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Protein

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

Gene

ALG12

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.2 Publications

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.1 Publication

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

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

GO - Biological processi

  • dolichol-linked oligosaccharide biosynthetic process Source: SGD
  • mannosylation Source: GOC
  • protein glycosylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-7190.
YEAST:MONOMER3O-256.
BRENDAi2.4.1.260. 984.
ReactomeiR-SCE-446193. 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
Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase
Extracellular mutant protein 39
Mannosyltransferase ALG12
Gene namesi
Name:ALG12
Synonyms:ECM39
Ordered Locus Names:YNR030W
ORF Names:N3265
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNR030W.
SGDiS000005313. ALG12.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 22LumenalSequence analysis
Transmembranei3 – 2321HelicalSequence analysisAdd
BLAST
Topological domaini24 – 6138CytoplasmicSequence analysisAdd
BLAST
Transmembranei62 – 8221HelicalSequence analysisAdd
BLAST
Topological domaini83 – 897LumenalSequence analysis
Transmembranei90 – 11021HelicalSequence analysisAdd
BLAST
Topological domaini111 – 13626CytoplasmicSequence analysisAdd
BLAST
Transmembranei137 – 15721HelicalSequence analysisAdd
BLAST
Topological domaini158 – 17821LumenalSequence analysisAdd
BLAST
Transmembranei179 – 19921HelicalSequence analysisAdd
BLAST
Topological domaini200 – 2023CytoplasmicSequence analysis
Transmembranei203 – 22321HelicalSequence analysisAdd
BLAST
Topological domaini224 – 2274LumenalSequence analysis
Transmembranei228 – 24821HelicalSequence analysisAdd
BLAST
Topological domaini249 – 27527CytoplasmicSequence analysisAdd
BLAST
Transmembranei276 – 29621HelicalSequence analysisAdd
BLAST
Topological domaini297 – 3037LumenalSequence analysis
Transmembranei304 – 32421HelicalSequence analysisAdd
BLAST
Topological domaini325 – 3317CytoplasmicSequence analysis
Transmembranei332 – 35221HelicalSequence analysisAdd
BLAST
Topological domaini353 – 36513LumenalSequence analysisAdd
BLAST
Transmembranei366 – 38621HelicalSequence analysisAdd
BLAST
Topological domaini387 – 41731CytoplasmicSequence analysisAdd
BLAST
Transmembranei418 – 43821HelicalSequence analysisAdd
BLAST
Topological domaini439 – 551113LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 551551Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferasePRO_0000215786Add
BLAST

Proteomic databases

MaxQBiP53730.
PeptideAtlasiP53730.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC155Q8N6L03EBI-28496,EBI-749265From a different organism.

Protein-protein interaction databases

BioGridi35854. 78 interactions.
DIPiDIP-4259N.
IntActiP53730. 23 interactions.
MINTiMINT-478020.

Structurei

3D structure databases

ProteinModelPortaliP53730.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 22 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00550000075005.
HOGENOMiHOG000248044.
InParanoidiP53730.
KOiK03847.
OMAiFRLEVGL.
OrthoDBiEOG786HC2.

Family and domain databases

InterProiIPR005599. GPI_mannosylTrfase.
[Graphical view]
PANTHERiPTHR22760. PTHR22760. 2 hits.
PfamiPF03901. Glyco_transf_22. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53730-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRWSVLDTVL LTVISFHLIQ APFTKVEESF NIQAIHDILT YSVFDISQYD
60 70 80 90 100
HLKFPGVVPR TFVGAVIIAM LSRPYLYLSS LIQTSRPTSI DVQLVVRGIV
110 120 130 140 150
GLTNGLSFIY LKNCLQDMFD EITEKKKEEN EDKDIYIYDS AGTWFLLFLI
160 170 180 190 200
GSFHLMFYST RTLPNFVMTL PLTNVALGWV LLGRYNAAIF LSALVAIVFR
210 220 230 240 250
LEVSALSAGI ALFSVIFKKI SLFDAIKFGI FGLGLGSAIS ITVDSYFWQE
260 270 280 290 300
WCLPEVDGFL FNVVAGYASK WGVEPVTAYF THYLRMMFMP PTVLLLNYFG
310 320 330 340 350
YKLAPAKLKI VSLASLFHII VLSFQPHKEW RFIIYAVPSI MLLGATGAAH
360 370 380 390 400
LWENMKVKKI TNVLCLAILP LSIMTSFFIS MAFLYISRMN YPGGEALTSF
410 420 430 440 450
NDMIVEKNIT NATVHISIPP CMTGVTLFGE LNYGVYGINY DKTENTTLLQ
460 470 480 490 500
EMWPSFDFLI THEPTASQLP FENKTTNHWE LVNTTKMFTG FDPTYIKNFV
510 520 530 540 550
FQERVNVLSL LKQIIFDKTP TVFLKELTAN SIVKSDVFFT YKRIKQDEKT

D
Length:551
Mass (Da):62,672
Last modified:October 1, 1996 - v1
Checksum:iB08A94BBF260502F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71645 Genomic DNA. Translation: CAA96310.1.
AY692956 Genomic DNA. Translation: AAT92975.1.
BK006947 Genomic DNA. Translation: DAA10570.1.
PIRiS63361.
RefSeqiNP_014427.1. NM_001183207.1.

Genome annotation databases

EnsemblFungiiYNR030W; YNR030W; YNR030W.
GeneIDi855764.
KEGGisce:YNR030W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71645 Genomic DNA. Translation: CAA96310.1.
AY692956 Genomic DNA. Translation: AAT92975.1.
BK006947 Genomic DNA. Translation: DAA10570.1.
PIRiS63361.
RefSeqiNP_014427.1. NM_001183207.1.

3D structure databases

ProteinModelPortaliP53730.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35854. 78 interactions.
DIPiDIP-4259N.
IntActiP53730. 23 interactions.
MINTiMINT-478020.

Protein family/group databases

CAZyiGT22. Glycosyltransferase Family 22.

Proteomic databases

MaxQBiP53730.
PeptideAtlasiP53730.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNR030W; YNR030W; YNR030W.
GeneIDi855764.
KEGGisce:YNR030W.

Organism-specific databases

EuPathDBiFungiDB:YNR030W.
SGDiS000005313. ALG12.

Phylogenomic databases

GeneTreeiENSGT00550000075005.
HOGENOMiHOG000248044.
InParanoidiP53730.
KOiK03847.
OMAiFRLEVGL.
OrthoDBiEOG786HC2.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciMetaCyc:MONOMER-7190.
YEAST:MONOMER3O-256.
BRENDAi2.4.1.260. 984.
ReactomeiR-SCE-446193. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

Miscellaneous databases

PROiP53730.

Family and domain databases

InterProiIPR005599. GPI_mannosylTrfase.
[Graphical view]
PANTHERiPTHR22760. PTHR22760. 2 hits.
PfamiPF03901. Glyco_transf_22. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis."
    Frank C.G., Aebi M.
    Glycobiology 15:1156-1163(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Ordered assembly of the asymmetrically branched lipid-linked oligosaccharide in the endoplasmic reticulum is ensured by the substrate specificity of the individual glycosyltransferases."
    Burda P., Jakob C.A., Beinhauer J., Hegemann J.H., Aebi M.
    Glycobiology 9:617-625(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.

Entry informationi

Entry nameiALG12_YEAST
AccessioniPrimary (citable) accession number: P53730
Secondary accession number(s): D6W1K4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3550 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

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 one 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.