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O15120 (PLCB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length278 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Ref.1 Ref.9 Ref.11

Catalytic activity

Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate. Ref.1 Ref.9 Ref.11

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.11.

Tissue specificity

Expressed predominantly in adipose tissue, pancreas and liver. Ref.11

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.9 Ref.12

Sequence similarities

Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.

Ontologies

Keywords
   Biological processLipid biosynthesis
Lipid metabolism
Phospholipid biosynthesis
Phospholipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseCongenital generalized lipodystrophy
Diabetes mellitus
Disease mutation
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCDP-diacylglycerol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

cellular lipid metabolic process

Traceable author statement. Source: Reactome

epidermis development

Inferred from electronic annotation. Source: Ensembl

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

phosphatidic acid biosynthetic process

Inferred from genetic interaction Ref.3. Source: BHF-UCL

phospholipid metabolic process

Non-traceable author statement PubMed 9461603. Source: UniProtKB

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_componentendoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_function1-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 2782551-acyl-sn-glycerol-3-phosphate acyltransferase beta
PRO_0000208192

Regions

Transmembrane30 – 5021Helical; Potential
Transmembrane122 – 14221Helical; Potential
Transmembrane187 – 20721Helical; Potential
Motif98 – 1036HXXXXD motif
Motif172 – 1754EGTR motif

Natural variations

Alternative sequence165 – 19632Missing in isoform 2.
VSP_005071
Natural variant1361G → R in CGL1; reduced 1-acyl-sn-glycerol-3-phosphate acyltransferase activity. Ref.9 Ref.12
VAR_017328
Natural variant1401Missing in CGL1; reduced 1-acyl-sn-glycerol-3-phosphate acyltransferase activity. Ref.9 Ref.12
VAR_017326
Natural variant2281L → P in CGL1; reduced 1-acyl-sn-glycerol-3-phosphate acyltransferase activity. Ref.9 Ref.12
VAR_017327
Natural variant2391A → V in CGL1; 90% of wild-type 1-acyl-sn-glycerol-3-phosphate acyltransferase activity. Ref.9 Ref.12
Corresponds to variant rs145975461 [ dbSNP | Ensembl ].
VAR_017325

Experimental info

Sequence conflict1261L → V in AAB64299. Ref.2
Sequence conflict2001V → F in AAH00026. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 1E58F537F703BE9F

FASTA27830,914
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 2A6E877F48DC3FE9
Show »

FASTA24627,279

References

« Hide '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), FUNCTION, CATALYTIC ACTIVITY.
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Enzymatic activity of naturally occurring 1-acylglycerol-3-phosphate-O-acyltransferase 2 mutants associated with congenital generalized lipodystrophy."
Haque W., Garg A., Agarwal A.K.
Biochem. Biophys. Res. Commun. 327:446-453(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANTS CGL1 ARG-136; PHE-140 DEL; PRO-228 AND VAL-239.
[10]"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].
[11]"Human 1-acylglycerol-3-phosphate O-acyltransferase isoforms 1 and 2: biochemical characterization and inability to rescue hepatic steatosis in Agpat2(-/-) gene lipodystrophic mice."
Agarwal A.K., Sukumaran S., Cortes V.A., Tunison K., Mizrachi D., Sankella S., Gerard R.D., Horton J.D., Garg A.
J. Biol. Chem. 286:37676-37691(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[12]"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.

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.
CCDSCCDS35181.1. [O15120-2]
CCDS7003.1. [O15120-1]
RefSeqNP_001012745.1. NM_001012727.1. [O15120-2]
NP_006403.2. NM_006412.3. [O15120-1]
UniGeneHs.320151.

3D structure databases

ProteinModelPortalO15120.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115806. 7 interactions.
IntActO15120. 6 interactions.
STRING9606.ENSP00000360761.

Chemistry

BindingDBO15120.
ChEMBLCHEMBL4772.

PTM databases

PhosphoSiteO15120.

Proteomic databases

MaxQBO15120.
PaxDbO15120.
PRIDEO15120.

Protocols and materials databases

DNASU10555.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371694; ENSP00000360759; ENSG00000169692. [O15120-2]
ENST00000371696; ENSP00000360761; ENSG00000169692. [O15120-1]
ENST00000538402; ENSP00000438919; ENSG00000169692. [O15120-1]
GeneID10555.
KEGGhsa:10555.
UCSCuc004cii.1. human. [O15120-1]
uc004cij.1. human. [O15120-2]

Organism-specific databases

CTD10555.
GeneCardsGC09M139567.
GeneReviewsAGPAT2.
HGNCHGNC:325. AGPAT2.
HPAHPA019544.
MIM603100. gene.
608594. phenotype.
neXtProtNX_O15120.
Orphanet528. Berardinelli-Seip congenital lipodystrophy.
PharmGKBPA24622.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0204.
HOVERGENHBG000676.
InParanoidO15120.
KOK13509.
OMAMFTHTAV.
OrthoDBEOG780RNF.
PhylomeDBO15120.
TreeFamTF314867.

Enzyme and pathway databases

BioCycMetaCyc:HS09990-MONOMER.
BRENDA2.3.1.51. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00557; UER00613.

Gene expression databases

ArrayExpressO15120.
BgeeO15120.
CleanExHS_AGPAT2.
GenevestigatorO15120.

Family and domain databases

InterProIPR004552. AGP_acyltrans.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsTIGR00530. AGP_acyltrn. 1 hit.
ProtoNetSearch...

Other

GeneWikiAGPAT2.
GenomeRNAi10555.
NextBio40047.
PROO15120.
SOURCESearch...

Entry information

Entry namePLCB_HUMAN
AccessionPrimary (citable) accession number: O15120
Secondary accession number(s): O00516 expand/collapse secondary AC list , O15106, Q5VUD3, Q5VUD4, Q9BSV7, Q9BWR7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM