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Protein

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

Gene

Alg12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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 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->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.

Pathwayi

GO - Molecular functioni

  1. dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase activity Source: UniProtKB-EC
  2. mannosyltransferase activity Source: GO_Central

GO - Biological processi

  1. dolichol-linked oligosaccharide biosynthetic process Source: MGI
  2. mannosylation Source: GOC
  3. protein N-linked glycosylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_320215. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT22. Glycosyltransferase Family 22.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Alg12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:2385025. Alg12.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3221HelicalSequence AnalysisAdd
BLAST
Transmembranei69 – 8921HelicalSequence AnalysisAdd
BLAST
Transmembranei94 – 11421HelicalSequence AnalysisAdd
BLAST
Transmembranei123 – 14321HelicalSequence AnalysisAdd
BLAST
Transmembranei146 – 16621HelicalSequence AnalysisAdd
BLAST
Transmembranei178 – 19821HelicalSequence AnalysisAdd
BLAST
Transmembranei213 – 23321HelicalSequence AnalysisAdd
BLAST
Transmembranei265 – 28521HelicalSequence AnalysisAdd
BLAST
Transmembranei291 – 31121HelicalSequence AnalysisAdd
BLAST
Transmembranei313 – 33321HelicalSequence AnalysisAdd
BLAST
Transmembranei344 – 36421HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: GO_Central
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferasePRO_0000215782Add
BLAST

Proteomic databases

MaxQBiQ8VDB2.
PaxDbiQ8VDB2.
PRIDEiQ8VDB2.

PTM databases

PhosphoSiteiQ8VDB2.

Expressioni

Gene expression databases

ExpressionAtlasiQ8VDB2. baseline and differential.
GenevestigatoriQ8VDB2.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 22 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG256776.
GeneTreeiENSGT00550000075005.
HOGENOMiHOG000265945.
HOVERGENiHBG050486.
InParanoidiQ8VDB2.
KOiK03847.
OMAiSYTHILM.
OrthoDBiEOG7ZGX2X.
TreeFamiTF314453.

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.

Q8VDB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGKKSSGKR SWPLLGLLVT VATIHLVICP YTKVEESFNL QATHDLLYHQ
60 70 80 90 100
LDIDKYDHHE FPGVVPRTFL GPLVIAAFSS PVVYVLSLLE VSKFYSQLIV
110 120 130 140 150
RGVLGLGVIS GLWTLQKEVR QQFGATVAVM FCWISATQFH LMFYCTRTLP
160 170 180 190 200
NVLALAVVLP ALTAWLQRRW ALFVWLSAFV IIGFRAELAM LLGIALLLTL
210 220 230 240 250
YQRRLTVARV LRHAIPAGLL CLGLTVAVDS YFWRYLVWPE GVVLWYNTVL
260 270 280 290 300
NKSSNWGTSP LLWYFYSALP RGLGCSLLFI PLGAVDRRTY ALALPSLGFV
310 320 330 340 350
ALYSLLPHKE LRFIIYTFPV LNIMAARGCT YILNKKSWPY KVRAMLVTGH
360 370 380 390 400
ILVNVAYTAT SLYVSHFNYP GGVAMQQLHE LVPPQTDVLL HIDVAAAQTG
410 420 430 440 450
VSRFLQVNDD WRYDKSEDVG AAAMLNYTHI LMEAVPGHPA LYRDTHRVLA
460 470 480
SIEGTTGISL NLMKLPPFDV NLQTKLVLLE RLLRPA
Length:486
Mass (Da):54,543
Last modified:September 18, 2013 - v2
Checksum:i011C1DA60919D0A3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti245 – 2451W → G in CAD22101 (PubMed:12200473).Curated
Sequence conflicti476 – 48510LVLLERLLRP → AGTSRAAA in CAD22101 (PubMed:12200473).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ429133 mRNA. Translation: CAD22101.1.
AK142322 mRNA. Translation: BAE25031.1.
AC117700 Genomic DNA. No translation available.
CCDSiCCDS49694.1.
RefSeqiNP_001135829.1. NM_001142357.1.
NP_663452.1. NM_145477.2.
XP_006520905.1. XM_006520842.2.
UniGeneiMm.41512.

Genome annotation databases

EnsembliENSMUST00000162183; ENSMUSP00000123935; ENSMUSG00000035845.
GeneIDi223774.
KEGGimmu:223774.
UCSCiuc007xeo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ429133 mRNA. Translation: CAD22101.1.
AK142322 mRNA. Translation: BAE25031.1.
AC117700 Genomic DNA. No translation available.
CCDSiCCDS49694.1.
RefSeqiNP_001135829.1. NM_001142357.1.
NP_663452.1. NM_145477.2.
XP_006520905.1. XM_006520842.2.
UniGeneiMm.41512.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT22. Glycosyltransferase Family 22.

PTM databases

PhosphoSiteiQ8VDB2.

Proteomic databases

MaxQBiQ8VDB2.
PaxDbiQ8VDB2.
PRIDEiQ8VDB2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000162183; ENSMUSP00000123935; ENSMUSG00000035845.
GeneIDi223774.
KEGGimmu:223774.
UCSCiuc007xeo.2. mouse.

Organism-specific databases

CTDi79087.
MGIiMGI:2385025. Alg12.

Phylogenomic databases

eggNOGiNOG256776.
GeneTreeiENSGT00550000075005.
HOGENOMiHOG000265945.
HOVERGENiHBG050486.
InParanoidiQ8VDB2.
KOiK03847.
OMAiSYTHILM.
OrthoDBiEOG7ZGX2X.
TreeFamiTF314453.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_320215. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

Miscellaneous databases

NextBioi376890.
PROiQ8VDB2.
SOURCEiSearch...

Gene expression databases

ExpressionAtlasiQ8VDB2. baseline and differential.
GenevestigatoriQ8VDB2.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiALG12_MOUSE
AccessioniPrimary (citable) accession number: Q8VDB2
Secondary accession number(s): Q3UQK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: September 18, 2013
Last modified: April 1, 2015
This is version 87 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.