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SFH5_EMENI
ID   SFH5_EMENI              Reviewed;         409 AA.
AC   Q5ATZ7; C8V7F5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Phosphatidylinositol transfer protein sfh5;
DE            Short=PITP sfh5;
GN   Name=sfh5; ORFNames=AN8233;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000144; EAA58889.1; -; Genomic_DNA.
DR   EMBL; BN001302; CBF74167.1; -; Genomic_DNA.
DR   RefSeq; XP_681502.1; XM_676410.1.
DR   AlphaFoldDB; Q5ATZ7; -.
DR   SMR; Q5ATZ7; -.
DR   STRING; 162425.CADANIAP00004285; -.
DR   EnsemblFungi; CBF74167; CBF74167; ANIA_08233.
DR   EnsemblFungi; EAA58889; EAA58889; AN8233.2.
DR   GeneID; 2869214; -.
DR   KEGG; ani:AN8233.2; -.
DR   VEuPathDB; FungiDB:AN8233; -.
DR   eggNOG; KOG1471; Eukaryota.
DR   HOGENOM; CLU_045138_1_0_1; -.
DR   InParanoid; Q5ATZ7; -.
DR   OMA; MLQVHDY; -.
DR   OrthoDB; 1182715at2759; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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: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; 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..409
FT                   /note="Phosphatidylinositol transfer protein sfh5"
FT                   /id="PRO_0000324979"
FT   DOMAIN          199..375
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   REGION          1..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..409
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         224
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         244
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         278
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         280
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         314
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
SQ   SEQUENCE   409 AA;  44576 MW;  921B3D3CFF8A563D CRC64;
     MAEQAKLPDQ AQPVPETQVP DNGKPEQQPT ATESAPAPEP ATTEPTTAAT APSAVDGTGE
     TAPAAPEPAA APVAAAAAAP APEPTKSEPQ PAVGEQSEPA KKDEPAKPEY FTKTPALEQF
     FDRLPTILSN TGHQEMWGVP LKHEVTDIPT INVLIKFLRA NAGDLKAAED QLSKALTWRK
     ENDPIALADA SKNSYDASKF KGLGYLTTYQ REGKGDLVVT WNIYGAVKKF DETFGDITEF
     IKWRAALMEL AVQELKLDQA TSVIDYDGED PYQMIQVHDY LNVSFLRMNP NVKAATKKTI
     DVFSTAYPEL LREKFFVNVP AIMGWMFAVM KVFVNQNTAR KFHPISNGAN LAKEFPAGVA
     EKFPKAYGGS APDLESSART VALKEVKEEK KEEPKEGSKE EQKGEQKGE
 
 
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