ID A0A091G0Y5_9AVES Unreviewed; 376 AA.
AC A0A091G0Y5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase gamma {ECO:0000313|EMBL:KFO76155.1};
GN ORFNames=N303_14978 {ECO:0000313|EMBL:KFO76155.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO76155.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO76155.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO76155.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; KL447686; KFO76155.1; -; Genomic_DNA.
DR RefSeq; XP_009559189.1; XM_009560894.1.
DR AlphaFoldDB; A0A091G0Y5; -.
DR STRING; 55661.A0A091G0Y5; -.
DR GeneID; 104059247; -.
DR KEGG; cuca:104059247; -.
DR CTD; 56894; -.
DR OrthoDB; 921703at2759; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR10983:SF9; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE GAMMA; 1.
DR PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1.
DR Pfam; PF16076; Acyltransf_C; 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 ECO:0000313|EMBL:KFO76155.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFO76155.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 90..212
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 376 AA; 43603 MW; 85599B38D07EA473 CRC64;
MGFIAFLKTQ FIVHLLIGFV FVVSGLIINF IQLCTLVLWP INKQFYRRVN CRLAYSLWSQ
LVMLLEWWSG TECTLFSDEA TVNTFGKEHV IIILNHNFEI DFLCGWTMTE RFGVLGSSKV
LAKRELLYVP LIGWTWYFLE IVFCKRKWEE DRDTVIEGLK RLADYPEYMW FLLYCEGTRF
TETKHRISME VAESKGLPKL KYHLLPRTKG FTTAVQCLRG TVSAVYDVTL NFRGNKNPSL
LGILYGKKYE ADMCVRRFPL EDIPQDEKEA ANWLHKLYQE KDALQEMYNQ EGIFPGQQFK
PPRRPWTLLN FLFWATVLLS PLFTFGFGVF ASGSPLLILA FLGLVGAASF GVRRLIGVTE
IEKGSSYGNQ EFKKKE
//
