Q3SYC2 (MOGT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2-acylglycerol O-acyltransferase 2
EC=2.3.1.22

Alternative name(s):
Acyl-CoA:monoacylglycerol acyltransferase 2
Short name=MGAT2
Short name=hMGAT2
Diacylglycerol O-acyltransferase candidate 5
Short name=hDC5
Diacylglycerol acyltransferase 2-like protein 5
Monoacylglycerol O-acyltransferase 2

Gene names

Name:	MOGAT2
Synonyms:	DC5, DGAT2L5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	334 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the formation of diacylglycerol from 2-monoacylglycerol and fatty acyl-CoA. Has a preference toward monoacylglycerols containing unsaturated fatty acids in an order of C18:3 > C18:2 > C18:1 > C18:0. Plays a central role in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. May play a role in diet-induced obesity. Ref.1
Catalytic activity	Acyl-CoA + 2-acylglycerol = CoA + diacylglycerol.
Enzyme regulation	Inhibited by oleic acid and sphingosine, while it is stimulated by phosphatidylcholine, phosphatidylserine and phosphatidic acid By similarity.
Pathway	Glycerolipid metabolism; triacylglycerol biosynthesis.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1.
Tissue specificity	Highly expressed in liver, small intestine, colon, stomach and kidney. Ref.1 Ref.5
Sequence similarities	Belongs to the diacylglycerol acyltransferase family.
Biophysicochemical properties	Kinetic parameters: KM=45 µM for sn-1-monooleoylglycerol Ref.1

Ontologies

Keywords
Biological process	Glycerol metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	diacylglycerol biosynthetic process Inferred from electronic annotation. Source: Compara glycerol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW intestinal absorption Inferred from electronic annotation. Source: Compara triglyceride biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	endoplasmic reticulum Inferred from direct assay PubMed 14966132. Source: MGI endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	2-acylglycerol O-acyltransferase activity Inferred from electronic annotation. Source: EC acetyltransferase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q3SYC2-1)

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: Q3SYC2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-82: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q3SYC2-3)

Also known as: MGAT2V; Trunc;

The sequence of this isoform differs from the canonical sequence as follows:
     218-284: APLVPIFSFG...PYRRPITTVV → YQASGKSTLG...PQRRLSDLRN
     285-334: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 334	334	2-acylglycerol O-acyltransferase 2		PRO_0000249062
Regions
	Transmembrane	23 – 37	15	Helical; Potential
	Transmembrane	38 – 59	22	Helical; Potential
	Transmembrane	103 – 123	21	Helical; Potential
Natural variations
	Alternative sequence	1 – 82	82	Missing in isoform 2.		VSP_020358
	Alternative sequence	218 – 284	67	APLVP…ITTVV → YQASGKSTLGSVGNWQGFYF GGKMAETNADSILVEIFSPF TIKIIFWCLMPKYLEKFPQR RLSDLRN in isoform 3.		VSP_020359
	Alternative sequence	285 – 334	50	Missing in isoform 3.		VSP_020360
	Natural variant	9	1	M → V. Ref.4 Corresponds to variant rs554202 [ dbSNP | Ensembl ].		VAR_027390
	Natural variant	196	1	P → H. Corresponds to variant rs34582952 [ dbSNP | Ensembl ].		VAR_048857
	Natural variant	313	1	C → Y. Corresponds to variant rs12281468 [ dbSNP | Ensembl ].		VAR_027391
Experimental info
	Sequence conflict	142	1	L → P in BAB15436. Ref.2
	Sequence conflict	267	1	F → L in BAC87534. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 5, 2006. Version 2. Checksum: 57C4A964BAFA76BD	FASTA	334	38,196
	10 20 30 40 50 60 MVEFAPLFMP WERRLQTLAV LQFVFSFLAL AEICTVGFIA LLFTRFWLLT VLYAAWWYLD 70 80 90 100 110 120 RDKPRQGGRH IQAIRCWTIW KYMKDYFPIS LVKTAELDPS RNYIAGFHPH GVLAVGAFAN 130 140 150 160 170 180 LCTESTGFSS IFPGIRPHLM MLTLWFRAPF FRDYIMSAGL VTSEKESAAH ILNRKGGGNL 190 200 210 220 230 240 LGIIVGGAQE ALDARPGSFT LLLRNRKGFV RLALTHGAPL VPIFSFGEND LFDQIPNSSG 250 260 270 280 290 300 SWLRYIQNRL QKIMGISLPL FHGRGVFQYS FGLIPYRRPI TTVVGKPIEV QKTLHPSEEE 310 320 330 VNQLHQRYIK ELCNLFEAHK LKFNIPADQH LEFC
	Isoform 2 [UniParc]. Checksum: 902B6B67B2E8CC02	FASTA	252	28,283
	10 20 30 40 50 60 MKDYFPISLV KTAELDPSRN YIAGFHPHGV LAVGAFANLC TESTGFSSIF PGIRPHLMML 70 80 90 100 110 120 TLWFRAPFFR DYIMSAGLVT SEKESAAHIL NRKGGGNLLG IIVGGAQEAL DARPGSFTLL 130 140 150 160 170 180 LRNRKGFVRL ALTHGAPLVP IFSFGENDLF DQIPNSSGSW LRYIQNRLQK IMGISLPLFH 190 200 210 220 230 240 GRGVFQYSFG LIPYRRPITT VVGKPIEVQK TLHPSEEEVN QLHQRYIKEL CNLFEAHKLK 250 FNIPADQHLE FC
	Isoform 3 (MGAT2V) (Trunc) [UniParc]. Checksum: E56F74332AF8D2DE	FASTA	284	32,298
	10 20 30 40 50 60 MVEFAPLFMP WERRLQTLAV LQFVFSFLAL AEICTVGFIA LLFTRFWLLT VLYAAWWYLD 70 80 90 100 110 120 RDKPRQGGRH IQAIRCWTIW KYMKDYFPIS LVKTAELDPS RNYIAGFHPH GVLAVGAFAN 130 140 150 160 170 180 LCTESTGFSS IFPGIRPHLM MLTLWFRAPF FRDYIMSAGL VTSEKESAAH ILNRKGGGNL 190 200 210 220 230 240 LGIIVGGAQE ALDARPGSFT LLLRNRKGFV RLALTHGYQA SGKSTLGSVG NWQGFYFGGK 250 260 270 280 MAETNADSIL VEIFSPFTIK IIFWCLMPKY LEKFPQRRLS DLRN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MGAT2, a monoacylglycerol acyltransferase expressed in the small intestine." Yen C.-L.E., Farese R.V. Jr. J. Biol. Chem. 278:18532-18537(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY. Tissue: Intestine.
[2]	"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] (ISOFORMS 1 AND 2). Tissue: Small intestine and Trachea.
[3]	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. , 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].
[4]	"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 3), VARIANT VAL-9.
[5]	"Human intestinal monoacylglycerol acyltransferase: differential features in tissue expression and activity." Lockwood J.F., Cao J., Burn P., Shi Y. Am. J. Physiol. 285:E927-E937(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY157608 mRNA. Translation: AAO23672.1. AK026297 mRNA. Translation: BAB15436.1. AK128620 mRNA. Translation: BAC87534.1. AK291998 mRNA. Translation: BAF84687.1. CH471076 Genomic DNA. Translation: EAW74983.1. BC103876 mRNA. Translation: AAI03877.1. BC103877 mRNA. Translation: AAI03878.1. BC103878 mRNA. Translation: AAI03879.1.
IPI	IPI00328730. IPI00785156. IPI00785203.
RefSeq	NP_079374.2. NM_025098.2.
UniGene	Hs.288568.
3D structure databases
ProteinModelPortal	Q3SYC2.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000198801.
Polymorphism databases
DMDM	114150036.
Proteomic databases
PaxDb	Q3SYC2.
PRIDE	Q3SYC2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000198801; ENSP00000198801; ENSG00000166391. ENST00000525093; ENSP00000436537; ENSG00000166391. ENST00000526712; ENSP00000436283; ENSG00000166391.
GeneID	80168.
KEGG	hsa:80168.
UCSC	uc001oww.1. human. uc010rru.2. human.
Organism-specific databases
CTD	80168.
GeneCards	GC11P075428.
HGNC	HGNC:23248. MOGAT2.
HPA	HPA028834.
MIM	610270. gene.
neXtProt	NX_Q3SYC2.
PharmGKB	PA134936582.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG258143.
HOGENOM	HOG000179738.
HOVERGEN	HBG065791.
InParanoid	Q3SYC2.
KO	K14457.
OMA	QLHQRYI.
OrthoDB	EOG4BP1C4.
PhylomeDB	Q3SYC2.
Enzyme and pathway databases
UniPathway	UPA00282.
Gene expression databases
Bgee	Q3SYC2.
CleanEx	HS_MOGAT2.
Genevestigator	Q3SYC2.
GermOnline	ENSG00000166391. Homo sapiens.
Family and domain databases
InterPro	IPR007130. DAGAT. [Graphical view]
PANTHER	PTHR12317. PTHR12317. 1 hit.
Pfam	PF03982. DAGAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	80168.
NextBio	70479.
SOURCE	Search...

Entry information

Entry name

MOGT2_HUMAN

Accession

Primary (citable) accession number: Q3SYC2
Secondary accession number(s): A8K7I3 , Q3SYC1, Q6ZQZ2, Q86UH6, Q9H630

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	September 5, 2006
Last modified:	April 3, 2013
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.