ID Q66J57_XENLA Unreviewed; 376 AA.
AC Q66J57;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=1-acylglycerol-3-phosphate O-acyltransferase 3 S homeolog {ECO:0000313|RefSeq:NP_001087659.1, ECO:0000313|RefSeq:XP_018103851.1, ECO:0000313|RefSeq:XP_041439122.1};
DE EC=2.3.1.51 {ECO:0000313|RefSeq:NP_001087659.1};
DE SubName: Full=MGC81841 protein {ECO:0000313|EMBL:AAH81052.1};
GN Name=agpat3.S {ECO:0000313|RefSeq:NP_001087659.1,
GN ECO:0000313|RefSeq:XP_018103851.1, ECO:0000313|RefSeq:XP_041439122.1,
GN ECO:0000313|Xenbase:XB-GENE-969512};
GN Synonyms=agpat3 {ECO:0000313|RefSeq:NP_001087659.1,
GN ECO:0000313|RefSeq:XP_018103851.1, ECO:0000313|RefSeq:XP_041439122.1,
GN ECO:0000313|Xenbase:XB-GENE-969512}, MGC81841
GN {ECO:0000313|EMBL:AAH81052.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH81052.1};
RN [1] {ECO:0000313|RefSeq:NP_001087659.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH81052.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000313|EMBL:AAH81052.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001087659.1, ECO:0000313|RefSeq:XP_018103851.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018103851.1,
RC ECO:0000313|RefSeq:XP_041439122.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018103851.1,
RC ECO:0000313|RefSeq:XP_041439122.1};
RG RefSeq;
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; BC081052; AAH81052.1; -; mRNA.
DR RefSeq; NP_001087659.1; NM_001094190.1.
DR RefSeq; XP_018103849.1; XM_018248360.1.
DR RefSeq; XP_018103851.1; XM_018248362.1.
DR RefSeq; XP_041439122.1; XM_041583188.1.
DR STRING; 8355.Q66J57; -.
DR PaxDb; 8355-Q66J57; -.
DR GeneID; 447483; -.
DR KEGG; xla:447483; -.
DR AGR; Xenbase:XB-GENE-969512; -.
DR CTD; 447483; -.
DR Xenbase; XB-GENE-969512; agpat3.S.
DR OMA; FHVHARR; -.
DR OrthoDB; 921703at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 447483; Expressed in camera-type eye and 19 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008654; P:phospholipid biosynthetic process; 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 2: Evidence at transcript level;
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:UP000186698};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..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; 43780 MW; 05003C13A5B442EB CRC64;
MGLWGFLKTQ FVVHLLIGFV FVMSGLIINF LQLCTLPLWG INKPLYRRIN CRMAYLLWSQ
LVMLLEWWSG TQCTLFTDQQ TIDHFGKEHV IVILNHNYEI DFLCGWTMCE RYGVLGSSKV
LAKNELLMVP LIGWTWYFLE IVFCKRKWEE DRDTVIQGLR DLRDYPEYMW FLLYCEGTRF
TETKHKISME VADKKGLARL KHHLLPRTKG FTTAVQCLRG TVSAVYDVTL NFRGNKNPSL
LGILYGKKYE ADMCVRRFPI EEIPEDEQEA AGWLHKLYQE KDALQEQYIQ EGTFPGTQFV
PPRRPWTLLN FLFWATLLLS PLFSFAIGIF ASGSPLLILS FMGFMWTASF AVRRLIGVTE
IDRGSSYGNH EVKKSI
//
