ID A7T2H2_NEMVE Unreviewed; 385 AA.
AC A7T2H2;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=NEMVEDRAFT_v1g195603 {ECO:0000313|EMBL:EDO29842.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO29842.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO29842.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS470252; EDO29842.1; -; Genomic_DNA.
DR RefSeq; XP_001621942.1; XM_001621892.1.
DR AlphaFoldDB; A7T2H2; -.
DR STRING; 45351.A7T2H2; -.
DR EnsemblMetazoa; EDO29842; EDO29842; NEMVEDRAFT_v1g195603.
DR GeneID; 5500507; -.
DR KEGG; nve:5500507; -.
DR eggNOG; KOG1505; Eukaryota.
DR HOGENOM; CLU_041844_5_2_1; -.
DR InParanoid; A7T2H2; -.
DR OMA; FHVHARR; -.
DR OrthoDB; 921703at2759; -.
DR PhylomeDB; A7T2H2; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
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:SF24; 1-ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 3, ISOFORM E-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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001593};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 91..213
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 385 AA; 44814 MW; 01F0C67E11312B75 CRC64;
MAGLLSALKK LPFIPLWFVM VFLITGMIIN IIQVAILPLW TFNKTLYRWI NMHVVYLHWS
QLTFLVDWWS ETDLRLYGNE EDFRYFGKES AICVANHRSD VDWLIGWVMA DRVDTLGTTK
CYMKGYLKYL PIMGFSWLSS EYAFVSRNWQ KDQRVLQNSL DTLQDFPYPF WIAIFAEGTR
LTQEKLQASI EYARSKNIPE LQHHLLPRPR GFSITVQHLK DKVSAVYDME VAFVEGKYPT
MKGLLLGVKY EIHLLIRRIP VKDIPMETIE VTSKWCQKLF QEKDKAMSYY LANGRYEEPL
VFHPRQYSNL VPLLVWHTLL SVPLLSYICY VLLSGDVFIL SVAAVVVSIC FVVFKILLHF
SDSQKGSSFG LKTTGSSLHA YKKEQ
//