位置:首页 > 蛋白库 > SFH5_ASHGO
SFH5_ASHGO
ID   SFH5_ASHGO              Reviewed;         295 AA.
AC   Q75BM4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Phosphatidylinositol transfer protein SFH5;
DE            Short=PITP SFH5;
GN   Name=SFH5; OrderedLocusNames=ACR247W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(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}.
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; AE016816; AAS51473.1; -; Genomic_DNA.
DR   RefSeq; NP_983649.1; NM_209002.1.
DR   AlphaFoldDB; Q75BM4; -.
DR   SMR; Q75BM4; -.
DR   STRING; 33169.AAS51473; -.
DR   EnsemblFungi; AAS51473; AAS51473; AGOS_ACR247W.
DR   GeneID; 4619784; -.
DR   KEGG; ago:AGOS_ACR247W; -.
DR   eggNOG; KOG1471; Eukaryota.
DR   HOGENOM; CLU_045138_0_1_1; -.
DR   InParanoid; Q75BM4; -.
DR   OMA; RKEFNPL; -.
DR   Proteomes; UP000000591; Chromosome III.
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; 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..295
FT                   /note="Phosphatidylinositol transfer protein SFH5"
FT                   /id="PRO_0000324966"
FT   DOMAIN          100..268
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   BINDING         131
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         151
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         176
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         178
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         212
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
SQ   SEQUENCE   295 AA;  33663 MW;  4384247BEBA54FB2 CRC64;
     MPSDMLQFPS ENDRQTFERL VSELPDLIHK RCHDYDELYG HKLLEEGPAE VAKFYSKDHA
     HALLFKFLKA NAFSYEGAVK QLVSTLNWRR EFQPLKAAFA EEHDERLMAA GYISYDASAA
     PNTRTVTWNL YGKLGACKDL FADQDTFIRY RVGLMERGLQ ALNLLDPDNC SMTQVHDYKD
     VSVWNMNADV KKCSRRVIAI FQDHYPELLY AKYFVNVPTI LRWVYDVVRA FVSEETSRKF
     VVLNDGTKLA AYFAGVPAAY GGTAPATLAE LPKPASRPSP YALFLLQKHI SEELD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024