RER1A_ARATH
ID RER1A_ARATH Reviewed; 191 AA.
AC O48670;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Protein RER1A;
DE Short=AtRER1A;
GN Name=RER1A; OrderedLocusNames=At4g39220; ORFNames=T22F8.120;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=10737146; DOI=10.1023/a:1006329828395;
RA Sato K., Ueda T., Nakano A.;
RT "The Arabidopsis thaliana RER1 gene family: its potential role in the
RT endoplasmic reticulum localization of membrane proteins.";
RL Plant Mol. Biol. 41:815-824(1999).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Involved in the retrieval of endoplasmic reticulum membrane
CC proteins from the early Golgi compartment. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RER1 family. {ECO:0000305}.
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DR EMBL; AB010945; BAA24803.1; -; mRNA.
DR EMBL; AL050351; CAB43637.1; -; Genomic_DNA.
DR EMBL; AL161594; CAB80585.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87039.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67842.1; -; Genomic_DNA.
DR EMBL; AY044321; AAK73262.1; -; mRNA.
DR EMBL; BT000929; AAN41329.1; -; mRNA.
DR EMBL; AY086110; AAM63317.1; -; mRNA.
DR PIR; T08570; T08570.
DR RefSeq; NP_001329643.1; NM_001342528.1.
DR RefSeq; NP_195633.1; NM_120082.4.
DR AlphaFoldDB; O48670; -.
DR STRING; 3702.AT4G39220.1; -.
DR TCDB; 9.B.82.1.3; the endoplasmic reticulum retrieval protein1 (putative heavy metal transporter) (rer1) family.
DR iPTMnet; O48670; -.
DR PaxDb; O48670; -.
DR PRIDE; O48670; -.
DR ProteomicsDB; 235003; -.
DR EnsemblPlants; AT4G39220.1; AT4G39220.1; AT4G39220.
DR EnsemblPlants; AT4G39220.2; AT4G39220.2; AT4G39220.
DR GeneID; 830077; -.
DR Gramene; AT4G39220.1; AT4G39220.1; AT4G39220.
DR Gramene; AT4G39220.2; AT4G39220.2; AT4G39220.
DR KEGG; ath:AT4G39220; -.
DR Araport; AT4G39220; -.
DR TAIR; locus:2136373; AT4G39220.
DR eggNOG; KOG1688; Eukaryota.
DR HOGENOM; CLU_074889_1_1_1; -.
DR InParanoid; O48670; -.
DR OMA; HANYRWI; -.
DR OrthoDB; 1458086at2759; -.
DR PhylomeDB; O48670; -.
DR PRO; PR:O48670; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O48670; baseline and differential.
DR Genevisible; O48670; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0006621; P:protein retention in ER lumen; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:TAIR.
DR InterPro; IPR004932; Rer1.
DR PANTHER; PTHR10743; PTHR10743; 1.
DR Pfam; PF03248; Rer1; 1.
DR PIRSF; PIRSF016013; AtER_Rer1p; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..191
FT /note="Protein RER1A"
FT /id="PRO_0000207594"
FT TRANSMEM 39..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 191 AA; 21977 MW; FAAFA2F0BE8233AF CRC64;
MDESGGDSGS VATPVQQRAH EAWRIYQHYL DKTTPHANYR WIGTLVVALI YCLRVYYIQG
FYIIAYGLGI YLLNLLIGFL SPLVDPEAGG VSDGPSLPTR GSDEFKPFIR RLPEFKFWYS
MTKAFCIAFL MTFFSVFDVP VFWPILLCYW IVLFVLTMRR QIAHMIKYKY IPFSFGKQKY
GGRSSSGSRA D
