PLCD_HUMAN
ID PLCD_HUMAN Reviewed; 378 AA.
AC Q9NRZ5; B4DSF9; Q5TEF0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase delta;
DE EC=2.3.1.51 {ECO:0000250|UniProtKB:Q8K4X7};
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 4;
DE Short=1-AGP acyltransferase 4;
DE Short=1-AGPAT 4;
DE AltName: Full=Lysophosphatidic acid acyltransferase delta;
DE Short=LPAAT-delta;
GN Name=AGPAT4; ORFNames=UNQ499/PRO1016;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11487472; DOI=10.2741/leung;
RA Leung D.W.;
RT "The structure and functions of human lysophosphatidic acid
RT acyltransferases.";
RL Front. Biosci. 6:D944-D953(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=21173190; DOI=10.1194/jlr.m007575;
RA Prasad S.S., Garg A., Agarwal A.K.;
RT "Enzymatic activities of the human AGPAT isoform 3 and isoform 5:
RT localization of AGPAT5 to mitochondria.";
RL J. Lipid Res. 52:451-462(2011).
CC -!- FUNCTION: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic
CC acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid
CC or PA) by incorporating an acyl moiety at the sn-2 position of the
CC glycerol backbone (By similarity). Exhibits high acyl-CoA specificity
CC for polyunsaturated fatty acyl-CoA, especially docosahexaenoyl-CoA
CC (22:6-CoA, DHA-CoA) (By similarity). {ECO:0000250|UniProtKB:Q8K4X7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + 1-hexadecanoyl-
CC sn-glycero-3-phosphate = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:55300,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57518, ChEBI:CHEBI:74298,
CC ChEBI:CHEBI:82928; Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55301;
CC Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-octadecanoyl-sn-glycero-3-
CC phosphate = 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:55304, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:74565, ChEBI:CHEBI:77098;
CC Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55305;
CC Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + 1-octadecanoyl-
CC sn-glycero-3-phosphate = 1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:55308,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:74298, ChEBI:CHEBI:74565,
CC ChEBI:CHEBI:77130; Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55309;
CC Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + 1-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z-octadecenoyl)-2-
CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:55312, ChEBI:CHEBI:57287, ChEBI:CHEBI:74298,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:138723;
CC Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55313;
CC Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC -!- INTERACTION:
CC Q9NRZ5; A6NM10-2: AQP12B; NbExp=3; IntAct=EBI-1754287, EBI-17265552;
CC Q9NRZ5; Q13520: AQP6; NbExp=3; IntAct=EBI-1754287, EBI-13059134;
CC Q9NRZ5; P34972: CNR2; NbExp=3; IntAct=EBI-1754287, EBI-2835940;
CC Q9NRZ5; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-1754287, EBI-6942903;
CC Q9NRZ5; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-1754287, EBI-781551;
CC Q9NRZ5; P12318-2: FCGR2A; NbExp=3; IntAct=EBI-1754287, EBI-17187481;
CC Q9NRZ5; Q96P31-6: FCRL3; NbExp=3; IntAct=EBI-1754287, EBI-17443171;
CC Q9NRZ5; O15552: FFAR2; NbExp=3; IntAct=EBI-1754287, EBI-2833872;
CC Q9NRZ5; Q96P66: GPR101; NbExp=3; IntAct=EBI-1754287, EBI-17935713;
CC Q9NRZ5; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-1754287, EBI-1052304;
CC Q9NRZ5; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-1754287, EBI-18053395;
CC Q9NRZ5; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-1754287, EBI-10266796;
CC Q9NRZ5; O95214: LEPROTL1; NbExp=3; IntAct=EBI-1754287, EBI-750776;
CC Q9NRZ5; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-1754287, EBI-17490413;
CC Q9NRZ5; Q8N386: LRRC25; NbExp=3; IntAct=EBI-1754287, EBI-11304917;
CC Q9NRZ5; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-1754287, EBI-11956541;
CC Q9NRZ5; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-1754287, EBI-373355;
CC Q9NRZ5; O14880: MGST3; NbExp=3; IntAct=EBI-1754287, EBI-724754;
CC Q9NRZ5; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-1754287, EBI-7545592;
CC Q9NRZ5; Q04864: REL; NbExp=3; IntAct=EBI-1754287, EBI-307352;
CC Q9NRZ5; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-1754287, EBI-10192441;
CC Q9NRZ5; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-1754287, EBI-17247926;
CC Q9NRZ5; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-1754287, EBI-17295964;
CC Q9NRZ5; Q9UHI5: SLC7A8; NbExp=3; IntAct=EBI-1754287, EBI-13292283;
CC Q9NRZ5; Q9HBV2: SPACA1; NbExp=3; IntAct=EBI-1754287, EBI-17498703;
CC Q9NRZ5; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-1754287, EBI-8638294;
CC Q9NRZ5; Q9Y320: TMX2; NbExp=3; IntAct=EBI-1754287, EBI-6447886;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8K4X7}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRZ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRZ5-2; Sequence=VSP_056928, VSP_056929;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in skeletal
CC muscle, followed by heart, liver, prostate and thymus.
CC {ECO:0000269|PubMed:21173190}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250|UniProtKB:Q9D517}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; AF156776; AAF80338.1; -; mRNA.
DR EMBL; AY358506; AAQ88870.1; -; mRNA.
DR EMBL; AK299721; BAG61621.1; -; mRNA.
DR EMBL; AL109942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020209; AAH20209.1; -; mRNA.
DR CCDS; CCDS5280.1; -. [Q9NRZ5-1]
DR RefSeq; NP_064518.1; NM_020133.2. [Q9NRZ5-1]
DR AlphaFoldDB; Q9NRZ5; -.
DR BioGRID; 121225; 82.
DR IntAct; Q9NRZ5; 36.
DR STRING; 9606.ENSP00000314036; -.
DR iPTMnet; Q9NRZ5; -.
DR PhosphoSitePlus; Q9NRZ5; -.
DR BioMuta; AGPAT4; -.
DR DMDM; 12230468; -.
DR EPD; Q9NRZ5; -.
DR jPOST; Q9NRZ5; -.
DR MassIVE; Q9NRZ5; -.
DR MaxQB; Q9NRZ5; -.
DR PaxDb; Q9NRZ5; -.
DR PeptideAtlas; Q9NRZ5; -.
DR PRIDE; Q9NRZ5; -.
DR ProteomicsDB; 5022; -.
DR ProteomicsDB; 82446; -. [Q9NRZ5-1]
DR Antibodypedia; 33497; 209 antibodies from 28 providers.
DR DNASU; 56895; -.
DR Ensembl; ENST00000320285.9; ENSP00000314036.4; ENSG00000026652.15. [Q9NRZ5-1]
DR GeneID; 56895; -.
DR KEGG; hsa:56895; -.
DR MANE-Select; ENST00000320285.9; ENSP00000314036.4; NM_020133.3; NP_064518.1.
DR UCSC; uc003qtr.2; human. [Q9NRZ5-1]
DR CTD; 56895; -.
DR DisGeNET; 56895; -.
DR GeneCards; AGPAT4; -.
DR HGNC; HGNC:20885; AGPAT4.
DR HPA; ENSG00000026652; Tissue enriched (brain).
DR MIM; 614795; gene.
DR neXtProt; NX_Q9NRZ5; -.
DR OpenTargets; ENSG00000026652; -.
DR PharmGKB; PA134961047; -.
DR VEuPathDB; HostDB:ENSG00000026652; -.
DR eggNOG; KOG1505; Eukaryota.
DR GeneTree; ENSGT00950000182836; -.
DR HOGENOM; CLU_041844_5_2_1; -.
DR InParanoid; Q9NRZ5; -.
DR OMA; KSVNFYW; -.
DR OrthoDB; 959325at2759; -.
DR PhylomeDB; Q9NRZ5; -.
DR TreeFam; TF314065; -.
DR BioCyc; MetaCyc:HS00452-MON; -.
DR BRENDA; 2.3.1.51; 2681.
DR PathwayCommons; Q9NRZ5; -.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR SignaLink; Q9NRZ5; -.
DR SIGNOR; Q9NRZ5; -.
DR UniPathway; UPA00557; UER00613.
DR BioGRID-ORCS; 56895; 6 hits in 1072 CRISPR screens.
DR ChiTaRS; AGPAT4; human.
DR GenomeRNAi; 56895; -.
DR Pharos; Q9NRZ5; Tbio.
DR PRO; PR:Q9NRZ5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NRZ5; protein.
DR Bgee; ENSG00000026652; Expressed in tendon of biceps brachii and 150 other tissues.
DR ExpressionAtlas; Q9NRZ5; baseline and differential.
DR Genevisible; Q9NRZ5; HS.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR GO; GO:0008654; P:phospholipid biosynthetic process; NAS:UniProtKB.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Endoplasmic reticulum;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..378
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
FT delta"
FT /id="PRO_0000208197"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 96..101
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9D517"
FT VAR_SEQ 60
FT /note="Q -> L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056928"
FT VAR_SEQ 61..222
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056929"
SQ SEQUENCE 378 AA; 44021 MW; 3EFC13D196F8CDC5 CRC64;
MDLAGLLKSQ FLCHLVFCYV FIASGLIINT IQLFTLLLWP INKQLFRKIN CRLSYCISSQ
LVMLLEWWSG TECTIFTDPR AYLKYGKENA IVVLNHKFEI DFLCGWSLSE RFGLLGGSKV
LAKKELAYVP IIGWMWYFTE MVFCSRKWEQ DRKTVATSLQ HLRDYPEKYF FLIHCEGTRF
TEKKHEISMQ VARAKGLPRL KHHLLPRTKG FAITVRSLRN VVSAVYDCTL NFRNNENPTL
LGVLNGKKYH ADLYVRRIPL EDIPEDDDEC SAWLHKLYQE KDAFQEEYYR TGTFPETPMV
PPRRPWTLVN WLFWASLVLY PFFQFLVSMI RSGSSLTLAS FILVFFVASV GVRWMIGVTE
IDKGSAYGNS DSKQKLND
