OST48_ARATH
ID OST48_ARATH Reviewed; 437 AA.
AC Q944K2; Q8LDT6; Q94CD6; Q9LVR2;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit;
DE Short=Oligosaccharyl transferase 48 kDa subunit;
DE AltName: Full=Protein DEFECTIVE GLYCOSYLATION 1;
DE Flags: Precursor;
GN Name=OST48; Synonyms=DGL1; OrderedLocusNames=At5g66680; ORFNames=MSN2.7;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=15860005; DOI=10.1111/j.1365-313x.2005.02392.x;
RA Lerouxel O., Mouille G., Andeme-Onzighi C., Bruyant M.P., Seveno M.,
RA Loutelier-Bourhis C., Driouich A., Hoefte H., Lerouge P.;
RT "Mutants in DEFECTIVE GLYCOSYLATION, an Arabidopsis homolog of an
RT oligosaccharyltransferase complex subunit, show protein underglycosylation
RT and defects in cell differentiation and growth.";
RL Plant J. 42:455-468(2005).
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 (PubMed:15860005). 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 (By similarity).
CC {ECO:0000250|UniProtKB:P33767, ECO:0000269|PubMed:15860005}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:P33767}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Embryo-lethal. {ECO:0000269|PubMed:15860005}.
CC -!- SIMILARITY: Belongs to the DDOST 48 kDa subunit family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97274.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB018119; BAA97274.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED98251.1; -; Genomic_DNA.
DR EMBL; AF428338; AAL16268.1; -; mRNA.
DR EMBL; AY034944; AAK59450.1; -; mRNA.
DR EMBL; AY150381; AAN12926.1; -; mRNA.
DR EMBL; AY085807; AAM63023.1; -; mRNA.
DR RefSeq; NP_569038.1; NM_126066.4.
DR AlphaFoldDB; Q944K2; -.
DR SMR; Q944K2; -.
DR BioGRID; 22043; 46.
DR IntAct; Q944K2; 20.
DR STRING; 3702.AT5G66680.1; -.
DR iPTMnet; Q944K2; -.
DR SwissPalm; Q944K2; -.
DR PaxDb; Q944K2; -.
DR PRIDE; Q944K2; -.
DR ProteomicsDB; 248831; -.
DR EnsemblPlants; AT5G66680.1; AT5G66680.1; AT5G66680.
DR GeneID; 836801; -.
DR Gramene; AT5G66680.1; AT5G66680.1; AT5G66680.
DR KEGG; ath:AT5G66680; -.
DR Araport; AT5G66680; -.
DR TAIR; locus:2173659; AT5G66680.
DR eggNOG; KOG2754; Eukaryota.
DR HOGENOM; CLU_031804_0_0_1; -.
DR InParanoid; Q944K2; -.
DR OMA; HIKADEP; -.
DR OrthoDB; 975158at2759; -.
DR PhylomeDB; Q944K2; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q944K2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q944K2; baseline and differential.
DR Genevisible; Q944K2; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009664; P:plant-type cell wall organization; IMP:TAIR.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR InterPro; IPR005013; DDOST_48_kDa_subunit.
DR PANTHER; PTHR10830; PTHR10830; 1.
DR Pfam; PF03345; DDOST_48kD; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..437
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase 48 kDa subunit"
FT /id="PRO_0000420813"
FT TOPO_DOM 25..414
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 265
FT /note="S -> I (in Ref. 4; AAM63023)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="D -> G (in Ref. 3; AAK59450)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 48744 MW; A227381107CD0287 CRC64;
MVNLSRSVAL ISVFLLPLLS FSFSVDNPTD RRVLVLLDDL SLKSSHSIFF NTLKSRGFDL
DFKLAEDSKL ALQRYGQYLY DGLIIFAPST ERFGGSLDSK SIADFVDSGR DLILSADTAA
SDLIRGIATE CGVDFDEDSS AMVIDHTSFS VSDVDGDHTL IAADDLVKSD VILGKTKIEA
PVLFRGVAHS LNPTNNLVLK VLSASPSAYS ANPSSKLSSP PQLTGSSISL VSVMQARNNA
RVVISGSVQL FSDRLIRSGV QKAGSPNQYE KSGNEQFVTE LSKWVFHERG HLKAGNLVHH
RVGETDEPAI YRIKDDLEFS VEIYEWSGKS WEPYVANDVQ VQFYMMSPYV LKTLSTDKKG
LFHTSFKVPD VYGVFQFKVE YEKLGYTTLS LSKQIPVRPY RHNEYERFIP TAYPYYGACF
TTMAGFFVFS FVYLYHK
