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Q8VDI9 (ALG9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. 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-1,2-mannosyltransferase ALG9
EC=2.4.1.259
EC=2.4.1.261
Alternative name(s):
Asparagine-linked glycosylation protein 9 homolog
Disrupted in bipolar disorder protein 1 homolog
Dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase
Dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase
Gene names
Name:Alg9
Synonyms:Dibd1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length611 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the transfer of mannose from Dol-P-Man to lipid-linked oligosaccharides 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->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-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.

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-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->2)-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 caution

The sequence BAC39717.1 differs from that shown. Reason: Frameshift at position 546.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 611611Alpha-1,2-mannosyltransferase ALG9
PRO_0000215788

Regions

Topological domain1 – 135135Lumenal Potential
Transmembrane136 – 15621Helical; Potential
Topological domain157 – 17115Cytoplasmic Potential
Transmembrane172 – 19221Helical; Potential
Topological domain193 – 21321Lumenal Potential
Transmembrane214 – 23421Helical; Potential
Topological domain235 – 24915Cytoplasmic Potential
Transmembrane250 – 27021Helical; Potential
Topological domain271 – 31040Lumenal Potential
Transmembrane311 – 33121Helical; Potential
Topological domain332 – 34211Cytoplasmic Potential
Transmembrane343 – 36321Helical; Potential
Topological domain364 – 3707Lumenal Potential
Transmembrane371 – 39121Helical; Potential
Topological domain392 – 40514Cytoplasmic Potential
Transmembrane406 – 42621Helical; Potential
Topological domain427 – 611185Lumenal Potential
Compositional bias12 – 2110Poly-Gly

Amino acid modifications

Glycosylation771N-linked (GlcNAc...) Potential
Glycosylation5501N-linked (GlcNAc...) Potential
Glycosylation5931N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict81Q → R in BAC34195. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8VDI9 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 3C96FFC7854F0133

FASTA61169,561
        10         20         30         40         50         60 
MASRRARQRL KGGGGGGGGG GDAGPAAEKL EQLGSREAGA EPRPESGNKA GQVWAPEGST 

        70         80         90        100        110        120 
AFKCLLSARL CAALLSNISD CDETFNYWEP THYLIYGKGF QTWEYSPVYA IRSYAYLLLH 

       130        140        150        160        170        180 
AWPAAFHARI LQTNKILVFY FLRCLLAFVS CVCELYFYKA VCKKFGLHVS RMMLAFLVLS 

       190        200        210        220        230        240 
TGMFCSSSAF LPSSFCMYTT LIAMTGWYMD KTPIAVLGVA AGAILGWPFS AALGLPIAFD 

       250        260        270        280        290        300 
LLARKHRWKS FLLWSLVALA LFLVPVVVID SYYYGKLVVA PLNIVLYNVF TSHGPDLYGT 

       310        320        330        340        350        360 
EPWYFYLING FLNFNVAFAL ALLVLPLTFL MEYLLQRFHV QNLGHPYWLT LAPMYIWFII 

       370        380        390        400        410        420 
FFIQPHKEER FLFPVYPLIC LCGAVALSAL QKCYHFVFQR YRLEHYTVTS NWLALGTVFL 

       430        440        450        460        470        480 
FGLLSFSRSV ALFRGYHGPL DLYPEFYRIA TDPTIHTVPE GRPVNVCVGK EWYRFPSSFL 

       490        500        510        520        530        540 
LPDNWQLQFI PSEFRGQLPK PFAEGPLATR TVPTHMNDQN REEPSRYIDI SKCHYLVDLD 

       550        560        570        580        590        600 
TMRETPREPN YSSHREEWVS LAHRPFLDAS RSSKLLRAFY VPFLSDQYTV YVNYTILKPR 

       610 
KAKPSRKKSG G

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo, Head, Liver and Ovary.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK020231 mRNA. Translation: BAC25619.1.
AK050335 mRNA. Translation: BAC34195.1.
AK054293 mRNA. Translation: BAC35720.1.
AK086674 mRNA. Translation: BAC39717.1. Frameshift.
BC021791 mRNA. Translation: AAH21791.1.
IPIIPI00459582.
RefSeqNP_598742.1. NM_133981.2.
UniGeneMm.160035.

3D structure databases

ProteinModelPortalQ8VDI9.
ModBaseSearch...

Protein family/group databases

CAZyGT22. Glycosyltransferase Family 22.

PTM databases

PhosphoSiteQ8VDI9.

Proteomic databases

PaxDbQ8VDI9.
PRIDEQ8VDI9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034561; ENSMUSP00000034561; ENSMUSG00000032059.
GeneID102580.
KEGGmmu:102580.
UCSCuc009pkt.1. mouse.

Organism-specific databases

CTD79796.
MGIMGI:1924753. Alg9.

Phylogenomic databases

eggNOGNOG278599.
GeneTreeENSGT00390000004731.
HOGENOMHOG000205434.
HOVERGENHBG062906.
InParanoidQ8VDI9.
KOK03846.
OMAHYLIYGE.
OrthoDBEOG4GB75G.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ8VDI9.
BgeeQ8VDI9.
GenevestigatorQ8VDI9.
GermOnlineENSMUSG00000032059. Mus musculus.

Family and domain databases

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

Other

NextBio355542.
SOURCESearch...

Entry information

Entry nameALG9_MOUSE
AccessionPrimary (citable) accession number: Q8VDI9
Secondary accession number(s): Q8BT44, Q8C378, Q8C7G0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 1, 2002
Last modified: April 3, 2013
This is version 85 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents