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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 (PubMed:17013544, PubMed:17689486). Required for primary processing step during piRNA biosynthesis (PubMed:23611983). Molecular mechanisms by which it promotes piRNA biosynthesis are unclear and do not involve its acyltransferase activity (PubMed:23611983).3 Publications

Catalytic activityi

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

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

GO - Biological processi

  • CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
  • glycerol-3-phosphate metabolic process Source: MGI
  • piRNA biosynthetic process Source: UniProtKB
  • triglyceride biosynthetic process Source: MGI

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processLipid 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 databases

SwissLipidsiSLP:000000102.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate acyltransferase 2, mitochondrial (EC:2.3.1.152 Publications)
Short name:
GPAT-2
Alternative name(s):
xGPAT11 Publication
Gene namesi
Name:Gpat2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2684962. Gpat2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 305CytoplasmicSequence analysisAdd BLAST305
Transmembranei306 – 332HelicalSequence analysisAdd BLAST27
Topological domaini333 – 449Mitochondrial intermembraneSequence analysisAdd BLAST117
Transmembranei450 – 472HelicalSequence analysisAdd BLAST23
Topological domaini473 – 801CytoplasmicSequence analysisAdd BLAST329

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial outer membrane Source: UniProtKB-SubCell
  • mitochondrion Source: MGI

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi205H → G: Does not affect ability to promote piRNA biosynthesis. 1 Publication1
Mutagenesisi210D → G: Does not affect ability to promote piRNA biosynthesis. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003258541 – 801Glycerol-3-phosphate acyltransferase 2, mitochondrialAdd BLAST801

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei662PhosphoserineCombined sources1
Modified residuei666PhosphothreonineCombined sources1
Modified residuei668PhosphoserineCombined sources1
Modified residuei670PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ14DK4.
PRIDEiQ14DK4.

PTM databases

iPTMnetiQ14DK4.
PhosphoSitePlusiQ14DK4.

Expressioni

Tissue specificityi

Highly expressed in the testis (PubMed:26268560). Expressed at lower levels in the heart, liver, kidney, spleen and adipose cells (PubMed:17013544, PubMed:17689486).3 Publications

Developmental stagei

Highly expressed in pachytene spermatocytes (at protein level) (PubMed:26268560).1 Publication

Inductioni

Up-regulated by retinoic acid (PubMed:26268560).1 Publication

Gene expression databases

BgeeiENSMUSG00000046338.
CleanExiMM_A530057A03RIK.
GenevisibleiQ14DK4. MM.

Interactioni

Subunit structurei

Interacts with PIWIL2 (PubMed:23611983).1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000106002.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni180 – 290AcyltransferaseAdd BLAST111

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi205 – 210HXXXXD motif6

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.
OMAiCVRVHLA.
OrthoDBiEOG091G0IKA.
PhylomeDBiQ14DK4.
TreeFamiTF313360.

Family and domain databases

InterProiView protein in InterPro
IPR022284. GPAT/DHAPAT.
IPR002123. Plipid/glycerol_acylTrfase.
PANTHERiPTHR12563. PTHR12563. 1 hit.
PfamiView protein in Pfam
PF01553. Acyltransferase. 1 hit.
SMARTiView protein in SMART
SM00563. PlsC. 1 hit.

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti150G → S in AAI13166 (PubMed:15489334).Curated1
Sequence conflicti150G → S in AAI13777 (PubMed:15489334).Curated1
Sequence conflicti238A → V in BAD21404 (PubMed:15449545).Curated1
Sequence conflicti272R → H in AAI13166 (PubMed:15489334).Curated1
Sequence conflicti272R → H in AAI13777 (PubMed:15489334).Curated1
Sequence conflicti482Q → E in BAC30772 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0324571 – 3Missing in isoform 2 and isoform 3. 2 Publications3
Alternative sequenceiVSP_032458414Missing in isoform 2. 1 Publication1

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_006499138.3. [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

Similar proteinsi

Entry informationi

Entry nameiGPAT2_MOUSE
AccessioniPrimary (citable) accession number: Q14DK4
Secondary accession number(s): B1AW16
, Q0KK60, Q14CH8, Q6KAQ3, Q8BRZ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 5, 2009
Last modified: August 30, 2017
This is version 87 of the entry and version 3 of the sequence. See 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