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Protein

Glycerol-3-phosphate acyltransferase 2, mitochondrial

Gene

Gpat2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis.2 Publications

Catalytic activityi

Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.

Enzyme regulationi

Inhibited by N-ethylmaleimide (NEM).1 Publication

Pathwayi: CDP-diacylglycerol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glycerol-3-phosphate acyltransferase 1, mitochondrial (Gpam), Glycerol-3-phosphate acyltransferase 4 (Gpat4), Glycerol-3-phosphate acyltransferase 3 (Gpat3), Glycerol-3-phosphate acyltransferase 2, mitochondrial (Gpat2)
  2. 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma (Agpat3), 1-acyl-sn-glycerol-3-phosphate acyltransferase beta (Agpat2), 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha (Agpat1), Lysocardiolipin acyltransferase 1 (Lclat1), 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon (Agpat5), 1-acyl-sn-glycerol-3-phosphate acyltransferase delta (Agpat4)
  3. Phosphatidate cytidylyltransferase, mitochondrial (Tamm41), Phosphatidate cytidylyltransferase, mitochondrial (Tamm41), Phosphatidate cytidylyltransferase (Cds2), Phosphatidate cytidylyltransferase (Cds2), Phosphatidate cytidylyltransferase 2 (Cds2), Phosphatidate cytidylyltransferase (Cds2), Phosphatidate cytidylyltransferase 1 (Cds1)
This subpathway is part of the pathway CDP-diacylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate, the pathway CDP-diacylglycerol biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

  • glycerol-3-phosphate O-acyltransferase activity Source: MGI

GO - Biological processi

  • CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
  • glycerol-3-phosphate metabolic process Source: MGI
  • triglyceride biosynthetic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BRENDAi2.3.1.15. 3474.
ReactomeiR-MMU-1483166. Synthesis of PA.
UniPathwayiUPA00557; UER00612.

Chemistry

SwissLipidsiSLP:000000102.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate acyltransferase 2, mitochondrial (EC:2.3.1.15)
Short name:
GPAT-2
Alternative name(s):
xGPAT1
Gene namesi
Name:Gpat2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2684962. Gpat2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 305305CytoplasmicSequence analysisAdd
BLAST
Transmembranei306 – 33227HelicalSequence analysisAdd
BLAST
Topological domaini333 – 449117Mitochondrial intermembraneSequence analysisAdd
BLAST
Transmembranei450 – 47223HelicalSequence analysisAdd
BLAST
Topological domaini473 – 801329CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial outer membrane Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 801801Glycerol-3-phosphate acyltransferase 2, mitochondrialPRO_0000325854Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei662 – 6621PhosphoserineCombined sources
Modified residuei666 – 6661PhosphothreonineCombined sources
Modified residuei668 – 6681PhosphoserineCombined sources
Modified residuei670 – 6701PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ14DK4.
PRIDEiQ14DK4.

PTM databases

iPTMnetiQ14DK4.
PhosphoSiteiQ14DK4.

Expressioni

Tissue specificityi

Highly exprresed in the testis. Expressed at lower levels in the heart, liver, kidney, spleen and adipose cells.2 Publications

Gene expression databases

BgeeiQ14DK4.
CleanExiMM_A530057A03RIK.
GenevisibleiQ14DK4. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000106002.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni180 – 290111AcyltransferaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi205 – 2106HXXXXD 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

Belongs to the GPAT/DAPAT family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IT7W. Eukaryota.
ENOG410YV5H. LUCA.
GeneTreeiENSGT00520000055570.
HOGENOMiHOG000112780.
InParanoidiQ14DK4.
KOiK00629.
OMAiNARSCWG.
OrthoDBiEOG74R1PZ.
PhylomeDBiQ14DK4.
TreeFamiTF313360.

Family and domain databases

InterProiIPR022284. GPAT/DHAPAT.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERiPTHR12563. PTHR12563. 1 hit.
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14DK4-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDTMLKSNPQ TQQRSNHNGQ ETSLWSSSFG MKMEAITPFL GKYRPFMGRC
60 70 80 90 100
CQTCTPKSWE SLFHRSIMDL GFCNVILVKE ENTRFRGWLV RRLCYFLWSL
110 120 130 140 150
EQHIPTSFDA SQKIMENTGV QNLLSGRVPG AAGEGQAPEL VKKEVQRILG
160 170 180 190 200
HIQTTPRPFL LRLFSWALLW FLNRLFLNVQ LHKGQMKMVQ KAVQEGSPLV
210 220 230 240 250
FLSTHKSLLD GFLLPFVLFS QGLGVVRVAL DSRTCSPALR ALLRKLGGLF
260 270 280 290 300
LPPEVNLSLD NSEGILARAV VRATVEELLT SGQPLLIFLE EPPGSPGPRL
310 320 330 340 350
SALGQAWLGV VIQAVQAGII SDATLVPVAI AYDLVPDAPC NMNHDLAPLG
360 370 380 390 400
LWTGALAVFR RLCNCWGCNR RVCVRVHLAQ PFSLQEYTIN ARSCWDSRQT
410 420 430 440 450
LEHLLQPIVL GECSVVPDTE KEQEWTPPTG LLLALKEEDQ LLVRRLSRHV
460 470 480 490 500
LSASVASSAV MSTAIMATLL LLKHQKGVVL SQLLGEFSWL TEETLLRGFD
510 520 530 540 550
VGFSGQLRCL AQHTLSLLRA HVVLLRVHQG DLVVVPRPGP GLTHLARLSM
560 570 580 590 600
ELLPTFLSEA VGACAVRGLL AGRVPPEGPW ELQGIELLSQ NELYRQILLL
610 620 630 640 650
LHLLPQDLLL PQPCQSSYCY CQEVLDRLIQ CGLLVAEETP GSRPACDTGR
660 670 680 690 700
QHLSAKLLWK PSGDFTDSES DDFEEPGGRC FRLSQQSRCP DFFLFLCRLL
710 720 730 740 750
SPILKAFAQA ATFLHLGQLP DSEVAYSEKL FQFLQACAQE EGIFECADPN
760 770 780 790 800
LAISAVWTFK DLGVLQEMPS PTGPQLHLSP TFATRDNQDK LEQFIRQFIC

S
Length:801
Mass (Da):89,150
Last modified:May 5, 2009 - v3
Checksum:i438B6E1530F27BBC
GO
Isoform 2 (identifier: Q14DK4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: Missing.
     414-414: Missing.

Note: No experimental confirmation available.
Show »
Length:797
Mass (Da):88,715
Checksum:i970B1E35D561870C
GO
Isoform 3 (identifier: Q14DK4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: Missing.

Show »
Length:798
Mass (Da):88,802
Checksum:i74B93430FB0F6644
GO

Sequence cautioni

The sequence AAI13777.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAD21404.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501G → S in AAI13166 (PubMed:15489334).Curated
Sequence conflicti150 – 1501G → S in AAI13777 (PubMed:15489334).Curated
Sequence conflicti238 – 2381A → V in BAD21404 (PubMed:15449545).Curated
Sequence conflicti272 – 2721R → H in AAI13166 (PubMed:15489334).Curated
Sequence conflicti272 – 2721R → H in AAI13777 (PubMed:15489334).Curated
Sequence conflicti482 – 4821Q → E in BAC30772 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 33Missing in isoform 2 and isoform 3. 2 PublicationsVSP_032457
Alternative sequencei414 – 4141Missing in isoform 2. 1 PublicationVSP_032458

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB257502 mRNA. Translation: BAF03614.1.
AK131154 mRNA. Translation: BAD21404.1. Different initiation.
AL731831, AL731836 Genomic DNA. Translation: CAM13442.1.
AL731836, AL731831 Genomic DNA. Translation: CAM13878.1.
BC113776 mRNA. Translation: AAI13777.1. Different initiation.
BC113165 mRNA. Translation: AAI13166.1.
AK040991 mRNA. Translation: BAC30772.1.
CCDSiCCDS38232.2. [Q14DK4-1]
RefSeqiNP_001074558.2. NM_001081089.2. [Q14DK4-1]
XP_006499201.1. XM_006499138.2. [Q14DK4-1]
UniGeneiMm.440454.
Mm.491813.

Genome annotation databases

EnsembliENSMUST00000062211; ENSMUSP00000049619; ENSMUSG00000046338. [Q14DK4-1]
GeneIDi215456.
KEGGimmu:215456.
UCSCiuc008mfj.2. mouse. [Q14DK4-1]
uc012cdn.1. mouse. [Q14DK4-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB257502 mRNA. Translation: BAF03614.1.
AK131154 mRNA. Translation: BAD21404.1. Different initiation.
AL731831, AL731836 Genomic DNA. Translation: CAM13442.1.
AL731836, AL731831 Genomic DNA. Translation: CAM13878.1.
BC113776 mRNA. Translation: AAI13777.1. Different initiation.
BC113165 mRNA. Translation: AAI13166.1.
AK040991 mRNA. Translation: BAC30772.1.
CCDSiCCDS38232.2. [Q14DK4-1]
RefSeqiNP_001074558.2. NM_001081089.2. [Q14DK4-1]
XP_006499201.1. XM_006499138.2. [Q14DK4-1]
UniGeneiMm.440454.
Mm.491813.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000106002.

Chemistry

SwissLipidsiSLP:000000102.

PTM databases

iPTMnetiQ14DK4.
PhosphoSiteiQ14DK4.

Proteomic databases

PaxDbiQ14DK4.
PRIDEiQ14DK4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000062211; ENSMUSP00000049619; ENSMUSG00000046338. [Q14DK4-1]
GeneIDi215456.
KEGGimmu:215456.
UCSCiuc008mfj.2. mouse. [Q14DK4-1]
uc012cdn.1. mouse. [Q14DK4-2]

Organism-specific databases

CTDi150763.
MGIiMGI:2684962. Gpat2.

Phylogenomic databases

eggNOGiENOG410IT7W. Eukaryota.
ENOG410YV5H. LUCA.
GeneTreeiENSGT00520000055570.
HOGENOMiHOG000112780.
InParanoidiQ14DK4.
KOiK00629.
OMAiNARSCWG.
OrthoDBiEOG74R1PZ.
PhylomeDBiQ14DK4.
TreeFamiTF313360.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00612.
BRENDAi2.3.1.15. 3474.
ReactomeiR-MMU-1483166. Synthesis of PA.

Miscellaneous databases

PROiQ14DK4.
SOURCEiSearch...

Gene expression databases

BgeeiQ14DK4.
CleanExiMM_A530057A03RIK.
GenevisibleiQ14DK4. MM.

Family and domain databases

InterProiIPR022284. GPAT/DHAPAT.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERiPTHR12563. PTHR12563. 1 hit.
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional characterization of a novel mitochondrial N-ethylmaleimide-sensitive glycerol-3-phosphate acyltransferase (GPAT2)."
    Wang S., Lee D.P., Gong N., Schwerbrock N.M.J., Mashek D.G., Gonzalez-Baro M.R., Stapleton C., Li L.O., Lewin T.M., Coleman R.A.
    Arch. Biochem. Biophys. 465:347-358(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "Molecular cloning of a murine glycerol-3-phosphate acyltransferase-like protein 1 (xGPAT1)."
    Harada N., Hara S., Yoshida M., Zenitani T., Mawatari K., Nakano M., Takahashi A., Hosaka T., Yoshimoto K., Nakaya Y.
    Mol. Cell. Biochem. 297:41-51(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Kidney.
  3. "Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
    DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Embryonic tail.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2 AND 3).
  6. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 482-801.
    Strain: C57BL/6J.
    Tissue: Aorta and Vein.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662; THR-666; SER-668 AND SER-670, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.
  8. Cited for: SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY.

Entry informationi

Entry nameiGPAT2_MOUSE
AccessioniPrimary (citable) accession number: Q14DK4
Secondary accession number(s): B1AW16
, Q0KK60, Q14CH8, Q6KAQ3, Q8BRZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 5, 2009
Last modified: June 8, 2016
This is version 78 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.