SEC14_KLULA
ID SEC14_KLULA Reviewed; 301 AA.
AC P24859; Q6CW66;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=SEC14 cytosolic factor;
DE AltName: Full=Phosphatidylinositol/phosphatidylcholine transfer protein;
DE Short=PI/PC TP;
GN Name=SEC14; OrderedLocusNames=KLLA0B06479g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2198263; DOI=10.1128/jb.172.8.4510-4521.1990;
RA Salama S.R., Cleves A.E., Malehorn D.E., Whitters E.A., Bankaitis V.A.;
RT "Cloning and characterization of Kluyveromyces lactis SEC14, a gene whose
RT product stimulates Golgi secretory function in Saccharomyces cerevisiae.";
RL J. Bacteriol. 172:4510-4521(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382122; CAH02216.1; -; Genomic_DNA.
DR PIR; A37766; A37766.
DR RefSeq; XP_451823.1; XM_451823.1.
DR AlphaFoldDB; P24859; -.
DR SMR; P24859; -.
DR STRING; 28985.XP_451823.1; -.
DR EnsemblFungi; CAH02216; CAH02216; KLLA0_B06479g.
DR GeneID; 2896969; -.
DR KEGG; kla:KLLA0_B06479g; -.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_014001_0_1_1; -.
DR InParanoid; P24859; -.
DR OMA; CECAGGC; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
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..301
FT /note="SEC14 cytosolic factor"
FT /id="PRO_0000210741"
FT DOMAIN 97..270
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 9..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 47
FT /note="Y -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 98..99
FT /note="KP -> NT (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="F -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 301 AA; 34647 MW; F6F78EE266B2A7E9 CRC64;
MVSEQEILES YPQVCPSGSL SGTPGNLDSE QEAKLKEFRE LLESLGYKER LDDSTLLRFL
RARKFDLEAS KIMYENCEKW RKEFGVDTIF EDFHYEEKPL VAKYYPQYYH KTDNDGRPVY
IEELGSVNLT QMYKITTQER MLKNLVWEYE AFVRYRLPAC SRKAGYLVET SCTILDLKGI
SISSAAQVLS YVREASNIGQ NYYPERMGKF YLINAPFGFS TAFRLFKPFL DPVTVSKIFI
LGSSYQKDLL KQIPAENLPK KFGGQSEVSE AEGGLYLSDI GPWREEEYIG PEGEAPKAFQ
L
