ID A0A091DC72_FUKDA Unreviewed; 376 AA.
AC A0A091DC72;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase gamma {ECO:0000313|EMBL:KFO28098.1};
GN ORFNames=H920_10472 {ECO:0000313|EMBL:KFO28098.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO28098.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO28098.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO28098.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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; KN122816; KFO28098.1; -; Genomic_DNA.
DR RefSeq; XP_010634747.1; XM_010636445.2.
DR RefSeq; XP_010634748.1; XM_010636446.1.
DR RefSeq; XP_010634749.1; XM_010636447.2.
DR RefSeq; XP_010634750.1; XM_010636448.1.
DR RefSeq; XP_010634751.1; XM_010636449.2.
DR RefSeq; XP_010634752.1; XM_010636450.1.
DR RefSeq; XP_010634753.1; XM_010636451.2.
DR AlphaFoldDB; A0A091DC72; -.
DR STRING; 885580.ENSFDAP00000018801; -.
DR Ensembl; ENSFDAT00000028173; ENSFDAP00000018801; ENSFDAG00000009578.
DR GeneID; 104870717; -.
DR CTD; 56894; -.
DR eggNOG; KOG1505; Eukaryota.
DR OMA; FHVHARR; -.
DR OrthoDB; 921703at2759; -.
DR Proteomes; UP000028990; 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:KFO28098.1};
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:UP000028990};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFO28098.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..39
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; 43682 MW; E951EA387EA08A30 CRC64;
MGLLAYLKTQ FIVHLLIGFV FVVSGLVINF IQLCTLVLWP INKQLYRHVN CRLAYSLWSQ
LVMLLEWWSC TECTIFTDLT TLKYIGKEHV VIILNHNFEI DFLCGWTMSE RFGLLGSSKV
LAKRELLYVP LIGWTWYFLE NVFCKRRWEE DRNTVVRGLK RLVDYPEYMW FLLYCEGTRF
TETKHRVSME VAASKGLPPL KYHLLPRTKG FTTTVQCLQG TVAAVYDVTL NFRKNKIPSL
LGILYGKKYE ADMCVRRFPL EEIPQDEQGA AQWLHKLYQE KDALQEMYNQ KGFFPGEQFK
PARRPWTLLN FLCWATVLLS PLFSFVLGVF SSGSPLLILT FLGFVGAASF GVRRLIGMTE
IEKGSSYGNQ EFKKKE
//
