OST1A_ARATH
ID OST1A_ARATH Reviewed; 614 AA.
AC Q9SFX3; Q8H795;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1A;
DE AltName: Full=Ribophorin IA;
DE Short=RPN-IA;
DE AltName: Full=Ribophorin-1A;
DE Flags: Precursor;
GN Name=OST1A; Synonyms=RPN1A; OrderedLocusNames=At1g76400; ORFNames=F15M4.10;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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).
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; AC012394; AAF16661.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35835.1; -; Genomic_DNA.
DR EMBL; AY081297; AAL91186.1; -; mRNA.
DR EMBL; AF083780; AAN60338.1; -; mRNA.
DR EMBL; AY128779; AAM91179.1; -; mRNA.
DR EMBL; AY139776; AAM98094.1; -; mRNA.
DR PIR; F96791; F96791.
DR RefSeq; NP_177766.1; NM_106289.4.
DR AlphaFoldDB; Q9SFX3; -.
DR SMR; Q9SFX3; -.
DR BioGRID; 29191; 23.
DR STRING; 3702.AT1G76400.1; -.
DR iPTMnet; Q9SFX3; -.
DR PaxDb; Q9SFX3; -.
DR PRIDE; Q9SFX3; -.
DR ProteomicsDB; 248774; -.
DR EnsemblPlants; AT1G76400.1; AT1G76400.1; AT1G76400.
DR GeneID; 843972; -.
DR Gramene; AT1G76400.1; AT1G76400.1; AT1G76400.
DR KEGG; ath:AT1G76400; -.
DR Araport; AT1G76400; -.
DR TAIR; locus:2014579; AT1G76400.
DR eggNOG; KOG2291; Eukaryota.
DR HOGENOM; CLU_031381_2_0_1; -.
DR InParanoid; Q9SFX3; -.
DR OrthoDB; 1294725at2759; -.
DR PhylomeDB; Q9SFX3; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9SFX3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SFX3; baseline and differential.
DR Genevisible; Q9SFX3; 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: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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Isopeptide bond; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..614
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 1A"
FT /id="PRO_0000420806"
FT TOPO_DOM 26..432
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..614
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
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 311
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9ZUA0"
SQ SEQUENCE 614 AA; 68642 MW; 80078AEBFA62FB17 CRC64;
MKQSSVVDLL LLLLAIALLA TPAFSDLVLS KVERRIDVTS QIARVTKTLK VVNSGSESVS
EFALTFPKFL GNNLAYLSVA PSEGKGKSKR TLVNLSVREA DQKGLPDSIS VYSVALPKPL
SKGDTLTLEV VAAFTNVLQP FPEKITQGEI HLVMLQESAQ YLSPYAVESQ SLSIKLPNAR
IESYTKFENT KLQGSELKYG PYKNLQSYSY SPIVVHFESK AAFAVAEKLV REIEVSHWGN
VQVTENYNVV HRGAQLKGEF SRLDFQARPN PRGASAFRHL LARLPPRAHS IYYRDDIGNI
STSEMKSDSK KTELLIEPRF PLFGGWKTFF TIGYGLPLTD FLFASEGKRF LNISFGSPIL
DLVTEKLIVQ VVLPEGSKDI SVTTPFAVKQ SQEIKYSHLD IAGRPVVVLE KNNVVPDHNQ
HIQVYYKFSN INLLSEPLML ISGFFILFIT CIIYTRADIS ISKSSPSYLA KLQWDEVLAT
LQEVQSIVQK CLATHDKLEA SLRDLSRTGD IQTCKAARKS TDSLLKDLSK ELKPLLGFLQ
SFPSASHISP KVEELVVKEK ELQEKLMAKH TTVVEGYEKK SSGRDIENRI ASQQQKIIAL
RQEIEDLLEF IDEI
