ID H0VIS9_CAVPO Unreviewed; 370 AA.
AC H0VIS9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Lysophosphatidylglycerol acyltransferase 1 {ECO:0000313|Ensembl:ENSCPOP00000010132.3};
GN Name=LPGAT1 {ECO:0000313|Ensembl:ENSCPOP00000010132.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000010132.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000010132.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000010132.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; AAKN02019002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003474270.1; XM_003474222.3.
DR AlphaFoldDB; H0VIS9; -.
DR STRING; 10141.ENSCPOP00000010132; -.
DR Ensembl; ENSCPOT00000011375.3; ENSCPOP00000010132.3; ENSCPOG00000011269.4.
DR GeneID; 100714870; -.
DR KEGG; cpoc:100714870; -.
DR CTD; 9926; -.
DR VEuPathDB; HostDB:ENSCPOG00000011269; -.
DR eggNOG; KOG1505; Eukaryota.
DR GeneTree; ENSGT00950000182836; -.
DR HOGENOM; CLU_046804_2_0_1; -.
DR InParanoid; H0VIS9; -.
DR OMA; PLDIQTW; -.
DR OrthoDB; 3012482at2759; -.
DR TreeFam; TF314346; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000011269; Expressed in frontal cortex and 12 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0047190; F:2-acylglycerophosphocholine O-acyltransferase activity; IEA:Ensembl.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IEA:Ensembl.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR10983:SF2; ACYL-COA:LYSOPHOSPHATIDYLGLYCEROL ACYLTRANSFERASE 1; 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 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:UP000005447};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 342..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 95..219
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 370 AA; 43051 MW; 44441ECF43CB89D9 CRC64;
MAVTWEEVPR LGWILVKALL RFAFMVANNL VAIPSYVCYV ILLQPLRLLD SKRFWCIEGI
MYKWLLGMVA SWGWHAGYTV VEWGEDVKAI SKDEAVMLVN HQSTGDVCTL MMCLQDKGMV
VAQMMWLMDH IFKYTNFGIV SLIHGDFFIR QGKSHRDQQL VLLKKHLENN YRSRDRKWIV
LFPEGGFLRK RRETSQAFAK KNNLPFLTHV TLPRVGATQI ILSALVARQE NGSPAGGDAK
ELENKSQGLQ WIIDTTIAYP KGELLDIQTW ILGYRKPTVT HVHYRIFPVK DVPLETEDLT
NWLYQRFIEK EHLLAHFYET GAFPPPEGHK EAISREMTLS NVWIFFIQSF AFLSGYMWYS
AIQYFYHCLF
//
