DAD1_MOUSE
ID DAD1_MOUSE Reviewed; 113 AA.
AC P61804; O08552; O70364; P46966; P46968; Q3V3W6; Q96GB7;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 {ECO:0000305};
DE Short=Oligosaccharyl transferase subunit DAD1;
DE AltName: Full=Defender against cell death 1;
DE Short=DAD-1;
GN Name=Dad1 {ECO:0000312|MGI:MGI:101912};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7737422; DOI=10.1016/0014-5793(95)00321-y;
RA Apte S.S., Mattei M.-G., Seldin M.F., Olsen B.R.;
RT "The highly conserved defender against the death 1 (DAD1) gene maps to
RT human chromosome 14q11-q12 and mouse chromosome 14 and has plant and
RT nematode homologs.";
RL FEBS Lett. 363:304-306(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=9121464; DOI=10.1128/mcb.17.4.2151;
RA Hong N.A., Cado D., Mitchell J., Ortiz B.D., Hsieh S.N., Winoto A.;
RT "A targeted mutation at the T-cell receptor alpha/delta locus impairs T-
RT cell development and reveals the presence of the nearby antiapoptosis gene
RT Dad1.";
RL Mol. Cell. Biol. 17:2151-2157(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Wang K., Gan L., Kuo C.L., Hood L.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RA Giegerich G.;
RT "Molecular cloning of the murine homologue of DAD-1, an ubiquitously
RT expressed and highly conserved suppressor of apoptosis.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, Ovary, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
RC STRAIN=129/SvJ;
RA Brewster J., Zachrone K., Hood L., Coffin J.D.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that
CC catalyzes the initial transfer of a defined glycan
CC (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-
CC pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr
CC consensus motif in nascent polypeptide chains, the first step in
CC protein N-glycosylation (By similarity). N-glycosylation occurs
CC cotranslationally and the complex associates with the Sec61 complex at
CC the channel-forming translocon complex that mediates protein
CC translocation across the endoplasmic reticulum (ER). All subunits are
CC required for a maximal enzyme activity. {ECO:0000250|UniProtKB:E2R4X3,
CC ECO:0000250|UniProtKB:P61803}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P61803}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. OST
CC exists in two different complex forms which contain common core
CC subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or
CC STT3B as catalytic subunits, and form-specific accessory subunits.
CC STT3A complex assembly occurs through the formation of 3 subcomplexes.
CC Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the
CC STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core
CC subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The
CC STT3A complex can form stable complexes with the Sec61 complex or with
CC both the Sec61 and TRAP complexes. {ECO:0000250|UniProtKB:E2R4X3}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DAD/OST2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U22107; AAA85855.1; -; mRNA.
DR EMBL; U81051; AAC53098.1; -; Genomic_DNA.
DR EMBL; U81050; AAC53098.1; JOINED; Genomic_DNA.
DR EMBL; U83628; AAC53359.1; -; mRNA.
DR EMBL; U84210; AAB58539.1; -; Genomic_DNA.
DR EMBL; U84209; AAB58539.1; JOINED; Genomic_DNA.
DR EMBL; Y13335; CAA73779.1; -; Genomic_DNA.
DR EMBL; AK002446; BAB22107.1; -; mRNA.
DR EMBL; AK006711; BAB24711.1; -; mRNA.
DR EMBL; AK030925; BAE20464.1; -; mRNA.
DR EMBL; AK054480; BAC35796.1; -; mRNA.
DR EMBL; BC024378; AAH24378.1; -; mRNA.
DR EMBL; BC053379; AAH53379.1; -; mRNA.
DR EMBL; BC058116; AAH58116.1; -; mRNA.
DR EMBL; AF051310; AAC05296.1; -; Genomic_DNA.
DR CCDS; CCDS27084.1; -.
DR PIR; I49285; I49285.
DR RefSeq; NP_001106829.1; NM_001113358.1.
DR RefSeq; NP_034145.1; NM_010015.4.
DR AlphaFoldDB; P61804; -.
DR SMR; P61804; -.
DR BioGRID; 199045; 2.
DR ComplexPortal; CPX-5821; Oligosaccharyltransferase complex A.
DR ComplexPortal; CPX-5822; Oligosaccharyltransferase complex B.
DR STRING; 10090.ENSMUSP00000122366; -.
DR iPTMnet; P61804; -.
DR PhosphoSitePlus; P61804; -.
DR SwissPalm; P61804; -.
DR EPD; P61804; -.
DR jPOST; P61804; -.
DR MaxQB; P61804; -.
DR PaxDb; P61804; -.
DR PeptideAtlas; P61804; -.
DR PRIDE; P61804; -.
DR ProteomicsDB; 279358; -.
DR TopDownProteomics; P61804; -.
DR Antibodypedia; 7790; 274 antibodies from 30 providers.
DR DNASU; 13135; -.
DR Ensembl; ENSMUST00000022781; ENSMUSP00000022781; ENSMUSG00000022174.
DR Ensembl; ENSMUST00000128231; ENSMUSP00000122366; ENSMUSG00000022174.
DR GeneID; 13135; -.
DR KEGG; mmu:13135; -.
DR UCSC; uc007tvm.2; mouse.
DR CTD; 1603; -.
DR MGI; MGI:101912; Dad1.
DR VEuPathDB; HostDB:ENSMUSG00000022174; -.
DR eggNOG; KOG1746; Eukaryota.
DR GeneTree; ENSGT00390000003324; -.
DR HOGENOM; CLU_111220_2_1_1; -.
DR InParanoid; P61804; -.
DR OMA; FIFAHII; -.
DR OrthoDB; 1586516at2759; -.
DR PhylomeDB; P61804; -.
DR TreeFam; TF312846; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 13135; 31 hits in 77 CRISPR screens.
DR ChiTaRS; Dad1; mouse.
DR PRO; PR:P61804; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P61804; protein.
DR Bgee; ENSMUSG00000022174; Expressed in choroid plexus of fourth ventricle and 289 other tissues.
DR Genevisible; P61804; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0001824; P:blastocyst development; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:MGI.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR InterPro; IPR003038; DAD/Ost2.
DR PANTHER; PTHR10705; PTHR10705; 1.
DR Pfam; PF02109; DAD; 1.
DR PIRSF; PIRSF005588; DAD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61803"
FT CHAIN 2..113
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit DAD1"
FT /id="PRO_0000124011"
FT TOPO_DOM 2..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P61803"
FT CONFLICT 18
FT /note="S -> N (in Ref. 2; AAC53098)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="A -> G (in Ref. 1; AAA85855)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="V -> G (in Ref. 7; AAC05296)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="A -> G (in Ref. 1; AAA85855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 113 AA; 12497 MW; 481983CADCEB2345 CRC64;
MSASVVSVIS RFLEEYLSST PQRLKLLDAY LLYILLTGAL QFGYCLLVGT FPFNSFLSGF
ISCVGSFILA VCLRIQINPQ NKADFQGISP ERAFADFLFA STILHLVVMN FVG
