Reviewed, UniProtKB/Swiss-Prot Q09327 (MGAT3_HUMAN)

Names and origin

Protein names

Recommended name:
    Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
    EC=2.4.1.144
Alternative name(s):
    N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III
      Short name=N-acetylglucosaminyltransferase III
      Short name=GlcNAc-T III
      Short name=GNT-III

Gene names

Name:	MGAT3
Synonyms:	GGNT3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	533 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	It is involved in the regulation of the biosynthesis and biological function of glycoprotein oligosaccharides. Catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked sugar chains. It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides.
Catalytic activity	UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R = UDP + 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence similarities	Belongs to the glycosyltransferase 17 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid N-linked glycosylation Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Ref.1 Traceable author statement. Source: ProtInc
Molecular function	beta-1,4-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 533	533	Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase		PRO_0000188842
Regions
	Topological domain	1 – 7	7	Cytoplasmic Potential
	Transmembrane	8 – 23	16	Signal-anchor for type II membrane protein Potential
	Topological domain	24 – 533	510	Lumenal Potential
	Compositional bias	35 – 86	52	Pro-rich
Amino acid modifications
	Modified residue	261	1	Phosphothreonine By similarity
	Glycosylation	141	1	N-linked (GlcNAc...) Potential
	Glycosylation	241	1	N-linked (GlcNAc...) Potential
	Glycosylation	259	1	N-linked (GlcNAc...) Potential
	Glycosylation	397	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	346	1	K → T in BAA02937. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q09327-1 [UniParc]. Last modified March 15, 2005. Version 3. Checksum: 11F56C44A6B173AB	FASTA	533	61,313
	10 20 30 40 50 60 MKMRRYKLFL MFCMAGLCLI SFLHFFKTLS YVTFPRELAS LSPNLVSSFF WNNAPVTPQA 70 80 90 100 110 120 SPEPGGPDLL RTPLYSHSPL LQPLPPSKAA EELHRVDLVL PEDTTEYFVR TKAGGVCFKP 130 140 150 160 170 180 GTKMLERPPP GRPEEKPEGA NGSSARRPPR YLLSARERTG GRGARRKWVE CVCLPGWHGP 190 200 210 220 230 240 SCGVPTVVQY SNLPTKERLV PREVPRRVIN AINVNHEFDL LDVRFHELGD VVDAFVVCES 250 260 270 280 290 300 NFTAYGEPRP LKFREMLTNG TFEYIRHKVL YVFLDHFPPG GRQDGWIADD YLRTFLTQDG 310 320 330 340 350 360 VSRLRNLRPD DVFIIDDADE IPARDGVLFL KLYDGWTEPF AFHMRKSLYG FFWKQPGTLE 370 380 390 400 410 420 VVSGCTVDML QAVYGLDGIR LRRRQYYTMP NFRQYENRTG HILVQWSLGS PLHFAGWHCS 430 440 450 460 470 480 WCFTPEGIYF KLVSAQNGDF PRWGDYEDKR DLNYIRGLIR TGGWFDGTQQ EYPPADPSEH 490 500 510 520 530 MYAPKYLLKN YDRFHYLLDN PYQEPRSTAA GGWRHRGPEG RPPARGKLDE AEV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning, expression, and chromosomal localization of human N-acetylglucosaminyltransferase III (GnT-III)." Ihara Y., Nishikawa A., Toma T., Soejima H., Niikawa N., Taniguchi N. J. Biochem. 113:692-698(1993) [PubMed: 8370666] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [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]. Tissue: Cerebellum and Fetal brain.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase

Cross-references

Sequence databases
EMBL GenBank DDBJ	D13789 mRNA. Translation: BAA02937.1. Different initiation. CR456519 mRNA. Translation: CAG30405.1. AL022312 Genomic DNA. Translation: CAI19177.1. BC075025 mRNA. Translation: AAH75025.1. BC075026 mRNA. Translation: AAH75026.1. BC113383 mRNA. Translation: AAI13384.1. BC113718 mRNA. Translation: AAI13719.1.
IPI	IPI00020406.
PIR	JN0586.
RefSeq	NP_001091740.1. NP_002400.3.
UniGene	Hs.276808
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q09327.
Protein family/group databases
CAZy	GT17. Glycosyltransferase Family 17.
PTM databases
PhosphoSite	Q09327.
Proteomic databases
PRIDE	Q09327.
Genome annotation databases
Ensembl	ENST00000341184; ENSP00000345270; ENSG00000128268; Homo sapiens. [Genome view]
GeneID	4248.
KEGG	hsa:4248.
UCSC	uc003axv.2. human.
Organism-specific databases
CTD	4248.
GeneCards	GC22P038177.
H-InvDB	HIX0041185.
HGNC	HGNC:7046. MGAT3.
HPA	HPA017598.
MIM	604621. gene.
PharmGKB	PA30781.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15132.
HOGENOM	HBG446579.
HOVERGEN	Q09327.
InParanoid	Q09327.
OMA	LHFAGWH.
OrthoDB	EOG9N5ZH7.
Enzyme and pathway databases
BRENDA	2.4.1.144. 247.
Gene expression databases
ArrayExpress	Q09327.
Bgee	Q09327.
CleanEx	HS_MGAT3.
Genevestigator	Q09327.
GermOnline	ENSG00000128268. Homo sapiens.
Family and domain databases
InterPro	IPR006813. Glyco_trans_17. [Graphical view]
PANTHER	PTHR12224. Glyco_trans_17. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	16745.
SOURCE	Search...

Entry information

Entry name

MGAT3_HUMAN

Accession

Primary (citable) accession number: Q09327
Secondary accession number(s): A6NGD0 , Q14CK5, Q6IC49, Q9UH32

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	March 15, 2005
Last modified:	February 9, 2010
This is version 85 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.