ID A8WXQ0_CAEBR Unreviewed; 440 AA.
AC A8WXQ0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Protein CBG04511 {ECO:0000313|EMBL:CAP25180.2};
GN ORFNames=CBG04511 {ECO:0000313|EMBL:CAP25180.2,
GN ECO:0000313|WormBase:CBG04511}, CBG_04511
GN {ECO:0000313|EMBL:CAP25180.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP25180.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP25180.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP25180.2,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; HE601277; CAP25180.2; -; Genomic_DNA.
DR RefSeq; XP_002644144.1; XM_002644098.1.
DR AlphaFoldDB; A8WXQ0; -.
DR STRING; 6238.A8WXQ0; -.
DR EnsemblMetazoa; CBG04511.1; CBG04511.1; WBGene00027165.
DR GeneID; 8586139; -.
DR WormBase; CBG04511; CBP27016; WBGene00027165; -.
DR eggNOG; KOG2898; Eukaryota.
DR HOGENOM; CLU_042575_0_0_1; -.
DR InParanoid; A8WXQ0; -.
DR OMA; GYCTNNT; -.
DR OrthoDB; 5471865at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR23063; PHOSPHOLIPID ACYLTRANSFERASE; 1.
DR PANTHER; PTHR23063:SF6; PLSC DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 194..309
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 440 AA; 50247 MW; 413810FC4DAE0E59 CRC64;
MLSTIFYLYG SVITLAYFST VFLIFFGLSW GILPHWYLHV VSLIQGHFPS ERHKIKVKRD
ENSNEQKEDK SADEIAEEQV KKLIESDLAP CFNTAHTIRP TLLGMMPEKN WTGAQKSIFF
VGLFFRAFFL MPVRIGLLLT SFIFVALAGL QTAFRTLSDH EKTWVAIVYC RLFSSSMGLV
ANYRYPQFRP KKPGVAVSNH LTPNDIQILF AGTPHGSSYG YVVTGQKHKG IIGVIEHLVE
KLCPSLWLER KCSNDRQGFL AEVLKTAKRE GPVLLFPEGY CSNNSKVLQF RKAIFEENVN
IYPVAIKQSP EFGDGFWYED EFFQYLVRTM LNWAVVYDIQ YLPMETRKES ENNSMFAARI
QHAIARAAGI SPCEHGGNLW YKQEERNKMK EVFKAQNEAA SLRRNDSSVS ETSSGISSGD
DFEKVEKVQE QFQKLITVMS
//