ID   CSR1_ASHGO              Reviewed;         436 AA.
AC   Q757H2;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Phosphatidylinositol transfer protein CSR1;
GN   Name=CSR1; OrderedLocusNames=AER041W;
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, AND SEQUENCE REVISION TO 236.
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. May also regulate post-
CC       Golgi membrane-trafficking events and have a role resistance to
CC       oxidative stress (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds phosphatidylinositol (PtdIns). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PITP family. {ECO:0000305}.
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DR   EMBL; AE016818; AAS52725.2; -; Genomic_DNA.
DR   RefSeq; NP_984901.2; NM_210255.2.
DR   AlphaFoldDB; Q757H2; -.
DR   SMR; Q757H2; -.
DR   STRING; 33169.AAS52725; -.
DR   EnsemblFungi; AAS52725; AAS52725; AGOS_AER041W.
DR   GeneID; 4621103; -.
DR   KEGG; ago:AGOS_AER041W; -.
DR   eggNOG; KOG1470; Eukaryota.
DR   HOGENOM; CLU_016665_3_0_1; -.
DR   InParanoid; Q757H2; -.
DR   OMA; QKAVICG; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid droplet; IEA:EnsemblFungi.
DR   GO; GO:0008526; F:phosphatidylinositol transfer activity; IEA:EnsemblFungi.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IEA:EnsemblFungi.
DR   GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:1901352; P:negative regulation of phosphatidylglycerol biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:2001247; P:positive regulation of phosphatidylcholine biosynthetic process; IEA:EnsemblFungi.
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   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF03765; CRAL_TRIO_N; 1.
DR   SMART; SM01100; 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; Endosome; Lipid degradation; Lipid metabolism; Lipid transport;
KW   Phospholipid degradation; Phospholipid metabolism; Reference proteome;
KW   Transport.
FT   CHAIN           1..436
FT                   /note="Phosphatidylinositol transfer protein CSR1"
FT                   /id="PRO_0000228154"
FT   DOMAIN          188..347
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   REGION          85..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   436 AA;  49149 MW;  BA3871B42BE216BB CRC64;
     MTQTAAPGRV QTLTKEQEKV LKQVWVHLFQ FWGIDVDGSA VLTAKEPEPA APSGKGRKLL
     GLFGKRKDAT GAARKESNGK AAAKVYDAEK VEDSDAEKEK PTPQKVEGLE EMYELLKELD
     GAAVSKEFWS MLRCDYPDNL LLRFVRARKW DINKAMIMMA HSLRWRLNEG KPEDIVFGGE
     RGAQKADKKG IVKQLELGKA TVRGFDKNGC PIVYVRPRLH HAADQTEAET SEYSLLIIEQ
     ARLFLKEPCD TATILFDLSG FSMANMDYAP VKFLITCFEA HYPECLGKLF IHKAPWIFPP
     IWNIIKNWLD PVVAAKIAFT KTAADLEEFI PAEQIPLELG GKDEYNFDGF VMPDGSADTK
     LSDEKGKAAV LEEREAIIKR FIDATISWIE STSDEESAKW LEKKIDLSKE LSENYSKLDP
     YIRSRSFYDV NGTLKV