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Reviewed, UniProtKB/Swiss-Prot Q812F8 (MGT4B_MOUSE)

Last modified December 15, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B
    EC=2.4.1.145
Alternative name(s):
    UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVb
    N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVb
      Short name=N-acetylglucosaminyltransferase IVb
      Short name=GlcNAc-T IVb
      Short name=GnT-IVb
Gene names
Name: Mgat4b
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N-linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains. Has lower affinities for donors or acceptors than MGAT4A, suggesting that, under physiological conditions, it is not the main contributor in N-glycan biosynthesis By similarity.

Catalytic activity

UDP-N-acetyl-D-glucosamine + 3-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 3-(2,4-bis(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R.

Cofactor

Divalent metal cations By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Sequence similarities

Belongs to the glycosyltransferase 54 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 548548Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B
PRO_0000288594

Regions

Topological domain1 – 77Cytoplasmic Potential
Transmembrane8 – 2821Signal-anchor for type II membrane protein Potential
Topological domain29 – 548520Lumenal Potential
Coiled coil36 – 8348 Potential

Amino acid modifications

Glycosylation871N-linked (GlcNAc...) Potential
Glycosylation1031N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict395 – 3962EH → SY in BAC55019. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q812F8-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: A66F88F4A05FBF27

FASTA54863,302
        10         20         30         40         50         60 
MRLRNGTFLT LLLFCLCAFL SLSWYAALSG QKGDVVDIYQ REFLALRDRL HAAEQESLKR 

        70         80         90        100        110        120 
SKELNLVLEE IKRAVSERQA LRDGEGNRTW GRLTEDPRLK PWNVSHRHVL HLPTVFHHLP 

       130        140        150        160        170        180 
HLLAKESSLQ PAVRVGQGRT GVSVVMGIPS VRREVHSYLT DTLHSLISEL SPQEKEDSVI 

       190        200        210        220        230        240 
VVLIAETDPQ YTSAVTENIK ALFPTEIHSG LLEVISPSPH FYPDFSRLRE SFGDPKERVR 

       250        260        270        280        290        300 
WRTKQNLDYC FLMMYAQSKG IYYVQLEDDI VAKPNYLSTM KNFALQQPSE DWMILEFSQL 

       310        320        330        340        350        360 
GFIGKMFKSL DLSLIVEFIL MFYRDKPIDW LLDHILWVKV CNPEKDAKHC DRQKANLRIR 

       370        380        390        400        410        420 
FKPSLFQHVG THSSLAGKIQ KLKDKDFGKH ALRKEHVNPP AEVSTSLKTY QHFTLEKAYL 

       430        440        450        460        470        480 
REDFFWAFTP AAGDFIRFRF FQPLRLERFF FRSGNIEHPE DKLFNTSVEV LPFDNPQSEK 

       490        500        510        520        530        540 
EALQEGRSAT LRYPRSPDGY LQIGSFYKGV AEGEVDPAFG PLEALRLSIQ TDSPVWVILS 


EIFLKKAD 

« Hide

References

« Hide 'large scale' references
[1]"A novel second isoenzyme of the human UDP-N-acetylglucosamine:alpha1,3-D-mannoside beta1,4-N-acetylglucosaminyltransferase family: cDNA cloning, expression, and chromosomal assignment."
Yoshida A., Minowa M.T., Takamatsu S., Hara T., Ikenaga H., Takeuchi M.
Glycoconj. J. 15:1115-1123(1998) [PubMed: 10372966] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/SvJ.
[2]"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. expand/collapse author list , 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].
Strain: C57BL/6J.
[3]"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. expand/collapse author list , 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 1-495.
Strain: NOD.
[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] OF 208-548.
Strain: FVB/N.
Tissue: Colon.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB053218 mRNA. Translation: BAC55019.1.
AB053219 Genomic DNA. Translation: BAC55020.1.
AL627187 Genomic DNA. Translation: CAI25119.1.
AK155336 mRNA. Translation: BAE33202.1.
BC026638 mRNA. Translation: AAH26638.1. Different initiation.
BC031613 mRNA. Translation: AAH31613.1. Different initiation.
IPIIPI00336218.
RefSeqNP_666038.3.
UniGeneMm.86759

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ812F8.

Protein family/group databases

CAZyGT54. Glycosyltransferase Family 54.

PTM databases

PhosphoSiteQ812F8.

Proteomic databases

PRIDEQ812F8.

Genome annotation databases

EnsemblENSMUST00000041725; ENSMUSP00000043346; ENSMUSG00000036620; Mus musculus. [Genome view]
GeneID103534.
UCSCuc007iry.1. mouse.

Organism-specific databases

CTD103534.
MGIMGI:2143974. Mgat4b.

Phylogenomic databases

HOGENOMHBG506643.
HOVERGENQ812F8.
InParanoidQ812F8.
OMADINRTWS.
OrthoDBEOG95MQQW.

Enzyme and pathway databases

BRENDA2.4.1.145. 244.

Gene expression databases

ArrayExpressQ812F8.
BgeeQ812F8.
GenevestigatorQ812F8.

Family and domain databases

InterProIPR006759. Glyco_transf_54.
[Graphical view]
PANTHERPTHR12062. Glyco_transf_54. 1 hit.
PfamPF04666. Glyco_transf_54. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio355989.
SOURCESearch...

Entry information

Entry nameMGT4B_MOUSE
AccessionPrimary (citable) accession number: Q812F8
Secondary accession number(s): Q3U2D9, Q812F9, Q8R0L4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: June 1, 2003
Last modified: December 15, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents