; Q5AP66; -.
DR GeneID; 3634884; -.
DR KEGG; cal:CAALFM_C110270CA; -.
DR CGD; CAL0000192835; SFH5.
DR VEuPathDB; FungiDB:C1_10270C_A; -.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_045138_0_1_1; -.
DR InParanoid; Q5AP66; -.
DR OMA; RKEFNPL; -.
DR OrthoDB; 1182715at2759; -.
DR PRO; PR:Q5AP66; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IBA:GO_Central.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IBA:GO_Central.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:EnsemblFungi.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IEA:EnsemblFungi.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
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..320
FT /note="Phosphatidylinositol transfer protein SFH5"
FT /id="PRO_0000324973"
FT DOMAIN 120..285
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT BINDING 134
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT BINDING 165
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT BINDING 190
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT BINDING 192
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 226
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250|UniProtKB:A6ZQI5"
SQ SEQUENCE 320 AA; 36660 MW; DD94730133076475 CRC64;
MSSSIEEVKA TIKSVKLTDS QAEKLSKLID SLPKILSGLD NPEYDEIFGY RINTKDKPYV
DESIRNEILL KFLAADDYNL ELSEKRLIDS LNWRNEFQPL SAAFEETFDK ELNELGVITN
FPNSNLKITT WNLYGNLKNP KKIFEKFGAN NKVSKLPGSQ FLRWRVGLME KSLQLIDFTS
TTDNRIAQVH DYNNVSMFKI DPGMKKATKE IITIFGANYP ELLSTKFFIN VPLIMGWVFT
FFKTIRVITE ATLKKFQVLN HGNLSESFNP DELPKVYGGK VEKSLFDIDV SDDIKLSEYG
EVILKKVGDE EINHINDDVE
