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Protein

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1

Gene

Dad1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER) (By similarity). Loss of the DAD1 protein triggers apoptosis.By similarity

Catalytic activityi

Dolichyl diphosphooligosaccharide + [protein]-L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.

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

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • blastocyst development Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • protein glycosylation Source: UniProtKB
  • response to drug Source: Ensembl
  • response to nutrient Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 (EC:2.4.99.18)
Short name:
Oligosaccharyl transferase subunit DAD1
Alternative name(s):
Defender against cell death 1
Short name:
DAD-1
Gene namesi
Name:Dad1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:101912. Dad1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 3029CytoplasmicSequence analysisAdd
BLAST
Transmembranei31 – 5121HelicalSequence analysisAdd
BLAST
Topological domaini52 – 521LumenalSequence analysis
Transmembranei53 – 7321HelicalSequence analysisAdd
BLAST
Topological domaini74 – 9219CytoplasmicSequence analysisAdd
BLAST
Transmembranei93 – 11321HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 113112Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1PRO_0000124011Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP61804.
MaxQBiP61804.
PaxDbiP61804.
PRIDEiP61804.
TopDownProteomicsiP61804.

PTM databases

iPTMnetiP61804.
PhosphoSiteiP61804.

Expressioni

Gene expression databases

BgeeiP61804.
CleanExiMM_DAD1.
GenevisibleiP61804. MM.

Interactioni

Subunit structurei

Component of the oligosaccharyltransferase (OST) complex. OST seems to exist in different forms which contain at least RPN1, RPN2, OST48, DAD1, OSTC, KRTCAP2 and either STT3A or STT3B. OST can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022781.

Structurei

3D structure databases

ProteinModelPortaliP61804.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DAD/OST2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1746. Eukaryota.
ENOG4111Q2I. LUCA.
GeneTreeiENSGT00390000003324.
HOVERGENiHBG004452.
InParanoidiP61804.
KOiK12668.
OMAiGVIQFVY.
OrthoDBiEOG7WT43N.
PhylomeDBiP61804.
TreeFamiTF312846.

Family and domain databases

InterProiIPR003038. DAD/Ost2.
[Graphical view]
PANTHERiPTHR10705. PTHR10705. 1 hit.
PfamiPF02109. DAD. 1 hit.
[Graphical view]
PIRSFiPIRSF005588. DAD. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61804-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSASVVSVIS RFLEEYLSST PQRLKLLDAY LLYILLTGAL QFGYCLLVGT
60 70 80 90 100
FPFNSFLSGF ISCVGSFILA VCLRIQINPQ NKADFQGISP ERAFADFLFA
110
STILHLVVMN FVG
Length:113
Mass (Da):12,497
Last modified:January 23, 2007 - v3
Checksum:i481983CADCEB2345
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181S → N in AAC53098 (PubMed:9121464).Curated
Sequence conflicti29 – 291A → G in AAA85855 (PubMed:7737422).Curated
Sequence conflicti71 – 711V → G in AAC05296 (Ref. 7) Curated
Sequence conflicti100 – 1001A → G in AAA85855 (PubMed:7737422).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22107 mRNA. Translation: AAA85855.1.
U81051, U81050 Genomic DNA. Translation: AAC53098.1.
U83628 mRNA. Translation: AAC53359.1.
U84210, U84209 Genomic DNA. Translation: AAB58539.1.
Y13335 Genomic DNA. Translation: CAA73779.1.
AK002446 mRNA. Translation: BAB22107.1.
AK006711 mRNA. Translation: BAB24711.1.
AK030925 mRNA. Translation: BAE20464.1.
AK054480 mRNA. Translation: BAC35796.1.
BC024378 mRNA. Translation: AAH24378.1.
BC053379 mRNA. Translation: AAH53379.1.
BC058116 mRNA. Translation: AAH58116.1.
AF051310 Genomic DNA. Translation: AAC05296.1.
CCDSiCCDS27084.1.
PIRiI49285.
RefSeqiNP_001106829.1. NM_001113358.1.
NP_034145.1. NM_010015.4.
UniGeneiMm.319038.

Genome annotation databases

EnsembliENSMUST00000022781; ENSMUSP00000022781; ENSMUSG00000022174.
ENSMUST00000128231; ENSMUSP00000122366; ENSMUSG00000022174.
GeneIDi13135.
KEGGimmu:13135.
UCSCiuc007tvm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22107 mRNA. Translation: AAA85855.1.
U81051, U81050 Genomic DNA. Translation: AAC53098.1.
U83628 mRNA. Translation: AAC53359.1.
U84210, U84209 Genomic DNA. Translation: AAB58539.1.
Y13335 Genomic DNA. Translation: CAA73779.1.
AK002446 mRNA. Translation: BAB22107.1.
AK006711 mRNA. Translation: BAB24711.1.
AK030925 mRNA. Translation: BAE20464.1.
AK054480 mRNA. Translation: BAC35796.1.
BC024378 mRNA. Translation: AAH24378.1.
BC053379 mRNA. Translation: AAH53379.1.
BC058116 mRNA. Translation: AAH58116.1.
AF051310 Genomic DNA. Translation: AAC05296.1.
CCDSiCCDS27084.1.
PIRiI49285.
RefSeqiNP_001106829.1. NM_001113358.1.
NP_034145.1. NM_010015.4.
UniGeneiMm.319038.

3D structure databases

ProteinModelPortaliP61804.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022781.

PTM databases

iPTMnetiP61804.
PhosphoSiteiP61804.

Proteomic databases

EPDiP61804.
MaxQBiP61804.
PaxDbiP61804.
PRIDEiP61804.
TopDownProteomicsiP61804.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022781; ENSMUSP00000022781; ENSMUSG00000022174.
ENSMUST00000128231; ENSMUSP00000122366; ENSMUSG00000022174.
GeneIDi13135.
KEGGimmu:13135.
UCSCiuc007tvm.2. mouse.

Organism-specific databases

CTDi1603.
MGIiMGI:101912. Dad1.

Phylogenomic databases

eggNOGiKOG1746. Eukaryota.
ENOG4111Q2I. LUCA.
GeneTreeiENSGT00390000003324.
HOVERGENiHBG004452.
InParanoidiP61804.
KOiK12668.
OMAiGVIQFVY.
OrthoDBiEOG7WT43N.
PhylomeDBiP61804.
TreeFamiTF312846.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

NextBioi283198.
PROiP61804.
SOURCEiSearch...

Gene expression databases

BgeeiP61804.
CleanExiMM_DAD1.
GenevisibleiP61804. MM.

Family and domain databases

InterProiIPR003038. DAD/Ost2.
[Graphical view]
PANTHERiPTHR10705. PTHR10705. 1 hit.
PfamiPF02109. DAD. 1 hit.
[Graphical view]
PIRSFiPIRSF005588. DAD. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The highly conserved defender against the death 1 (DAD1) gene maps to human chromosome 14q11-q12 and mouse chromosome 14 and has plant and nematode homologs."
    Apte S.S., Mattei M.-G., Seldin M.F., Olsen B.R.
    FEBS Lett. 363:304-306(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A targeted mutation at the T-cell receptor alpha/delta locus impairs T-cell development and reveals the presence of the nearby antiapoptosis gene Dad1."
    Hong N.A., Cado D., Mitchell J., Ortiz B.D., Hsieh S.N., Winoto A.
    Mol. Cell. Biol. 17:2151-2157(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  3. Wang K., Gan L., Kuo C.L., Hood L.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  4. "Molecular cloning of the murine homologue of DAD-1, an ubiquitously expressed and highly conserved suppressor of apoptosis."
    Giegerich G.
    Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/cJ.
  5. "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: Kidney, Ovary, Testis and Thymus.
  6. "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: C57BL/6J and FVB/N.
    Tissue: Brain and Colon.
  7. Brewster J., Zachrone K., Hood L., Coffin J.D.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
    Strain: 129/SvJ.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiDAD1_MOUSE
AccessioniPrimary (citable) accession number: P61804
Secondary accession number(s): O08552
, O70364, P46966, P46968, Q3V3W6, Q96GB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 112 of the entry and version 3 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

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.