OST1B_ARATH
ID OST1B_ARATH Reviewed; 464 AA.
AC Q9ZUA0;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1B;
DE AltName: Full=Ribophorin IB;
DE Short=RPN-IB;
DE AltName: Full=Ribophorin-1B;
DE Flags: Precursor;
GN Name=OST1B; Synonyms=RPN1B; OrderedLocusNames=At2g01720; ORFNames=T8O11.11;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-310, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=19292762; DOI=10.1111/j.1365-313x.2009.03862.x;
RA Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.;
RT "Tandem affinity purification and mass spectrometric analysis of
RT ubiquitylated proteins in Arabidopsis.";
RL Plant J. 59:344-358(2009).
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:P41543}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:P41543}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the OST1 family. {ECO:0000305}.
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DR EMBL; AC006069; AAD12699.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05488.1; -; Genomic_DNA.
DR EMBL; BT022017; AAY25429.1; -; mRNA.
DR EMBL; AK226319; BAE98471.1; -; mRNA.
DR PIR; C84428; C84428.
DR RefSeq; NP_178281.1; NM_126233.6.
DR AlphaFoldDB; Q9ZUA0; -.
DR SMR; Q9ZUA0; -.
DR BioGRID; 104; 22.
DR STRING; 3702.AT2G01720.1; -.
DR iPTMnet; Q9ZUA0; -.
DR PaxDb; Q9ZUA0; -.
DR PRIDE; Q9ZUA0; -.
DR ProteomicsDB; 248670; -.
DR EnsemblPlants; AT2G01720.1; AT2G01720.1; AT2G01720.
DR GeneID; 814701; -.
DR Gramene; AT2G01720.1; AT2G01720.1; AT2G01720.
DR KEGG; ath:AT2G01720; -.
DR Araport; AT2G01720; -.
DR TAIR; locus:2065378; AT2G01720.
DR eggNOG; KOG2291; Eukaryota.
DR HOGENOM; CLU_031381_0_1_1; -.
DR InParanoid; Q9ZUA0; -.
DR OMA; KTYMDTL; -.
DR OrthoDB; 1294725at2759; -.
DR PhylomeDB; Q9ZUA0; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9ZUA0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUA0; baseline and differential.
DR Genevisible; Q9ZUA0; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IBA:GO_Central.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:TAIR.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR InterPro; IPR007676; Ribophorin_I.
DR PANTHER; PTHR21049; PTHR21049; 1.
DR Pfam; PF04597; Ribophorin_I; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Isopeptide bond; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..464
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 1B"
FT /id="PRO_0000420808"
FT TOPO_DOM 25..436
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 310
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19292762"
SQ SEQUENCE 464 AA; 52219 MW; 1BE3264069DDEDDB CRC64;
MAARIGIFSV FVAVLLSISA FSSAQDLQIV NAERRIDLSS HIVKAFLTLK VENIGKDPAA
EMLLAFPPTQ IKNLAMVQAL ATTGKKKKKT YLPLDVKPTE QPDAPNDTGY YRVTFISPLG
PGETVSLEVL YILTHSLEPF PVEITQSESQ LVYYHDSAVI LSPYHVKQQT TFIKTPSTRV
ESFTSIEPAN RAGKEIKYGP YENRASYSYT PVIIHFENNS PFAVVEELVR EIEISHWGSL
QITENYRLTH GGARHKGVFS RVDYQSKRSV SGASSFNALL AVLPPRVNSV YYRDEIGNIS
TSHLRTGFRK SELEFEPRYP LFGGWSATFI IGYRVPLEDY LFEASDGRRY LNFTFGCPLV
ETIVNKLTIK VVLPEGSKDP SAVLPFTVNQ ELQVKYSYLD IVGRTVVVLQ KDNVVPTHNV
PFQVYYTFKP IYMLAEPFML VSAFFLVFVA SLAYVHIDLN IVRK
