Q86VF5 (MOGT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2-acylglycerol O-acyltransferase 3
EC=2.3.1.20
EC=2.3.1.22

Alternative name(s):
Acyl-CoA:monoacylglycerol acyltransferase 3
Short name=MGAT3
Diacylglycerol O-acyltransferase candidate 7
Short name=hDC7
Diacylglycerol acyltransferase 2-like protein 7
Monoacylglycerol O-acyltransferase 3

Gene names

Name:	MOGAT3
Synonyms:	DC7, DGAT2L7
ORF Names:	UNQ9383/PRO34208

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	341 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. Also able to catalyze the terminal step in triacylglycerol synthesis by using diacylglycerol and fatty acyl-CoA as substrates. Has a preference toward palmitoyl-CoA and oleoyl-CoA. May be involved in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. Ref.1
Catalytic activity	Acyl-CoA + 2-acylglycerol = CoA + diacylglycerol. Ref.1 Acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol. Ref.1
Pathway	Glycerolipid metabolism; triacylglycerol biosynthesis.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity Ref.1.
Tissue specificity	Selectively expressed in the digestive system. Highly expressed in the ileum, and at lower level in jejunum, duodenum, colon, cecum and the rectum. Not expressed in the stomach and the esophagus and trachea. Expressed at very low level in liver. Ref.1
Sequence similarities	Belongs to the diacylglycerol acyltransferase family.
Biophysicochemical properties	Kinetic parameters: Vmax=9.3 nmol/min/mg enzyme with diacylglycerol as substrate Ref.1 Vmax=22.8 nmol/min/mg enzyme with 2-monoacylglycerol as substrate
Sequence caution	The sequence AAD45832.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Glycerol metabolism Lipid metabolism Lipid synthesis
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glycerol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW lipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	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 diacylglycerol O-acyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q86VF5-1)

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: Q86VF5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     224-281: ASLVPVYSFG...LFSATSWGLL → GPPHPRPPAP...LHLGLAAAFR
     282-341: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q86VF5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     291-341: VGRPIPVPQR...VPASTCLTFI → GECPPPGGRP...RKSITITPST

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 341	341	2-acylglycerol O-acyltransferase 3		PRO_0000249067
Regions
	Transmembrane	29 – 49	21	Helical; Potential
	Transmembrane	50 – 70	21	Helical; Potential
	Transmembrane	137 – 157	21	Helical; Potential
Amino acid modifications
	Glycosylation	126	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	224 – 281	58	ASLVP…SWGLL → GPPHPRPPAPPPHRGGSQSL SRPLHDGPGAALRGAQGKLW GPRFHLPHLHLGLAAAFR in isoform 2.		VSP_020361
	Alternative sequence	282 – 341	60	Missing in isoform 2.		VSP_020362
	Alternative sequence	291 – 341	51	VGRPI…CLTFI → GECPPPGGRPPAAAWASGIP RPPVSLSLQWAAPSPSPSAS TPPRRKSITITPST in isoform 3.		VSP_020363
Experimental info
	Sequence conflict	265	1	C → Y in AAI00954. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 3F4981AE0D05B613	FASTA	341	38,730
	10 20 30 40 50 60 MGVATTLQPP TTSKTLQKQH LEAVGAYQYV LTFLFMGPFF SLLVFVLLFT SLWPFSVFYL 70 80 90 100 110 120 VWLYVDWDTP NQGGRRSEWI RNRAIWRQLR DYYPVKLVKT AELPPDRNYV LGAHPHGIMC 130 140 150 160 170 180 TGFLCNFSTE SNGFSQLFPG LRPWLAVLAG LFYLPVYRDY IMSFGLCPVS RQSLDFILSQ 190 200 210 220 230 240 PQLGQAVVIM VGGAHEALYS VPGEHCLTLQ KRKGFVRLAL RHGASLVPVY SFGENDIFRL 250 260 270 280 290 300 KAFATGSWQH WCQLTFKKLM GFSPCIFWGR GLFSATSWGL LPFAVPITTV VGRPIPVPQR 310 320 330 340 LHPTEEEVNH YHALYMTALE QLFEEHKESC GVPASTCLTF I
	Isoform 2 [UniParc]. Checksum: D1D0C8B2EF0D3992	FASTA	281	31,498
	10 20 30 40 50 60 MGVATTLQPP TTSKTLQKQH LEAVGAYQYV LTFLFMGPFF SLLVFVLLFT SLWPFSVFYL 70 80 90 100 110 120 VWLYVDWDTP NQGGRRSEWI RNRAIWRQLR DYYPVKLVKT AELPPDRNYV LGAHPHGIMC 130 140 150 160 170 180 TGFLCNFSTE SNGFSQLFPG LRPWLAVLAG LFYLPVYRDY IMSFGLCPVS RQSLDFILSQ 190 200 210 220 230 240 PQLGQAVVIM VGGAHEALYS VPGEHCLTLQ KRKGFVRLAL RHGGPPHPRP PAPPPHRGGS 250 260 270 280 QSLSRPLHDG PGAALRGAQG KLWGPRFHLP HLHLGLAAAF R
	Isoform 3 [UniParc]. Checksum: 3836BCF9E68C500C	FASTA	344	38,353
	10 20 30 40 50 60 MGVATTLQPP TTSKTLQKQH LEAVGAYQYV LTFLFMGPFF SLLVFVLLFT SLWPFSVFYL 70 80 90 100 110 120 VWLYVDWDTP NQGGRRSEWI RNRAIWRQLR DYYPVKLVKT AELPPDRNYV LGAHPHGIMC 130 140 150 160 170 180 TGFLCNFSTE SNGFSQLFPG LRPWLAVLAG LFYLPVYRDY IMSFGLCPVS RQSLDFILSQ 190 200 210 220 230 240 PQLGQAVVIM VGGAHEALYS VPGEHCLTLQ KRKGFVRLAL RHGASLVPVY SFGENDIFRL 250 260 270 280 290 300 KAFATGSWQH WCQLTFKKLM GFSPCIFWGR GLFSATSWGL LPFAVPITTV GECPPPGGRP 310 320 330 340 PAAAWASGIP RPPVSLSLQW AAPSPSPSAS TPPRRKSITI TPST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of acyl coenzyme A:monoacylglycerol acyltransferase 3, an intestinal specific enzyme implicated in dietary fat absorption." Cheng D., Nelson T.C., Chen J., Walker S.G., Wardwell-Swanson J., Meegalla R., Taub R., Billheimer J.T., Ramaker M., Feder J.N. J. Biol. Chem. 278:13611-13614(2003) [PubMed: 12618427] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY229854 mRNA. Translation: AAO63579.1. AY358200 mRNA. Translation: AAQ88567.1. AC004876 Genomic DNA. Translation: AAD45832.1. Sequence problems. BC100953 mRNA. Translation: AAI00954.1. BC100954 mRNA. Translation: AAI00955.1. BC100955 mRNA. Translation: AAI00956.1.
IPI	IPI00328886. IPI00645251. IPI00784889.
RefSeq	NP_835470.1. NM_178176.2.
UniGene	Hs.512217.
3D structure databases
ProteinModelPortal	Q86VF5.
ModBase	Search...
Protein-protein interaction databases
STRING	Q86VF5.
Polymorphism databases
DMDM	74727570.
Proteomic databases
PRIDE	Q86VF5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000223114; ENSP00000223114; ENSG00000106384.
GeneID	346606.
KEGG	hsa:346606.
UCSC	uc003uyc.1. human. uc010lhr.1. human.
Organism-specific databases
CTD	346606.
GeneCards	GC07M100838.
H-InvDB	HIX0201187.
HGNC	HGNC:23249. MOGAT3.
HPA	HPA011940.
MIM	610184. gene.
neXtProt	NX_Q86VF5.
PharmGKB	PA134959238.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG12071.
GeneTree	ENSGT00550000074276.
HOVERGEN	HBG065791.
InParanoid	Q86VF5.
OMA	RRKSITI.
OrthoDB	EOG408N8B.
PhylomeDB	Q86VF5.
Enzyme and pathway databases
BRENDA	2.3.1.22. 2681.
Gene expression databases
ArrayExpress	Q86VF5.
Bgee	Q86VF5.
CleanEx	HS_MOGAT3.
Genevestigator	Q86VF5.
GermOnline	ENSG00000106384. Homo sapiens.
Family and domain databases
InterPro	IPR007130. DAGAT. [Graphical view]
KO	K14456.
PANTHER	PTHR12317. DAGAT. 1 hit.
Pfam	PF03982. DAGAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	98991.
SOURCE	Search...

Entry information

Entry name

MOGT3_HUMAN

Accession

Primary (citable) accession number: Q86VF5
Secondary accession number(s): Q496A6 , Q496A7, Q496A8, Q9UDW7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 64 of the entry and version 1 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.