ID   SEC14_CANGA             Reviewed;         302 AA.
AC   P53989; Q6FVZ2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=SEC14 cytosolic factor;
DE   AltName: Full=Phosphatidylinositol/phosphatidylcholine transfer protein;
DE            Short=PI/PC TP;
GN   Name=SEC14; OrderedLocusNames=CAGL0D04290g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 6425 / NCYC 350;
RX   PubMed=9249074; DOI=10.1016/s0378-1119(97)00103-0;
RA   Dundon W., Islam K.;
RT   "Nucleotide sequence of the gene coding for SEC14p in Candida (torulopsis)
RT   glabrata.";
RL   Gene 193:115-118(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Required for transport of secretory proteins from the Golgi
CC       complex. Catalyzes the transfer of phosphatidylinositol and
CC       phosphatidylcholine between membranes in vitro (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
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DR   EMBL; X97320; CAA65985.1; -; Genomic_DNA.
DR   EMBL; CR380950; CAG58513.2; -; Genomic_DNA.
DR   RefSeq; XP_445602.2; XM_445602.2.
DR   AlphaFoldDB; P53989; -.
DR   SMR; P53989; -.
DR   STRING; 5478.XP_445602.2; -.
DR   EnsemblFungi; CAG58513; CAG58513; CAGL0D04290g.
DR   GeneID; 2887243; -.
DR   KEGG; cgr:CAGL0D04290g; -.
DR   CGD; CAL0128111; SEC14.
DR   VEuPathDB; FungiDB:CAGL0D04290g; -.
DR   eggNOG; KOG1471; Eukaryota.
DR   HOGENOM; CLU_014001_0_1_1; -.
DR   InParanoid; P53989; -.
DR   OMA; CECAGGC; -.
DR   Proteomes; UP000002428; Chromosome D.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008525; F:phosphatidylcholine transporter activity; IEA:EnsemblFungi.
DR   GO; GO:0008526; F:phosphatidylinositol transfer activity; IEA:EnsemblFungi.
DR   GO; GO:0030437; P:ascospore formation; IEA:EnsemblFungi.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IEA:EnsemblFungi.
DR   GO; GO:0006896; P:Golgi to vacuole transport; IEA:EnsemblFungi.
DR   GO; GO:0048194; P:Golgi vesicle budding; IEA:EnsemblFungi.
DR   GO; GO:2001246; P:negative regulation of phosphatidylcholine 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   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   Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..302
FT                   /note="SEC14 cytosolic factor"
FT                   /id="PRO_0000210740"
FT   DOMAIN          97..270
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
SQ   SEQUENCE   302 AA;  34292 MW;  A857E3C70DBA2DDF CRC64;
     MVSEAEFLAS YPQKCPAGSL PGTPGNTDEA QEGALKQLRS ELEAAGFKER LDDSTLLRFL
     RARKFDVALA KEMFENCEKW RKEYGTNTIM QDFHYDEKPL VAKYYPQYYH KTDKDGRPVY
     FEELGAVNLT EMEKITTQER MLKNLVWEYE SVVNYRLPAC SRAAGYLVET SCTVMDLKGI
     SISSAYSVLS YVREASYISQ NYYPERMGKF YLINAPFGFS TAFRLFKPFL DPVTVSKIFI
     LGSSYQSELL KQIPAENLPS KFGGKSEVDE AAGGLYLSDI GPWRDAKYIG PEGEAPEMFS
     MK