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Q8VDB2 (ALG12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. 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

Names and origin

Protein namesRecommended name:
Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase

EC=2.4.1.260
Alternative name(s):
Asparagine-linked glycosylation protein 12 homolog
Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase
Mannosyltransferase ALG12 homolog
Gene names
Name:Alg12
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man7GlcNAc2) required for protein glycosylation By similarity.

Catalytic activity

Dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the glycosyltransferase 22 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase
PRO_0000215782

Regions

Transmembrane12 – 3221Helical; Potential
Transmembrane69 – 8921Helical; Potential
Transmembrane94 – 11421Helical; Potential
Transmembrane123 – 14321Helical; Potential
Transmembrane146 – 16621Helical; Potential
Transmembrane178 – 19821Helical; Potential
Transmembrane213 – 23321Helical; Potential
Transmembrane265 – 28521Helical; Potential
Transmembrane291 – 31121Helical; Potential
Transmembrane313 – 33321Helical; Potential
Transmembrane344 – 36421Helical; Potential

Experimental info

Sequence conflict2451W → G in CAD22101. Ref.1
Sequence conflict476 – 48510LVLLERLLRP → AGTSRAAA in CAD22101. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8VDB2 [UniParc].

Last modified September 18, 2013. Version 2.
Checksum: 011C1DA60919D0A3

FASTA48654,543
        10         20         30         40         50         60 
MAGKKSSGKR SWPLLGLLVT VATIHLVICP YTKVEESFNL QATHDLLYHQ LDIDKYDHHE 

        70         80         90        100        110        120 
FPGVVPRTFL GPLVIAAFSS PVVYVLSLLE VSKFYSQLIV RGVLGLGVIS GLWTLQKEVR 

       130        140        150        160        170        180 
QQFGATVAVM FCWISATQFH LMFYCTRTLP NVLALAVVLP ALTAWLQRRW ALFVWLSAFV 

       190        200        210        220        230        240 
IIGFRAELAM LLGIALLLTL YQRRLTVARV LRHAIPAGLL CLGLTVAVDS YFWRYLVWPE 

       250        260        270        280        290        300 
GVVLWYNTVL NKSSNWGTSP LLWYFYSALP RGLGCSLLFI PLGAVDRRTY ALALPSLGFV 

       310        320        330        340        350        360 
ALYSLLPHKE LRFIIYTFPV LNIMAARGCT YILNKKSWPY KVRAMLVTGH ILVNVAYTAT 

       370        380        390        400        410        420 
SLYVSHFNYP GGVAMQQLHE LVPPQTDVLL HIDVAAAQTG VSRFLQVNDD WRYDKSEDVG 

       430        440        450        460        470        480 
AAAMLNYTHI LMEAVPGHPA LYRDTHRVLA SIEGTTGISL NLMKLPPFDV NLQTKLVLLE 


RLLRPA 

« Hide

References

« Hide 'large scale' references
[1]"Common origin and evolution of glycosyltransferases using Dol-P-monosaccharides as donor substrate."
Oriol R., Martinez-Duncker I., Chantret I., Mollicone R., Codogno P.
Mol. Biol. Evol. 19:1451-1463(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: FVB/N.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Heart.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ429133 mRNA. Translation: CAD22101.1.
AK142322 mRNA. Translation: BAE25031.1.
AC117700 Genomic DNA. No translation available.
RefSeqNP_001135829.1. NM_001142357.1.
NP_663452.1. NM_145477.2.
XP_006520905.1. XM_006520842.1.
UniGeneMm.41512.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT22. Glycosyltransferase Family 22.

PTM databases

PhosphoSiteQ8VDB2.

Proteomic databases

PaxDbQ8VDB2.
PRIDEQ8VDB2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000162183; ENSMUSP00000123935; ENSMUSG00000035845.
GeneID223774.
KEGGmmu:223774.
UCSCuc007xeo.2. mouse.

Organism-specific databases

CTD79087.
MGIMGI:2385025. Alg12.

Phylogenomic databases

eggNOGNOG256776.
GeneTreeENSGT00550000075005.
HOGENOMHOG000265945.
HOVERGENHBG050486.
InParanoidQ8VDB2.
KOK03847.
OMAFHLMFYS.
OrthoDBEOG7ZGX2X.
TreeFamTF314453.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

GenevestigatorQ8VDB2.

Family and domain databases

InterProIPR005599. GPI_mannosylTrfase.
[Graphical view]
PANTHERPTHR22760. PTHR22760. 1 hit.
PfamPF03901. Glyco_transf_22. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio376890.
PROQ8VDB2.
SOURCESearch...

Entry information

Entry nameALG12_MOUSE
AccessionPrimary (citable) accession number: Q8VDB2
Secondary accession number(s): Q3UQK8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: September 18, 2013
Last modified: April 16, 2014
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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