SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q53EU6

- GPAT3_HUMAN

UniProt

Q53EU6 - GPAT3_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Glycerol-3-phosphate acyltransferase 3
Gene
AGPAT9, GPAT3, MAG1, HMFN0839, UNQ2753/PRO6492
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May transfer the acyl-group from acyl-coA to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Also transfers the acyl-group from acyl-coA to the sn-2 position of 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid, or LPA), forming 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid, or PA).3 Publications

Catalytic activityi

Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.3 Publications
Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.3 Publications

Enzyme regulationi

Inhibited by N-ethylmaleimide (NEM).1 Publication

Pathwayi

GO - Molecular functioni

  1. 1-acylglycerol-3-phosphate O-acyltransferase activity Source: UniProtKB-EC
  2. glycerol-3-phosphate O-acyltransferase activity Source: UniProtKB

GO - Biological processi

  1. CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
  2. cellular lipid metabolic process Source: Reactome
  3. glycerophospholipid biosynthetic process Source: Reactome
  4. phosphatidic acid biosynthetic process Source: Reactome
  5. phospholipid metabolic process Source: Reactome
  6. regulation of TOR signaling Source: UniProtKB
  7. small molecule metabolic process Source: Reactome
  8. triglyceride biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiREACT_1190. Triglyceride Biosynthesis.
REACT_120906. Synthesis of PA.
UniPathwayiUPA00282.
UPA00557; UER00612.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate acyltransferase 3 (EC:2.3.1.15)
Short name:
GPAT-3
Alternative name(s):
1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10
Short name:
AGPAT 10
1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9 (EC:2.3.1.51)
Short name:
1-AGP acyltransferase 9
Short name:
1-AGPAT 9
Acyl-CoA:glycerol-3-phosphate acyltransferase 3
Short name:
hGPAT3
Lung cancer metastasis-associated protein 1
Lysophosphatidic acid acyltransferase theta
Short name:
LPAAT-theta
MAG-1
Gene namesi
Name:AGPAT9
Synonyms:GPAT3, MAG1
ORF Names:HMFN0839, UNQ2753/PRO6492
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:28157. AGPAT9.

Subcellular locationi

Endoplasmic reticulum membrane; Multi-pass membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei14 – 3421Helical; Reviewed prediction
Add
BLAST
Transmembranei137 – 15721Helical; Reviewed prediction
Add
BLAST
Transmembranei161 – 18121Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum membrane Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162375888.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Glycerol-3-phosphate acyltransferase 3
PRO_0000291570Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei68 – 681Phosphoserine1 Publication
Modified residuei77 – 771Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ53EU6.
PaxDbiQ53EU6.
PRIDEiQ53EU6.

PTM databases

PhosphoSiteiQ53EU6.

Expressioni

Tissue specificityi

Widely expressed. Expressed in liver, kidney, testis, brain, heart, skeletal muscle, thyroid, prostate, thymus and placenta. Also expressed lung and adipose tissue.2 Publications

Gene expression databases

BgeeiQ53EU6.
CleanExiHS_AGPAT9.
GenevestigatoriQ53EU6.

Organism-specific databases

HPAiCAB033749.
HPA029414.

Interactioni

Protein-protein interaction databases

BioGridi124267. 2 interactions.
STRINGi9606.ENSP00000264409.

Structurei

3D structure databases

ProteinModelPortaliQ53EU6.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi229 – 2346HXXXXD motif

Domaini

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 similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0204.
HOGENOMiHOG000265725.
InParanoidiQ53EU6.
KOiK13506.
OMAiLVRYCVL.
OrthoDBiEOG70GMFG.
PhylomeDBiQ53EU6.
TreeFamiTF315039.

Family and domain databases

InterProiIPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q53EU6-1 [UniParc]FASTAAdd to Basket

« Hide

MEGAELAGKI LSTWLTLVLG FILLPSVFGV SLGISEIYMK ILVKTLEWAT    50
IRIEKGTPKE SILKNSASVG IIQRDESPME KGLSGLRGRD FELSDVFYFS 100
KKGLEAIVED EVTQRFSSEE LVSWNLLTRT NVNFQYISLR LTMVWVLGVI 150
VRYCVLLPLR VTLAFIGISL LVIGTTLVGQ LPDSSLKNWL SELVHLTCCR 200
ICVRALSGTI HYHNKQYRPQ KGGICVANHT SPIDVLILTT DGCYAMVGQV 250
HGGLMGIIQR AMVKACPHVW FERSEMKDRH LVTKRLKEHI ADKKKLPILI 300
FPEGTCINNT SVMMFKKGSF EIGGTIHPVA IKYNPQFGDA FWNSSKYNMV 350
SYLLRMMTSW AIVCDVWYMP PMTREEGEDA VQFANRVKSA IAIQGGLTEL 400
PWDGGLKRAK VKDIFKEEQQ KNYSKMIVGN GSLS 434
Length:434
Mass (Da):48,705
Last modified:June 26, 2007 - v2
Checksum:i80DD5423E5E7847A
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti156 – 1561L → I in BAD97263. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ324782 mRNA. Translation: ABC55674.1.
DQ345298 mRNA. Translation: ABC70186.1.
AY358100 mRNA. Translation: AAQ88467.1.
AK055749 mRNA. Translation: BAB71002.1.
AK223543 mRNA. Translation: BAD97263.1.
BC073136 mRNA. Translation: AAH73136.1.
BC090956 mRNA. Translation: AAH90956.1.
AB075872 mRNA. Translation: BAD38654.1.
CCDSiCCDS3606.1.
RefSeqiNP_001243350.1. NM_001256421.1.
NP_001243351.1. NM_001256422.1.
NP_116106.2. NM_032717.4.
UniGeneiHs.99196.

Genome annotation databases

EnsembliENST00000264409; ENSP00000264409; ENSG00000138678.
ENST00000395226; ENSP00000378651; ENSG00000138678.
GeneIDi84803.
KEGGihsa:84803.
UCSCiuc003how.4. human.

Polymorphism databases

DMDMi150403919.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ324782 mRNA. Translation: ABC55674.1 .
DQ345298 mRNA. Translation: ABC70186.1 .
AY358100 mRNA. Translation: AAQ88467.1 .
AK055749 mRNA. Translation: BAB71002.1 .
AK223543 mRNA. Translation: BAD97263.1 .
BC073136 mRNA. Translation: AAH73136.1 .
BC090956 mRNA. Translation: AAH90956.1 .
AB075872 mRNA. Translation: BAD38654.1 .
CCDSi CCDS3606.1.
RefSeqi NP_001243350.1. NM_001256421.1.
NP_001243351.1. NM_001256422.1.
NP_116106.2. NM_032717.4.
UniGenei Hs.99196.

3D structure databases

ProteinModelPortali Q53EU6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124267. 2 interactions.
STRINGi 9606.ENSP00000264409.

PTM databases

PhosphoSitei Q53EU6.

Polymorphism databases

DMDMi 150403919.

Proteomic databases

MaxQBi Q53EU6.
PaxDbi Q53EU6.
PRIDEi Q53EU6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264409 ; ENSP00000264409 ; ENSG00000138678 .
ENST00000395226 ; ENSP00000378651 ; ENSG00000138678 .
GeneIDi 84803.
KEGGi hsa:84803.
UCSCi uc003how.4. human.

Organism-specific databases

CTDi 84803.
GeneCardsi GC04P084457.
HGNCi HGNC:28157. AGPAT9.
HPAi CAB033749.
HPA029414.
MIMi 610958. gene.
neXtProti NX_Q53EU6.
PharmGKBi PA162375888.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0204.
HOGENOMi HOG000265725.
InParanoidi Q53EU6.
KOi K13506.
OMAi LVRYCVL.
OrthoDBi EOG70GMFG.
PhylomeDBi Q53EU6.
TreeFami TF315039.

Enzyme and pathway databases

UniPathwayi UPA00282 .
UPA00557 ; UER00612 .
Reactomei REACT_1190. Triglyceride Biosynthesis.
REACT_120906. Synthesis of PA.

Miscellaneous databases

GeneWikii AGPAT9.
GenomeRNAii 84803.
NextBioi 74971.
PROi Q53EU6.
SOURCEi Search...

Gene expression databases

Bgeei Q53EU6.
CleanExi HS_AGPAT9.
Genevestigatori Q53EU6.

Family and domain databases

InterProi IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view ]
Pfami PF01553. Acyltransferase. 1 hit.
[Graphical view ]
SMARTi SM00563. PlsC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of metastasis associated genes MAG-1 and MAG-2."
    Zhang J., Meng Y., Du Z., Chen Z., Ling X., Xu Y., Lu Y.
    Zhongguo Fei Ai Za Zhi 6:460-463(2003)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Identification of a novel human lysophosphatidic acid acyltransferase, LPAAT-theta, which activates mTOR pathway."
    Tang W., Yuan J., Chen X., Gu X., Luo K., Li J., Wan B., Wang Y., Yu L.
    J. Biochem. Mol. Biol. 39:626-635(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  6. "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: PNS and Testis.
  7. "Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas."
    Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.
    Oncogene 23:5901-5911(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-434.
  8. "Molecular identification of microsomal acyl-CoA:glycerol-3-phosphate acyltransferase, a key enzyme in de novo triacylglycerol synthesis."
    Cao J., Li J.-L., Li D., Tobin J.F., Gimeno R.E.
    Proc. Natl. Acad. Sci. U.S.A. 103:19695-19700(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68 AND SER-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Functional characterization of the human 1-acylglycerol-3-phosphate-O-acyltransferase isoform 10/glycerol-3-phosphate acyltransferase isoform 3."
    Sukumaran S., Barnes R.I., Garg A., Agarwal A.K.
    J. Mol. Endocrinol. 42:469-478(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiGPAT3_HUMAN
AccessioniPrimary (citable) accession number: Q53EU6
Secondary accession number(s): Q68CJ4, Q6GPI6, Q96NA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: September 3, 2014
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

Despite its name, this protein appears to lack measurable glycerol-3-phosphate acyltransferase activity under some conditions (PMID:19318427).

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi