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DAD2_ARATH
ID   DAD2_ARATH              Reviewed;         115 AA.
AC   O22622; Q94A89; Q9SLH6;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 132.
DE   RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD2;
DE            Short=Oligosaccharyl transferase subunit DAD2;
DE   AltName: Full=Defender against cell death 2;
DE            Short=AtDAD2;
DE            Short=DAD-2;
GN   Name=DAD2; OrderedLocusNames=At2g35520; ORFNames=T32F12.10;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Danon A., Gallois P.;
RT   "AtDAD2: a new gene from the DAD1 family in Arabidopsis.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RA   Sugiura T., Naito K., Asahi T., Suzuki H.;
RT   "Differential regulation of two types of the defender against apoptotic
RT   cell death 1 (dad1) genes in senescing cotyledons and petals of Arabidopsis
RT   thaliana.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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. N-glycosylation occurs cotranslationally and
CC       the complex associates with the Sec61 complex at the channel-forming
CC       translocon complex that mediates protein translocation across the
CC       endoplasmic reticulum (ER). All subunits are required for a maximal
CC       enzyme activity. {ECO:0000250|UniProtKB:P46964}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC       {ECO:0000250|UniProtKB:P46964}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O22622-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O22622-2; Sequence=VSP_008913, VSP_008914;
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DAD/OST2 family. {ECO:0000305}.
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DR   EMBL; AF030172; AAB86478.1; -; Genomic_DNA.
DR   EMBL; Y17609; CAC80055.1; -; Genomic_DNA.
DR   EMBL; AC005314; AAC36169.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09116.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM62783.1; -; Genomic_DNA.
DR   EMBL; AK119013; BAC43589.1; -; mRNA.
DR   EMBL; AY049271; AAK83613.1; -; mRNA.
DR   EMBL; AY087959; AAM65506.1; -; mRNA.
DR   PIR; F84769; F84769.
DR   RefSeq; NP_001318358.1; NM_001336559.1. [O22622-1]
DR   RefSeq; NP_565807.1; NM_129104.4. [O22622-1]
DR   AlphaFoldDB; O22622; -.
DR   SMR; O22622; -.
DR   BioGRID; 3463; 63.
DR   IntAct; O22622; 63.
DR   STRING; 3702.AT2G35520.2; -.
DR   PaxDb; O22622; -.
DR   ProteomicsDB; 224703; -. [O22622-1]
DR   EnsemblPlants; AT2G35520.1; AT2G35520.1; AT2G35520. [O22622-1]
DR   EnsemblPlants; AT2G35520.3; AT2G35520.3; AT2G35520. [O22622-1]
DR   GeneID; 818117; -.
DR   Gramene; AT2G35520.1; AT2G35520.1; AT2G35520. [O22622-1]
DR   Gramene; AT2G35520.3; AT2G35520.3; AT2G35520. [O22622-1]
DR   KEGG; ath:AT2G35520; -.
DR   Araport; AT2G35520; -.
DR   eggNOG; KOG1746; Eukaryota.
DR   InParanoid; O22622; -.
DR   OMA; AFLEFCF; -.
DR   PhylomeDB; O22622; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:O22622; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O22622; baseline and differential.
DR   Genevisible; O22622; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   InterPro; IPR003038; DAD/Ost2.
DR   PANTHER; PTHR10705; PTHR10705; 1.
DR   Pfam; PF02109; DAD; 1.
DR   PIRSF; PIRSF005588; DAD; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Apoptosis; Endoplasmic reticulum; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..115
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase subunit DAD2"
FT                   /id="PRO_0000124020"
FT   TOPO_DOM        1..31
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..55
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..94
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         29..53
FT                   /note="IIDLYVCFAVFTALIQVAYMALVGS -> VHHYHFVLIFYESSLKLKNPLNV
FT                   LV (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_008913"
FT   VAR_SEQ         54..115
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_008914"
SQ   SEQUENCE   115 AA;  12647 MW;  A9B76DDF6ABA5F62 CRC64;
     MVKSTSKDAQ DLFHSLHSAY TATPTNLKII DLYVCFAVFT ALIQVAYMAL VGSFPFNSFL
     SGVLSCIGTA VLAVCLRIQV NKENKEFKDL APERAFADFV LCNLVLHLVI INFLG
 
 
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