O15120 (PLCB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 2
Short name=1-AGP acyltransferase 2
Short name=1-AGPAT 2
Lysophosphatidic acid acyltransferase beta
Short name=LPAAT-beta

Gene names

Name:

AGPAT2

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	278 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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.
Tissue specificity	Expressed predominantly in heart and liver.
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.
Involvement in disease	Congenital generalized lipodystrophy 1 (CGL1) [MIM:608594]: An autosomal recessive disorder characterized by a near complete absence of adipose tissue, extreme insulin resistance, hypertriglyceridemia, hepatic steatosis and early onset of diabetes. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10
Sequence similarities	Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Disease	Congenital generalized lipodystrophy Diabetes mellitus Disease mutation
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	CDP-diacylglycerol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway phosphatidic acid biosynthetic process Inferred from genetic interaction Ref.3. Source: BHF-UCL positive regulation of cytokine production Inferred from mutant phenotype Ref.3. Source: BHF-UCL positive regulation of cytokine-mediated signaling pathway Inferred by curator Ref.3. 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 Non-traceable author statement PubMed 9461603. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O15120-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O15120-2)

The sequence of this isoform differs from the canonical sequence as follows:
     165-196: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 278	278	1-acyl-sn-glycerol-3-phosphate acyltransferase beta		PRO_0000208192
Regions
	Transmembrane	1 – 21	21	Helical; Potential
	Transmembrane	30 – 50	21	Helical; Potential
	Transmembrane	122 – 142	21	Helical; Potential
	Motif	98 – 103	6	HXXXXD motif
Amino acid modifications
	Modified residue	255	1	Phosphothreonine By similarity
	Modified residue	260	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	165 – 196	32	Missing in isoform 2.		VSP_005071
	Natural variant	136	1	G → R in CGL1. Ref.10		VAR_017328
	Natural variant	140	1	Missing in CGL1. Ref.10		VAR_017326
	Natural variant	228	1	L → P in CGL1. Ref.10		VAR_017327
	Natural variant	239	1	A → V in CGL1. Ref.10		VAR_017325
Experimental info
	Sequence conflict	126	1	L → V in AAB64299. Ref.2
	Sequence conflict	200	1	V → F in AAH00026. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 1E58F537F703BE9F	FASTA	278	30,914
	10 20 30 40 50 60 MELWPCLAAA LLLLLLLVQL SRAAEFYAKV ALYCALCFTV SAVASLVCLL RHGGRTVENM 70 80 90 100 110 120 SIIGWFVRSF KYFYGLRFEV RDPRRLQEAR PCVIVSNHQS ILDMMGLMEV LPERCVQIAK 130 140 150 160 170 180 RELLFLGPVG LIMYLGGVFF INRQRSSTAM TVMADLGERM VRENLKVWIY PEGTRNDNGD 190 200 210 220 230 240 LLPFKKGAFY LAVQAQVPIV PVVYSSFSSF YNTKKKFFTS GTVTVQVLEA IPTSGLTAAD 250 260 270 VPALVDTCHR AMRTTFLHIS KTPQENGATA GSGVQPAQ
	Isoform 2 [UniParc]. Checksum: 2A6E877F48DC3FE9	FASTA	246	27,279
	10 20 30 40 50 60 MELWPCLAAA LLLLLLLVQL SRAAEFYAKV ALYCALCFTV SAVASLVCLL RHGGRTVENM 70 80 90 100 110 120 SIIGWFVRSF KYFYGLRFEV RDPRRLQEAR PCVIVSNHQS ILDMMGLMEV LPERCVQIAK 130 140 150 160 170 180 RELLFLGPVG LIMYLGGVFF INRQRSSTAM TVMADLGERM VRENVPIVPV VYSSFSSFYN 190 200 210 220 230 240 TKKKFFTSGT VTVQVLEAIP TSGLTAADVP ALVDTCHRAM RTTFLHISKT PQENGATAGS GVQPAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human lysophosphatidic acid acyltransferase. cDNA cloning, expression, and localization to chromosome 9q34.3." Eberhardt C., Gray P.W., Tjoelker L.W. J. Biol. Chem. 272:20299-20305(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] (ISOFORM 1).
[3]	"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] (ISOFORM 1).
[4]	Leung D.W., Tompkin C.K., West J. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 51.
[5]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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].
[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] (ISOFORMS 1 AND 2). Tissue: Kidney and Skin.
[8]	"Acquired and inherited lipodystrophies." Garg A. N. Engl. J. Med. 350:1220-1234(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"AGPAT2 is mutated in congenital generalized lipodystrophy linked to chromosome 9q34." Agarwal A.K., Arioglu E., de Almeida S., Akkoc N., Taylor S.I., Bowcock A.M., Barnes R.I., Garg A. Nat. Genet. 31:21-23(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CGL1 ARG-136; PHE-140 DEL; PRO-228 AND VAL-239.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF000237 mRNA. Translation: AAC51649.1. AF011374 mRNA. Translation: AAB64299.1. U56418 mRNA. Translation: AAB58776.2. AL590226 Genomic DNA. Translation: CAH71722.1. AL590226 Genomic DNA. Translation: CAH71723.1. CH471090 Genomic DNA. Translation: EAW88249.1. CH471090 Genomic DNA. Translation: EAW88251.1. BC000026 mRNA. Translation: AAH00026.1. BC004529 mRNA. Translation: AAH04529.1.
IPI	IPI00221372. IPI00464993.
RefSeq	NP_001012745.1. NM_001012727.1. NP_006403.2. NM_006412.3.
UniGene	Hs.320151.
3D structure databases
ProteinModelPortal	O15120.
ModBase	Search...
Protein-protein interaction databases
IntAct	O15120. 6 interactions.
STRING	9606.ENSP00000360761.
PTM databases
PhosphoSite	O15120.
Proteomic databases
PaxDb	O15120.
PRIDE	O15120.
Protocols and materials databases
DNASU	10555.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000371694; ENSP00000360759; ENSG00000169692. ENST00000371696; ENSP00000360761; ENSG00000169692. ENST00000538402; ENSP00000438919; ENSG00000169692.
GeneID	10555.
KEGG	hsa:10555.
UCSC	uc004cii.1. human. uc004cij.1. human.
Organism-specific databases
CTD	10555.
GeneCards	GC09M139567.
HGNC	HGNC:325. AGPAT2.
HPA	HPA019544.
MIM	603100. gene. 608594. phenotype.
neXtProt	NX_O15120.
Orphanet	528. Berardinelli-Seip congenital lipodystrophy.
PharmGKB	PA24622.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0204.
HOVERGEN	HBG000676.
InParanoid	O15120.
KO	K13509.
OMA	EARPCVI.
OrthoDB	EOG483D59.
Enzyme and pathway databases
BioCyc	MetaCyc:HS09990-MONOMER.
BRENDA	2.3.1.51. 2681.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00557; UER00613.
Gene expression databases
ArrayExpress	O15120.
Bgee	O15120.
CleanEx	HS_AGPAT2.
Genevestigator	O15120.
GermOnline	ENSG00000169692. 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
BindingDB	O15120.
ChEMBL	CHEMBL4772.
GenomeRNAi	10555.
NextBio	40047.
SOURCE	Search...

Entry information

Entry name

PLCB_HUMAN

Accession

Primary (citable) accession number: O15120
Secondary accession number(s): O00516 , O15106, Q5VUD3, Q5VUD4, Q9BSV7, Q9BWR7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 122 of the entry and version 1 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.