RPN2_ARATH
ID RPN2_ARATH Reviewed; 691 AA.
AC Q93Z16; O49556;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2;
DE AltName: Full=Protein HAPLESS 6;
DE AltName: Full=Ribophorin II;
DE Short=RPN-II;
DE AltName: Full=Ribophorin-2;
DE Flags: Precursor;
GN Name=RPN2; Synonyms=HAP6; OrderedLocusNames=At4g21150; ORFNames=F7J7.90;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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;
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 DISRUPTION PHENOTYPE.
RX PubMed=15514068; DOI=10.1534/genetics.104.029447;
RA Johnson M.A., von Besser K., Zhou Q., Smith E., Aux G., Patton D.,
RA Levin J.Z., Preuss D.;
RT "Arabidopsis hapless mutations define essential gametophytic functions.";
RL Genetics 168:971-982(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
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:Q02795}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:Q02795}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q93Z16-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Short pollen tube growth and failure to exit the
CC style. {ECO:0000269|PubMed:15514068}.
CC -!- SIMILARITY: Belongs to the SWP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA17534.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79115.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021960; CAA17534.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161554; CAB79115.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84408.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84410.1; -; Genomic_DNA.
DR EMBL; AY058845; AAL24233.1; -; mRNA.
DR EMBL; AY079034; AAL79584.1; -; mRNA.
DR PIR; T04946; T04946.
DR RefSeq; NP_001190785.1; NM_001203856.1. [Q93Z16-1]
DR RefSeq; NP_193847.2; NM_118234.4. [Q93Z16-1]
DR AlphaFoldDB; Q93Z16; -.
DR BioGRID; 13154; 35.
DR IntAct; Q93Z16; 2.
DR STRING; 3702.AT4G21150.1; -.
DR PaxDb; Q93Z16; -.
DR PRIDE; Q93Z16; -.
DR ProteomicsDB; 227976; -. [Q93Z16-1]
DR EnsemblPlants; AT4G21150.1; AT4G21150.1; AT4G21150. [Q93Z16-1]
DR EnsemblPlants; AT4G21150.3; AT4G21150.3; AT4G21150. [Q93Z16-1]
DR GeneID; 827863; -.
DR Gramene; AT4G21150.1; AT4G21150.1; AT4G21150. [Q93Z16-1]
DR Gramene; AT4G21150.3; AT4G21150.3; AT4G21150. [Q93Z16-1]
DR KEGG; ath:AT4G21150; -.
DR Araport; AT4G21150; -.
DR TAIR; locus:2127328; AT4G21150.
DR eggNOG; KOG2447; Eukaryota.
DR InParanoid; Q93Z16; -.
DR OMA; TTWSART; -.
DR OrthoDB; 1001599at2759; -.
DR PhylomeDB; Q93Z16; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q93Z16; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93Z16; baseline and differential.
DR Genevisible; Q93Z16; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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: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:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR InterPro; IPR008814; Swp1.
DR PANTHER; PTHR12640; PTHR12640; 1.
DR Pfam; PF05817; Ribophorin_II; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..691
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 2"
FT /id="PRO_0000420811"
FT TOPO_DOM 22..593
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..614
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 615..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 631..651
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 652..653
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..691
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 691 AA; 74668 MW; 1E9FA626FF8388FB CRC64;
MMAGGNVRFL VLILAVAICG AASVFQPISD SHRSAALDVF VPVDGSYKSL EEAYEALKTL
EILGIDKKSD LSSKTCENVV KVLQSSSSTL KDAFYALNVN GILKCKIGEA GPKDIVSQLQ
AGVKDAKLLL DFYYSVRGLV LAKEQFPGTH ISLGDAEAIF RSIKSLSQSD GRWRYSSNNP
ESSTFAAGLA YETLAGVISL APSEFDPSLI QSVKTGILKL SDSIQKYDDG TFYFDEKSVD
ASQGPISTTA SVIRGLTSFA ASESTGLNLP GDKIVGLAKF FLGVGIPGDA KDFFNQIDAL
ACLEDNKFSV PLILSLPSTV ISLTKKEPLK VKVSTVLGSK APALSVKLTQ ALSSKSVDSS
VINNQELKFD ADSATYFLDS FPKNFDIGKY TFVFKIVLDE SAHEKVYITE AQTKVPIAAT
GAISIENAEI AVLDSDIGSV ESQKKLDLTK DGAVSLSANH LQKLRLSFQL TTPLGNAFKP
HQAFFKLKHE SQVEHIFLVK TSGKKSELVL DFLGLVEKLY YLSGKYEIQL TIGDASMENS
LLSNIGHIEL DLPERPEKAT RPPLQSTEPY SRYGPKAEIS HIFRIPEKLP AKQLSLVFLG
VIVLPFIGFL IGLTRLGVNI KSFPSSTGSA ISALLFHCGI GAVLLLYVLF WLKLDLFTTL
KALSLLGVFL LFVGHRTLSQ LASASNKLKS A
