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SFH5_COCIM
ID   SFH5_COCIM              Reviewed;         457 AA.
AC   Q1DSY1; A0A0D6K9N9; J3K945;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Phosphatidylinositol transfer protein SFH5;
DE            Short=PITP SFH5;
GN   Name=SFH5; ORFNames=CIMG_06582;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; GG704912; EAS31103.1; -; Genomic_DNA.
DR   RefSeq; XP_001242686.1; XM_001242685.2.
DR   AlphaFoldDB; Q1DSY1; -.
DR   SMR; Q1DSY1; -.
DR   STRING; 246410.Q1DSY1; -.
DR   EnsemblFungi; EAS31103; EAS31103; CIMG_06582.
DR   GeneID; 4560896; -.
DR   KEGG; cim:CIMG_06582; -.
DR   VEuPathDB; FungiDB:CIMG_06582; -.
DR   InParanoid; Q1DSY1; -.
DR   OMA; MLQVHDY; -.
DR   OrthoDB; 1182715at2759; -.
DR   Proteomes; UP000001261; 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; 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..457
FT                   /note="Phosphatidylinositol transfer protein SFH5"
FT                   /id="PRO_0000324976"
FT   DOMAIN          196..371
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          378..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..414
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         221
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         241
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         275
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
FT   BINDING         277
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         311
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250|UniProtKB:A6ZQI5"
SQ   SEQUENCE   457 AA;  49844 MW;  EDFB97FBABFA9CF4 CRC64;
     MEKVQEQPAQ TLSETAEQPA ERVVEQPQDS AATAAPPGDS KEAETEKPAE VAPKEDSKEA
     PAPPPAATTA ATADDANSDI IEEVKDKAGA NTQVADPKPQ EPADTRPSYL VNNAALSQFF
     DRLAPIVEKA GHNEMWGVPL KDAQDAPTVN IMIKFLRANE GNVKLAEEQL VKALEWRKKM
     NPLALAESAA FPSSKFKGLG YITTYRDPTT EKNVVFTWNI YGSVKNVDLT FGNLEEFIKW
     RVALMELAIR ELRLESATSV MDYNGEDPYQ MIQVHDYQNV SFIRMNPNIR AASRETIEVF
     STAYPELLKE KYFVNLPVVM GWVFTALKVF LSKNTIRKFH PITNGVNLAR EFTTFGEEIP
     KTYGGKGDVL ADSGRTVTLQ DDKAPETKPE ENGNASQAPE AEPASGNPAQ TDATNGPAKD
     DAPKNDKPAV PTDTKTDAPA DAPANTLADA PADSRPN
 
 
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