YD018_YEAST
ID YD018_YEAST Reviewed; 396 AA.
AC Q12185; D6VS04;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Uncharacterized acyltransferase YDR018C;
DE EC=2.3.-.-;
GN OrderedLocusNames=YDR018C; ORFNames=PZF396, YD9335.04C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8896275;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1085::aid-yea9>3.3.co;2-s;
RA Eide L.G., Sander C., Prydz H.;
RT "Sequencing and analysis of a 35.4 kb region on the right arm of chromosome
RT IV from Saccharomyces cerevisiae reveal 23 open reading frames.";
RL Yeast 12:1085-1090(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase 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; X95966; CAA65210.1; -; Genomic_DNA.
DR EMBL; Z49770; CAA89843.1; -; Genomic_DNA.
DR EMBL; Z74314; CAA98838.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11864.1; -; Genomic_DNA.
DR PIR; S54641; S54641.
DR RefSeq; NP_010301.1; NM_001180326.1.
DR AlphaFoldDB; Q12185; -.
DR BioGRID; 32068; 39.
DR DIP; DIP-5174N; -.
DR IntAct; Q12185; 1.
DR MINT; Q12185; -.
DR STRING; 4932.YDR018C; -.
DR PaxDb; Q12185; -.
DR PRIDE; Q12185; -.
DR EnsemblFungi; YDR018C_mRNA; YDR018C; YDR018C.
DR GeneID; 851581; -.
DR KEGG; sce:YDR018C; -.
DR SGD; S000002425; YDR018C.
DR VEuPathDB; FungiDB:YDR018C; -.
DR eggNOG; KOG1505; Eukaryota.
DR GeneTree; ENSGT00950000182836; -.
DR HOGENOM; CLU_041844_3_2_1; -.
DR InParanoid; Q12185; -.
DR OMA; KSVNFYW; -.
DR BioCyc; YEAST:G3O-29636-MON; -.
DR Reactome; R-SCE-1482925; Acyl chain remodelling of PG.
DR PRO; PR:Q12185; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12185; protein.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0016746; F:acyltransferase activity; ISS:SGD.
DR GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISS:SGD.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..396
FT /note="Uncharacterized acyltransferase YDR018C"
FT /id="PRO_0000208208"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 117..122
FT /note="HXXXXD motif"
SQ SEQUENCE 396 AA; 45939 MW; 9F55AB56C8FD44DD CRC64;
MKHSQKYRRY GIYEKTGNPF IKGLQRLLIA CLFISGSLSI VVFQICLQVL LPWSKIRFQN
GINQSKKAFI VLLCMILNMV APSSLNVTFE TSRPLKNSSN AKPCFRFKDR AIIIANHQMY
ADWIYLWWLS FVSNLGGNVY IILKKALQYI PLLGFGMRNF KFIFLSRNWQ KDEKALTNSL
VSMDLNARCK GPLTNYKSCY SKTNESIAAY NLIMFPEGTN LSLKTREKSE AFCQRAHLDH
VQLRHLLLPH SKGLKFAVEK LAPSLDAIYD VTIGYSPALR TEYVGTKFTL KKIFLMGVYP
EKVDFYIREF RVNEIPLQDD EVFFNWLLGV WKEKDQLLED YYNTGQFKSN AKNDNQSIVV
TTQTTGFQHE TLTPRILSYY GFFAFLILVF VMKKNH
