ID L5M7Y4_MYODS Unreviewed; 376 AA.
AC L5M7Y4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase gamma {ECO:0000313|EMBL:ELK33833.1};
GN ORFNames=MDA_GLEAN10004965 {ECO:0000313|EMBL:ELK33833.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK33833.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; KB103804; ELK33833.1; -; Genomic_DNA.
DR RefSeq; XP_006759048.1; XM_006758985.2.
DR RefSeq; XP_015416307.1; XM_015560821.1.
DR RefSeq; XP_015416308.1; XM_015560822.1.
DR RefSeq; XP_015416309.1; XM_015560823.1.
DR RefSeq; XP_015416310.1; XM_015560824.1.
DR AlphaFoldDB; L5M7Y4; -.
DR GeneID; 102756653; -.
DR KEGG; myd:102756653; -.
DR CTD; 56894; -.
DR eggNOG; KOG1505; Eukaryota.
DR OrthoDB; 921703at2759; -.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; 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:ELK33833.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023209};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ELK33833.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..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; 43486 MW; AA61098C1FAD51CA CRC64;
MGLLAYLKTQ FELHLLIGFV FVVSGLVINF IQLCTLVLWP LNKQLYRRLN CRLAYSLWSQ
LVMLLEWWSC TQCTLFADQA TMDRLGKEHA IIILNHNFEI DFLCGWTMCE RFGVLGSSKV
LAKRELLCVP LIGWTWYFLE IVFCKRKWEE DRDTVIAGLR CLADYPEYMW FLLYCEGTRF
TEKKHRVSME VAASKGLPPL KHHLLPRTKG FTTAVQCLRG TVAAIYDVTL NFRGNKNPSL
LGILYGKKYE ADMCLRRFPL EEIPQDEKEA AQWLHKLYQE KDALQETYNQ KGVFPGEPFR
PARRPWTLLN FLFWATVLLS PLFRFVLGVF ASGSPLLILT FLGFVGAASF GVRRLIGVTE
IEKGSSYGNQ EFKKKE
//