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Q9VH78 (ALG12_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 74. 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:
Probable 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
ORF Names:CG8412
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length678 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 – 678678Probable Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase
PRO_0000215784

Regions

Transmembrane1 – 2121Helical; Potential
Transmembrane56 – 7621Helical; Potential
Transmembrane81 – 10121Helical; Potential
Transmembrane109 – 12921Helical; Potential
Transmembrane133 – 15321Helical; Potential
Transmembrane168 – 18821Helical; Potential
Transmembrane200 – 22021Helical; Potential
Transmembrane252 – 27221Helical; Potential
Transmembrane279 – 29921Helical; Potential
Transmembrane301 – 32121Helical; Potential
Transmembrane334 – 35421Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
Q9VH78 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 415BA0D1EF546013

FASTA67876,553
        10         20         30         40         50         60 
MDILIFVTAA AHLVYTPFTK VEESFNLQAM HDILYLRNNF TQYDHHDYPG VVPRTFIGPL 

        70         80         90        100        110        120 
VVSIISAPFV LLFETLSINK FWAQYVVRLV LAGAISVAWN SLRQAVTKIY GVEVRLWFTA 

       130        140        150        160        170        180 
ITITQFHFMF YMTRPLPNIF ALPIVLFAIA YWLRDQHKPF IICSGISILV FRSELALFLG 

       190        200        210        220        230        240 
ILLVVSLLRR KVSIDGLLKV ALPAGVCILA ATVLVDSFFW RRLLWPEGEV LWYNTVLNKS 

       250        260        270        280        290        300 
SNWGTSPFLW YFYSALPRAM GASLVLVPIG VALEPRIRPL VLSALLFVLL YSILPHKELR 

       310        320        330        340        350        360 
FIIYVFPVLN IAAACACQRI WMNSAKSTWH SFLALACGAH LLLNVFITLF LLVISGTNYP 

       370        380        390        400        410        420 
GGAALSRLHR LEAGTSNVSV HISNLAAQSG VSRFMEINNE WTYSKDETMN YTQADLVAYT 

       430        440        450        460        470        480 
HLLVEAKNKQ NTELWASLQN EFDTLEFIDC FNSIGIQYNS LLPVRIKTKP CIGILKKRPV 

       490        500        510        520        530        540 
APKEASKTKE KIAKTKTYPV EKETLLAPVK EFPKVIGDPK MKSRLQVDAD DDDGIVSTVE 

       550        560        570        580        590        600 
EMSLELETDT EPHAGAETIE TPLKEINFQE LRTLALGQAT KKSRAATKMK IRQIIEQHYR 

       610        620        630        640        650        660 
AKGKQIENDS AETQKTQGKA GLRQSVKSII KQEKIKEMIE QIATMDLTRI CDLERTSTKD 

       670 
CLKQVIDKID DSEGLKSK

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014297 Genomic DNA. Translation: AAF54441.1.
AY071132 mRNA. Translation: AAL48754.1.
RefSeqNP_649939.1. NM_141682.3.
UniGeneDm.6098.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ9VH78.

Protein family/group databases

CAZyGT22. Glycosyltransferase Family 22.

Proteomic databases

PRIDEQ9VH78.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0082130; FBpp0081608; FBgn0037743.
GeneID41191.
KEGGdme:Dmel_CG8412.
NMPDRfig|7227.3.peg.11963.
UCSCCG8412-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0037743. CG8412.

Phylogenomic databases

eggNOGinNOG09006.
GeneTreeEMGT00050000010281.
InParanoidQ9VH78.
OMATRICDLE.
OrthoDBEOG47SQVZ.
PhylomeDBQ9VH78.

Gene expression databases

BgeeQ9VH78.
GermOnlineCG8412. Drosophila melanogaster.

Family and domain databases

InterProIPR005599. GPI_mannosylTrfase.
[Graphical view]
KOK03847.
PANTHERPTHR22760. Alg9_trans. 1 hit.
PfamPF03901. Glyco_transf_22. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio822644.

Entry information

Entry nameALG12_DROME
AccessionPrimary (citable) accession number: Q9VH78
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

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