Reviewed, UniProtKB/Swiss-Prot P61803 (DAD1_HUMAN)

Names and origin

Protein names

Recommended name:
    Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
      Short name=Oligosaccharyl transferase subunit DAD1
    EC=2.4.1.119
Alternative name(s):
    Defender against cell death 1
      Short name=DAD-1

Gene names

Name:

DAD1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	113 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the N-oligosaccharyl transferase enzyme 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). Loss of the DAD1 protein triggers apoptosis By similarity.
Catalytic activity	Dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine.
Subunit structure	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.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Sequence similarities	Belongs to the DAD/OST2 family.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane
Molecular function	Transferase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	anti-apoptosis Ref.1 Traceable author statement. Source: ProtInc apoptosis Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid N-linked glycosylation via asparagine Inferred by curator. Source: HGNC
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW oligosaccharyltransferase complex Traceable author statement. Source: HGNC
Molecular function	dolichyl-diphosphooligosaccharide-protein glycotransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7 Ref.8
	Chain	2 – 113	112	Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1		PRO_0000124009
Regions
	Transmembrane	31 – 51	21	Potential
	Transmembrane	53 – 73	21	Potential
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.8
Natural variations
	Natural variant	83	1	A → T: dbSNP rs5742796. Ref.5		VAR_018825
Experimental info
	Sequence conflict	20	1	T → I in AAH09798. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P61803-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 481983CADCEB2345	FASTA	113	12,497
	10 20 30 40 50 60 MSASVVSVIS RFLEEYLSST PQRLKLLDAY LLYILLTGAL QFGYCLLVGT FPFNSFLSGF 70 80 90 100 110 ISCVGSFILA VCLRIQINPQ NKADFQGISP ERAFADFLFA STILHLVVMN FVG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a human cDNA encoding a novel protein, DAD1, whose defect causes apoptotic cell death in hamster BHK21 cells." Nakashima T., Sekiguchi T., Kuraoka A., Fukushima K., Shibata Y., Komiyama S., Nishimoto T. Mol. Cell. Biol. 13:6367-6374(1993) [PubMed: 8413235] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Wang K., Lee I.Y., Hood L. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	NIEHS SNPs program Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-83.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Skin.
[7]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11. Tissue: Platelet.
[8]	Bienvenut W.V. Submitted (JUN-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-23, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBLGenBankDDBJ	D15057 mRNA. Translation: BAA03650.1. U84213, U84212 Genomic DNA. Translation: AAB58540.1. CR407682 mRNA. Translation: CAG28610.1. CR542204 mRNA. Translation: CAG47001.1. AY259117 Genomic DNA. Translation: AAO74827.1. BC007403 mRNA. Translation: AAH07403.1. BC009798 mRNA. Translation: AAH09798.1.
IPI	IPI00009407.
PIR	A54437.
RefSeq	NP_001335.1.
UniGene	Hs.82890
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P61803. 3 interactions.
Proteomic databases
PRIDE	P61803.
Genome annotation databases
Ensembl	ENSG00000129562. Homo sapiens. [Contig view]
GeneID	1603.
KEGG	hsa:1603.
Organism-specific databases
GeneCards	GC14M022103.
H-InvDB	HIX0011517.
HGNC	HGNC:2664. DAD1.
MIM	600243. gene.
PharmGKB	PA27136.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P61803.
OMA	P61803. YCCLVGT.
Enzyme and pathway databases
BRENDA	2.4.1.119. 247.
Gene expression databases
ArrayExpress	P61803.
Bgee	P61803.
CleanEx	HS_DAD1.
GermOnline	ENSG00000129562. Homo sapiens.
Family and domain databases
InterPro	IPR003038. DAD. [Graphical view]
PANTHER	PTHR10705. DAD. 1 hit.
Pfam	PF02109. DAD. 1 hit. [Graphical view]
PIRSF	PIRSF005588. DAD. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	6578.
SOURCE	Search...

Entry information

Entry name

DAD1_HUMAN

Accession

Primary (citable) accession number: P61803
Secondary accession number(s): O08552 , O70364, P46966, P46968, Q6FGA3, Q96GB7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 53 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)