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Database: UniProt
Entry: A7T2H2_NEMVE
LinkDB: A7T2H2_NEMVE
Original site: A7T2H2_NEMVE 
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}.
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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
//
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