Q14DK4 (GPAT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycerol-3-phosphate acyltransferase 2, mitochondrial
Short name=GPAT-2
EC=2.3.1.15

Alternative name(s):
xGPAT1

Gene names

Name:

Gpat2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	801 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Ref.1 Ref.2
Catalytic activity	Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.
Enzyme regulation	Inhibited by N-ethylmaleimide (NEM). Ref.1
Pathway	Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
Subcellular location	Mitochondrion outer membrane; Multi-pass membrane protein Ref.1 Ref.2.
Tissue specificity	Highly exprresed in the testis. Expressed at lower levels in the heart, liver, kidney, spleen and adipose cells. Ref.1 Ref.2
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.
Sequence similarities	Belongs to the GPAT/DAPAT family.
Sequence caution	The sequence AAI13777.1 differs from that shown. Reason: Erroneous initiation. The sequence BAD21404.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glycerol-3-phosphate metabolic process Inferred from direct assay Ref.1. Source: MGI phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW triglyceride biosynthetic process Inferred from direct assay Ref.1. Source: MGI
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glycerol-3-phosphate O-acyltransferase activity Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q14DK4-1)

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: Q14DK4-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: Q14DK4-3)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 801	801	Glycerol-3-phosphate acyltransferase 2, mitochondrial		PRO_0000325854
Regions
	Transmembrane	159 – 179	21	Helical; Potential
	Transmembrane	450 – 470	21	Helical; Potential
	Region	180 – 290	111	Acyltransferase
	Motif	205 – 210	6	HXXXXD motif
Natural variations
	Alternative sequence	1 – 3	3	Missing in isoform 2 and isoform 3.		VSP_032457
	Alternative sequence	414	1	Missing in isoform 2.		VSP_032458
Experimental info
	Sequence conflict	150	1	G → S in AAI13166. Ref.5
	Sequence conflict	150	1	G → S in AAI13777. Ref.5
	Sequence conflict	238	1	A → V in BAD21404. Ref.3
	Sequence conflict	272	1	R → H in AAI13166. Ref.5
	Sequence conflict	272	1	R → H in AAI13777. Ref.5
	Sequence conflict	482	1	Q → E in BAC30772. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 5, 2009. Version 3. Checksum: 438B6E1530F27BBC	FASTA	801	89,150
	10 20 30 40 50 60 MDTMLKSNPQ TQQRSNHNGQ ETSLWSSSFG MKMEAITPFL GKYRPFMGRC CQTCTPKSWE 70 80 90 100 110 120 SLFHRSIMDL GFCNVILVKE ENTRFRGWLV RRLCYFLWSL EQHIPTSFDA SQKIMENTGV 130 140 150 160 170 180 QNLLSGRVPG AAGEGQAPEL VKKEVQRILG HIQTTPRPFL LRLFSWALLW FLNRLFLNVQ 190 200 210 220 230 240 LHKGQMKMVQ KAVQEGSPLV FLSTHKSLLD GFLLPFVLFS QGLGVVRVAL DSRTCSPALR 250 260 270 280 290 300 ALLRKLGGLF LPPEVNLSLD NSEGILARAV VRATVEELLT SGQPLLIFLE EPPGSPGPRL 310 320 330 340 350 360 SALGQAWLGV VIQAVQAGII SDATLVPVAI AYDLVPDAPC NMNHDLAPLG LWTGALAVFR 370 380 390 400 410 420 RLCNCWGCNR RVCVRVHLAQ PFSLQEYTIN ARSCWDSRQT LEHLLQPIVL GECSVVPDTE 430 440 450 460 470 480 KEQEWTPPTG LLLALKEEDQ LLVRRLSRHV LSASVASSAV MSTAIMATLL LLKHQKGVVL 490 500 510 520 530 540 SQLLGEFSWL TEETLLRGFD VGFSGQLRCL AQHTLSLLRA HVVLLRVHQG DLVVVPRPGP 550 560 570 580 590 600 GLTHLARLSM ELLPTFLSEA VGACAVRGLL AGRVPPEGPW ELQGIELLSQ NELYRQILLL 610 620 630 640 650 660 LHLLPQDLLL PQPCQSSYCY CQEVLDRLIQ CGLLVAEETP GSRPACDTGR QHLSAKLLWK 670 680 690 700 710 720 PSGDFTDSES DDFEEPGGRC FRLSQQSRCP DFFLFLCRLL SPILKAFAQA ATFLHLGQLP 730 740 750 760 770 780 DSEVAYSEKL FQFLQACAQE EGIFECADPN LAISAVWTFK DLGVLQEMPS PTGPQLHLSP 790 800 TFATRDNQDK LEQFIRQFIC S
	Isoform 2 [UniParc]. Checksum: 970B1E35D561870C	FASTA	797	88,715
	10 20 30 40 50 60 MLKSNPQTQQ RSNHNGQETS LWSSSFGMKM EAITPFLGKY RPFMGRCCQT CTPKSWESLF 70 80 90 100 110 120 HRSIMDLGFC NVILVKEENT RFRGWLVRRL CYFLWSLEQH IPTSFDASQK IMENTGVQNL 130 140 150 160 170 180 LSGRVPGAAG EGQAPELVKK EVQRILGHIQ TTPRPFLLRL FSWALLWFLN RLFLNVQLHK 190 200 210 220 230 240 GQMKMVQKAV QEGSPLVFLS THKSLLDGFL LPFVLFSQGL GVVRVALDSR TCSPALRALL 250 260 270 280 290 300 RKLGGLFLPP EVNLSLDNSE GILARAVVRA TVEELLTSGQ PLLIFLEEPP GSPGPRLSAL 310 320 330 340 350 360 GQAWLGVVIQ AVQAGIISDA TLVPVAIAYD LVPDAPCNMN HDLAPLGLWT GALAVFRRLC 370 380 390 400 410 420 NCWGCNRRVC VRVHLAQPFS LQEYTINARS CWDSRQTLEH LLQPIVLGEC VVPDTEKEQE 430 440 450 460 470 480 WTPPTGLLLA LKEEDQLLVR RLSRHVLSAS VASSAVMSTA IMATLLLLKH QKGVVLSQLL 490 500 510 520 530 540 GEFSWLTEET LLRGFDVGFS GQLRCLAQHT LSLLRAHVVL LRVHQGDLVV VPRPGPGLTH 550 560 570 580 590 600 LARLSMELLP TFLSEAVGAC AVRGLLAGRV PPEGPWELQG IELLSQNELY RQILLLLHLL 610 620 630 640 650 660 PQDLLLPQPC QSSYCYCQEV LDRLIQCGLL VAEETPGSRP ACDTGRQHLS AKLLWKPSGD 670 680 690 700 710 720 FTDSESDDFE EPGGRCFRLS QQSRCPDFFL FLCRLLSPIL KAFAQAATFL HLGQLPDSEV 730 740 750 760 770 780 AYSEKLFQFL QACAQEEGIF ECADPNLAIS AVWTFKDLGV LQEMPSPTGP QLHLSPTFAT 790 RDNQDKLEQF IRQFICS
	Isoform 3 [UniParc]. Checksum: 74B93430FB0F6644	FASTA	798	88,802
	10 20 30 40 50 60 MLKSNPQTQQ RSNHNGQETS LWSSSFGMKM EAITPFLGKY RPFMGRCCQT CTPKSWESLF 70 80 90 100 110 120 HRSIMDLGFC NVILVKEENT RFRGWLVRRL CYFLWSLEQH IPTSFDASQK IMENTGVQNL 130 140 150 160 170 180 LSGRVPGAAG EGQAPELVKK EVQRILGHIQ TTPRPFLLRL FSWALLWFLN RLFLNVQLHK 190 200 210 220 230 240 GQMKMVQKAV QEGSPLVFLS THKSLLDGFL LPFVLFSQGL GVVRVALDSR TCSPALRALL 250 260 270 280 290 300 RKLGGLFLPP EVNLSLDNSE GILARAVVRA TVEELLTSGQ PLLIFLEEPP GSPGPRLSAL 310 320 330 340 350 360 GQAWLGVVIQ AVQAGIISDA TLVPVAIAYD LVPDAPCNMN HDLAPLGLWT GALAVFRRLC 370 380 390 400 410 420 NCWGCNRRVC VRVHLAQPFS LQEYTINARS CWDSRQTLEH LLQPIVLGEC SVVPDTEKEQ 430 440 450 460 470 480 EWTPPTGLLL ALKEEDQLLV RRLSRHVLSA SVASSAVMST AIMATLLLLK HQKGVVLSQL 490 500 510 520 530 540 LGEFSWLTEE TLLRGFDVGF SGQLRCLAQH TLSLLRAHVV LLRVHQGDLV VVPRPGPGLT 550 560 570 580 590 600 HLARLSMELL PTFLSEAVGA CAVRGLLAGR VPPEGPWELQ GIELLSQNEL YRQILLLLHL 610 620 630 640 650 660 LPQDLLLPQP CQSSYCYCQE VLDRLIQCGL LVAEETPGSR PACDTGRQHL SAKLLWKPSG 670 680 690 700 710 720 DFTDSESDDF EEPGGRCFRL SQQSRCPDFF LFLCRLLSPI LKAFAQAATF LHLGQLPDSE 730 740 750 760 770 780 VAYSEKLFQF LQACAQEEGI FECADPNLAI SAVWTFKDLG VLQEMPSPTG PQLHLSPTFA 790 TRDNQDKLEQ FIRQFICS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 17689486] [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: 17013544] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY. Strain: C57BL/6. 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: 15449545] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Embryonic tail.
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] 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: 15489334] [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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 482-801. Strain: C57BL/6J. Tissue: Aorta and Vein.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00421026. IPI00889266. IPI00889271.
RefSeq	NP_001074558.1. NM_001081089.1.
UniGene	Mm.440454.
3D structure databases
ProteinModelPortal	Q14DK4.
ModBase	Search...
Protein-protein interaction databases
STRING	Q14DK4.
PTM databases
PhosphoSite	Q14DK4.
Proteomic databases
PRIDE	Q14DK4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000062211; ENSMUSP00000049619; ENSMUSG00000046338. ENSMUST00000110373; ENSMUSP00000106002; ENSMUSG00000046338.
GeneID	215456.
KEGG	mmu:215456.
UCSC	uc008mfj.1. mouse. uc012cdn.1. mouse.
Organism-specific databases
CTD	150763.
MGI	MGI:2684962. Gpat2.
Phylogenomic databases
GeneTree	ENSGT00520000055570.
HOGENOM	HBG403174.
InParanoid	Q14DK4.
OMA	QETSLWS.
OrthoDB	EOG4H9XK3.
Gene expression databases
ArrayExpress	Q14DK4.
Bgee	Q14DK4.
CleanEx	MM_A530057A03RIK.
Genevestigator	Q14DK4.
Family and domain databases
InterPro	IPR002123. Acyltransferase. [Graphical view]
KO	K00629.
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
SMART	SM00563. PlsC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

GPAT2_MOUSE

Accession

Primary (citable) accession number: Q14DK4
Secondary accession number(s): B1AW16 , Q0KK60, Q14CH8, Q6KAQ3, Q8BRZ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	May 5, 2009
Last modified:	November 16, 2011
This is version 48 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program