Q99943 (PLCA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
EC=2.3.1.51

Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 1
Short name=1-AGP acyltransferase 1
Short name=1-AGPAT 1
Lysophosphatidic acid acyltransferase alpha
Short name=LPAAT-alpha
Protein G15

Gene names

Name:	AGPAT1
Synonyms:	G15

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	283 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.
Catalytic activity	Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
Pathway	Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Domain	The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate By similarity.
Sequence similarities	Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
Sequence caution	The sequence AAB47493.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	CDP-diacylglycerol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway energy reserve metabolic process Traceable author statement. Source: Reactome phosphatidic acid biosynthetic process Inferred from genetic interaction Ref.1. Source: BHF-UCL positive regulation of cellular metabolic process Traceable author statement. Source: Reactome positive regulation of cytokine production Inferred from mutant phenotype Ref.1. Source: BHF-UCL positive regulation of cytokine-mediated signaling pathway Inferred by curator Ref.1. Source: BHF-UCL small molecule metabolic process Traceable author statement. Source: Reactome triglyceride biosynthetic process Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	1-acylglycerol-3-phosphate O-acyltransferase activity Inferred from genetic interaction Ref.1. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 283	283	1-acyl-sn-glycerol-3-phosphate acyltransferase alpha		PRO_0000208190
Regions
	Transmembrane	7 – 27	21	Helical; Potential
	Transmembrane	38 – 58	21	Helical; Potential
	Transmembrane	128 – 148	21	Helical; Potential
	Motif	104 – 109	6	HXXXXD motif
Natural variations
	Natural variant	30	1	P → S. Corresponds to variant rs11964847 [ dbSNP | Ensembl ].		VAR_050593

Sequences

	Sequence		Length	Mass (Da)
	Q99943 [UniParc]. Last modified January 1, 1998. Version 2. Checksum: 71F3207259747C68	FASTA	283	31,717
	10 20 30 40 50 60 MDLWPGAWML LLLLFLLLLF LLPTLWFCSP SAKYFFKMAF YNGWILFLAV LAIPVCAVRG 70 80 90 100 110 120 RNVENMKILR LMLLHIKYLY GIRVEVRGAH HFPPSQPYVV VSNHQSSLDL LGMMEVLPGR 130 140 150 160 170 180 CVPIAKRELL WAGSAGLACW LAGVIFIDRK RTGDAISVMS EVAQTLLTQD VRVWVFPEGT 190 200 210 220 230 240 RNHNGSMLPF KRGAFHLAVQ AQVPIVPIVM SSYQDFYCKK ERRFTSGQCQ VRVLPPVPTE 250 260 270 280 GLTPDDVPAL ADRVRHSMLT VFREISTDGR GGGDYLKKPG GGG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells." West J., Tompkins C.K., Balantac N., Nudelman E., Meengs B., White T., Bursten S., Coleman J., Kumar A., Singer J.W., Leung D.W. DNA Cell Biol. 16:691-701(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases." Stamps A.C., Elmore M.A., Hill M.E., Kelly K., Makda A.A., Finnen M.J. Biochem. J. 326:455-461(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Characterization of a human lysophosphatidic acid acyltransferase that is encoded by a gene located in the class III region of the human major histocompatibility complex." Aguado B., Campbell R.D. J. Biol. Chem. 273:4096-4105(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse." Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L. Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Lung and Skin.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U56417 mRNA. Translation: AAB58775.1. U75971 mRNA. Translation: AAB96378.1. Y09565 mRNA. Translation: CAA70758.1. U89336 Genomic DNA. Translation: AAB47493.1. Different initiation. AL662884 Genomic DNA. Translation: CAI18347.1. AL662828 Genomic DNA. Translation: CAI17430.1. AL845464 Genomic DNA. Translation: CAI41807.1. BX284686 Genomic DNA. Translation: CAM26221.1. BX927239 Genomic DNA. Translation: CAQ06593.1. CR933878 Genomic DNA. Translation: CAQ09622.1. CR812478 Genomic DNA. Translation: CAQ10697.1. CH471081 Genomic DNA. Translation: EAX03600.1. BC002402 mRNA. Translation: AAH02402.1. BC003007 mRNA. Translation: AAH03007.1. BC004310 mRNA. Translation: AAH04310.1. BC090849 mRNA. Translation: AAH90849.1.
IPI	IPI00019141.
RefSeq	NP_006402.1. NM_006411.3. NP_116130.2. NM_032741.4.
UniGene	Hs.409230.
3D structure databases
ProteinModelPortal	Q99943.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99943. 2 interactions.
STRING	9606.ENSP00000337463.
PTM databases
PhosphoSite	Q99943.
Polymorphism databases
DMDM	3914372.
Proteomic databases
PaxDb	Q99943.
PRIDE	Q99943.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000336984; ENSP00000337463; ENSG00000204310. ENST00000375104; ENSP00000364245; ENSG00000204310. ENST00000375107; ENSP00000364248; ENSG00000204310. ENST00000383294; ENSP00000372782; ENSG00000206324. ENST00000395496; ENSP00000378874; ENSG00000204310. ENST00000395497; ENSP00000378875; ENSG00000204310. ENST00000395499; ENSP00000378877; ENSG00000204310. ENST00000399825; ENSP00000382721; ENSG00000206324. ENST00000399827; ENSP00000382723; ENSG00000206324. ENST00000399829; ENSP00000382725; ENSG00000206324. ENST00000399830; ENSP00000382726; ENSG00000206324. ENST00000399833; ENSP00000382728; ENSG00000206324. ENST00000414520; ENSP00000406615; ENSG00000227642. ENST00000414933; ENSP00000388870; ENSG00000227642. ENST00000415173; ENSP00000412805; ENSG00000228892. ENST00000416363; ENSP00000407189; ENSG00000236873. ENST00000417388; ENSP00000415015; ENSG00000228892. ENST00000424030; ENSP00000397765; ENSG00000236873. ENST00000425204; ENSP00000388253; ENSG00000226467. ENST00000425572; ENSP00000394919; ENSG00000235758. ENST00000427763; ENSP00000401410; ENSG00000226467. ENST00000430226; ENSP00000412304; ENSG00000235758. ENST00000430777; ENSP00000392820; ENSG00000236873. ENST00000433376; ENSP00000387810; ENSG00000228892. ENST00000433896; ENSP00000408842; ENSG00000236873. ENST00000434614; ENSP00000401287; ENSG00000235758. ENST00000436149; ENSP00000388090; ENSG00000235758. ENST00000439774; ENSP00000398016; ENSG00000236873. ENST00000440840; ENSP00000395863; ENSG00000236873. ENST00000444369; ENSP00000408032; ENSG00000227642. ENST00000446323; ENSP00000392083; ENSG00000226467. ENST00000446463; ENSP00000405864; ENSG00000226467. ENST00000448196; ENSP00000404106; ENSG00000235758. ENST00000449776; ENSP00000410831; ENSG00000226467. ENST00000451833; ENSP00000406582; ENSG00000228892. ENST00000452393; ENSP00000406614; ENSG00000228892. ENST00000452427; ENSP00000387738; ENSG00000235758. ENST00000454929; ENSP00000390988; ENSG00000227642. ENST00000455898; ENSP00000395613; ENSG00000228892. ENST00000456421; ENSP00000389516; ENSG00000227642. ENST00000456679; ENSP00000388815; ENSG00000227642. ENST00000457923; ENSP00000405565; ENSG00000226467.
GeneID	10554.
KEGG	hsa:10554.
UCSC	uc003oae.3. human.
Organism-specific databases
CTD	10554.
GeneCards	GC06M032135.
HGNC	HGNC:324. AGPAT1.
MIM	603099. gene.
neXtProt	NX_Q99943.
PharmGKB	PA24621.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0204.
HOGENOM	HOG000026375.
HOVERGEN	HBG000676.
InParanoid	Q99943.
KO	K13509.
OMA	GVVIIEM.
OrthoDB	EOG483D59.
PhylomeDB	Q99943.
Enzyme and pathway databases
BioCyc	MetaCyc:HS09762-MONOMER.
BRENDA	2.3.1.51. 2681.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00557; UER00613.
Gene expression databases
ArrayExpress	Q99943.
Bgee	Q99943.
CleanEx	HS_AGPAT1.
Genevestigator	Q99943.
GermOnline	ENSG00000204310. Homo sapiens.
Family and domain databases
InterPro	IPR004552. AGP_acyltrans. IPR002123. Plipid/glycerol_acylTrfase. [Graphical view]
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
SMART	SM00563. PlsC. 1 hit. [Graphical view]
TIGRFAMs	TIGR00530. AGP_acyltrn. 1 hit.
ProtoNet	Search...
Other
ChEMBL	CHEMBL3583.
GenomeRNAi	10554.
NextBio	40041.
SOURCE	Search...

Entry information

Entry name

PLCA_HUMAN

Accession

Primary (citable) accession number: Q99943
Secondary accession number(s): A2BFI5, Q5BL03

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 1, 1998
Last modified:	April 3, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.