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Database: UniProt
Entry: F1L665_ASCSU
LinkDB: F1L665_ASCSU
Original site: F1L665_ASCSU 
ID   F1L665_ASCSU            Unreviewed;       398 AA.
AC   F1L665;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   22-FEB-2023, entry version 19.
DE   SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase acl-12 {ECO:0000313|EMBL:ADY45619.1};
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY45619.1};
RN   [1] {ECO:0000313|EMBL:ADY45619.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21685128; DOI=10.1101/gr.121426.111;
RA   Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA   Davis R.E.;
RT   "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT   functional diversification, and novel developmental profiles.";
RL   Genome Res. 21:1462-1477(2011).
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR   EMBL; JI172164; ADY45619.1; -; mRNA.
DR   AlphaFoldDB; F1L665; -.
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:SF14; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE ACL-12-RELATED; 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   2: Evidence at transcript level;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000313|EMBL:ADY45619.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADY45619.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        36..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          117..241
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   398 AA;  45979 MW;  BB3B6FDC756B44D4 CRC64;
     MLEGSANDTA IDGRTMSVED THCGSSLGGS MDVRKIIAFI GAFYWIVMTV LIVPGAVVAS
     FFTIMLPAML IWIPLHNWID HKLCRMVNDH WVSASQSAGL NVIEYGDDIS EIAEKRVLFL
     SNHLGLVDHF VLMCAMYNKG TIAEKYLWVI FNIWKMTPLG AMWLTHGNYF INGGASKRER
     LLKQFREHLK DNYWKFDHRW IVMYPEGSRL YLIRESNARY AKKIGQKIFK NCALPRSSGA
     HAVFEVAGKS YDSTDKELGL ARCGLGGPIE YVVDCTLGYY KGDVPELGRY MTGEFPHKHS
     AVGVHYKIYP TKAEWLDEEK LRQWLYARYE EKDELLEYYY TKGTFPVNAK SRPRPLHFPF
     SRCVVVETFW ILLFYAHYYI WVKPLCIFLM NIVLSMFV
//
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