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Q8VDI9

- ALG9_MOUSE

UniProt

Q8VDI9 - ALG9_MOUSE

Protein

Alpha-1,2-mannosyltransferase ALG9

Gene

Alg9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of mannose from Dol-P-Man to lipid-linked oligosaccharides.By similarity

    Catalytic activityi

    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.

    Pathwayi

    GO - Molecular functioni

    1. dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity Source: UniProtKB-EC
    2. dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. protein glycosylation Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT22. Glycosyltransferase Family 22.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Alg9
    Synonyms:Dibd1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1924753. Alg9.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 611611Alpha-1,2-mannosyltransferase ALG9PRO_0000215788Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi77 – 771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi550 – 5501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi593 – 5931N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ8VDI9.
    PRIDEiQ8VDI9.

    PTM databases

    PhosphoSiteiQ8VDI9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8VDI9.
    BgeeiQ8VDI9.
    GenevestigatoriQ8VDI9.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VDI9.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 135135LumenalSequence AnalysisAdd
    BLAST
    Topological domaini157 – 17115CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini193 – 21321LumenalSequence AnalysisAdd
    BLAST
    Topological domaini235 – 24915CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini271 – 31040LumenalSequence AnalysisAdd
    BLAST
    Topological domaini332 – 34211CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini364 – 3707LumenalSequence Analysis
    Topological domaini392 – 40514CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini427 – 611185LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei136 – 15621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei172 – 19221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei214 – 23421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei250 – 27021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei311 – 33121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei343 – 36321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei371 – 39121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei406 – 42621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi12 – 2110Poly-Gly

    Sequence similaritiesi

    Belongs to the glycosyltransferase 22 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG278599.
    GeneTreeiENSGT00390000004731.
    HOGENOMiHOG000205434.
    HOVERGENiHBG062906.
    InParanoidiQ8VDI9.
    KOiK03846.
    OMAiISPLYIW.
    OrthoDBiEOG74TWZM.
    PhylomeDBiQ8VDI9.

    Family and domain databases

    InterProiIPR005599. GPI_mannosylTrfase.
    [Graphical view]
    PANTHERiPTHR22760. PTHR22760. 1 hit.
    PfamiPF03901. Glyco_transf_22. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8VDI9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASRRARQRL KGGGGGGGGG GDAGPAAEKL EQLGSREAGA EPRPESGNKA    50
    GQVWAPEGST AFKCLLSARL CAALLSNISD CDETFNYWEP THYLIYGKGF 100
    QTWEYSPVYA IRSYAYLLLH AWPAAFHARI LQTNKILVFY FLRCLLAFVS 150
    CVCELYFYKA VCKKFGLHVS RMMLAFLVLS TGMFCSSSAF LPSSFCMYTT 200
    LIAMTGWYMD KTPIAVLGVA AGAILGWPFS AALGLPIAFD LLARKHRWKS 250
    FLLWSLVALA LFLVPVVVID SYYYGKLVVA PLNIVLYNVF TSHGPDLYGT 300
    EPWYFYLING FLNFNVAFAL ALLVLPLTFL MEYLLQRFHV QNLGHPYWLT 350
    LAPMYIWFII FFIQPHKEER FLFPVYPLIC LCGAVALSAL QKCYHFVFQR 400
    YRLEHYTVTS NWLALGTVFL FGLLSFSRSV ALFRGYHGPL DLYPEFYRIA 450
    TDPTIHTVPE GRPVNVCVGK EWYRFPSSFL LPDNWQLQFI PSEFRGQLPK 500
    PFAEGPLATR TVPTHMNDQN REEPSRYIDI SKCHYLVDLD TMRETPREPN 550
    YSSHREEWVS LAHRPFLDAS RSSKLLRAFY VPFLSDQYTV YVNYTILKPR 600
    KAKPSRKKSG G 611
    Length:611
    Mass (Da):69,561
    Last modified:March 1, 2002 - v1
    Checksum:i3C96FFC7854F0133
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81Q → R in BAC34195. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS23175.1.
    RefSeqiNP_598742.1. NM_133981.2.
    UniGeneiMm.160035.

    Genome annotation databases

    EnsembliENSMUST00000034561; ENSMUSP00000034561; ENSMUSG00000032059.
    GeneIDi102580.
    KEGGimmu:102580.
    UCSCiuc009pkt.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS23175.1.
    RefSeqi NP_598742.1. NM_133981.2.
    UniGenei Mm.160035.

    3D structure databases

    ProteinModelPortali Q8VDI9.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GT22. Glycosyltransferase Family 22.

    PTM databases

    PhosphoSitei Q8VDI9.

    Proteomic databases

    PaxDbi Q8VDI9.
    PRIDEi Q8VDI9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034561 ; ENSMUSP00000034561 ; ENSMUSG00000032059 .
    GeneIDi 102580.
    KEGGi mmu:102580.
    UCSCi uc009pkt.2. mouse.

    Organism-specific databases

    CTDi 79796.
    MGIi MGI:1924753. Alg9.

    Phylogenomic databases

    eggNOGi NOG278599.
    GeneTreei ENSGT00390000004731.
    HOGENOMi HOG000205434.
    HOVERGENi HBG062906.
    InParanoidi Q8VDI9.
    KOi K03846.
    OMAi ISPLYIW.
    OrthoDBi EOG74TWZM.
    PhylomeDBi Q8VDI9.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    NextBioi 355542.
    PROi Q8VDI9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8VDI9.
    Bgeei Q8VDI9.
    Genevestigatori Q8VDI9.

    Family and domain databases

    InterProi IPR005599. GPI_mannosylTrfase.
    [Graphical view ]
    PANTHERi PTHR22760. PTHR22760. 1 hit.
    Pfami PF03901. Glyco_transf_22. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiALG9_MOUSE
    AccessioniPrimary (citable) accession number: Q8VDI9
    Secondary accession number(s): Q8BT44, Q8C378, Q8C7G0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3