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Q9D306 (MGT4C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase C
EC=2.4.1.145
Alternative name(s):
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVc
Short name=GnT-IVc
Short name=N-acetylglucosaminyltransferase IVc
UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVc
Gene names
Name:Mgat4c
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
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. Does not catalyze the transfer of GlcNAc to the Manalpha1-6 arm to form GlcNAcBeta1-4Manalpha1-6 linkage ('GnT-VI' activity) 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 – 478478Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase C
PRO_0000288598

Regions

Topological domain1 – 2525Cytoplasmic Potential
Transmembrane26 – 4318Helical; Signal-anchor for type II membrane protein; Potential
Topological domain44 – 478435Lumenal Potential

Amino acid modifications

Glycosylation841N-linked (GlcNAc...) Potential
Glycosylation2151N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9D306 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: EC8EC991A802F1BC

FASTA47856,250
        10         20         30         40         50         60 
MLKFYQMKYI FQILDKMRCL RKRSTVSFLG VLVVFLLFMN LYIEDSYVLE GDKQLIRETS 

        70         80         90        100        110        120 
THQLNSERYV HTFKDLSNFS GTINVTYRYL AATPLQRKRY LTIGLSSVKR KKGNYLLDTI 

       130        140        150        160        170        180 
KSIFEQSSYE ELKEISVVVH LADFNSSWRD AMVQDITQKF AHHIIAGRLM VIHAPEEYYP 

       190        200        210        220        230        240 
VLDGLKRNYN DPEDRVRFRS KQNVDYAFLL NFCANTSDYY VMLEDDVRCS RNFLTAIKKV 

       250        260        270        280        290        300 
IASLEGTYWV TLEFSKLGYI GKLYHSHDLP RLAHFLLMFY QEMPCDWLLT HFRGLLAQKN 

       310        320        330        340        350        360 
VIRFKPSLFQ HMGYYSSYKG TENKLKDDDF EEESFDIPDN PPASFYTNMN VFENYEASKA 

       370        380        390        400        410        420 
YSSVDEYFWG KSPSMGDTFV IVFENPITIK KIKVNTGTED RQNDILQHGA LDVGEKLIFS 

       430        440        450        460        470 
KQIRQCDTYL RLGEFKNGYF EMSDVNQKIP FDIHCMRICV TKTQKEWLII RSISIWTS

« Hide

References

[1]"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].
Strain: C57BL/6J.
Tissue: Cecum and Colon.
[2]"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].
Strain: FVB/N.
Tissue: Colon.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK018574 mRNA. Translation: BAB31286.1.
AK018672 mRNA. Translation: BAB31336.1.
AK033482 mRNA. Translation: BAC28312.1.
BC046987 mRNA. Translation: AAH46987.1.
IPIIPI00387409.
RefSeqNP_001155840.1. NM_001162368.1.
NP_001155841.1. NM_001162369.1.
NP_001192027.1. NM_001205098.1.
NP_080519.2. NM_026243.4.
UniGeneMm.25252.
Mm.403713.

3D structure databases

ProteinModelPortalQ9D306.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9D306.

Protein family/group databases

CAZyGT54. Glycosyltransferase Family 54.

PTM databases

PhosphoSiteQ9D306.

Proteomic databases

PRIDEQ9D306.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020039; ENSMUSP00000020039; ENSMUSG00000019888.
ENSMUST00000120748; ENSMUSP00000114010; ENSMUSG00000019888.
ENSMUST00000163753; ENSMUSP00000131551; ENSMUSG00000019888.
GeneID67569.
KEGGmmu:67569.
UCSCuc007gyc.2. mouse.

Organism-specific databases

CTD25834.
MGIMGI:1914819. Mgat4c.

Phylogenomic databases

GeneTreeENSGT00550000074578.
HOGENOMHBG444742.
HOVERGENHBG103174.
InParanoidQ9D306.
OMADVRCSKN.
PhylomeDBQ9D306.

Gene expression databases

ArrayExpressQ9D306.
BgeeQ9D306.
GenevestigatorQ9D306.

Family and domain databases

InterProIPR006759. Glyco_transf_54.
[Graphical view]
KOK13748.
PANTHERPTHR12062. Glyco_transf_54. 1 hit.
PfamPF04666. Glyco_transf_54. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio324937.
SOURCESearch...

Entry information

Entry nameMGT4C_MOUSE
AccessionPrimary (citable) accession number: Q9D306
Secondary accession number(s): Q9D2X2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: June 1, 2001
Last modified: November 16, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

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