Q5E9C2 (DAD1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

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

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	113 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the DAD/OST2 family.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW protein glycosylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW oligosaccharyltransferase complex Inferred from sequence or structural similarity. Source: UniProtKB
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 By similarity
	Chain	2 – 113	112	Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1		PRO_0000124008
Regions
	Transmembrane	31 – 51	21	Helical; Potential
	Transmembrane	53 – 73	21	Helical; Potential
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5E9C2 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: EC5901CE03440C84	FASTA	113	12,495
	10 20 30 40 50 60 MSASVLSVIS RFLEEYLSAT PQRLKLLDAY LLYILLTGAL QFGYCLLVGT FPFNSFLSGF 70 80 90 100 110 ISCVGSFILA VCLRIQINPQ NKADFQGISP ERAFADFLFA STILHLVVMN FVG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic sequencing of the T cell receptor alpha locus." Conrad M.L., Mawer M.A., Davis S.K., Koop B.F. Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY227782 Genomic DNA. Translation: AAT39322.2. BT020998 mRNA. Translation: AAX09015.1. BC102081 mRNA. Translation: AAI02082.1.
IPI	IPI00708428.
RefSeq	NP_001029933.1. NM_001034761.1.
UniGene	Bt.30555.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5E9C2.
Proteomic databases
PRIDE	Q5E9C2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000025397; ENSBTAP00000025397; ENSBTAG00000019077.
GeneID	614538.
KEGG	bta:614538.
Organism-specific databases
CTD	1603.
Phylogenomic databases
eggNOG	maNOG20653.
GeneTree	ENSGT00390000003324.
HOVERGEN	HBG004452.
InParanoid	Q5E9C2.
OMA	YCCLVGT.
OrthoDB	EOG4G7C0W.
PhylomeDB	Q5E9C2.
Family and domain databases
InterPro	IPR003038. DAD. [Graphical view]
KO	K12668.
PANTHER	PTHR10705. DAD. 1 hit.
Pfam	PF02109. DAD. 1 hit. [Graphical view]
PIRSF	PIRSF005588. DAD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DAD1_BOVIN

Accession

Primary (citable) accession number: Q5E9C2
Secondary accession number(s): Q3T175, Q53ZY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 53 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program