RTNLA_ARATH
ID RTNLA_ARATH Reviewed; 275 AA.
AC Q9SUR3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Reticulon-like protein B1;
DE Short=AtRTNLB1;
DE AltName: Full=VirB2-interacting protein 1;
GN Name=RTNLB1; Synonyms=BTI1; OrderedLocusNames=At4g23630;
GN ORFNames=F9D16.100;
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 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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT proteome.";
RL Mol. Cell. Proteomics 3:675-691(2004).
RN [6]
RP FUNCTION, INTERACTION WITH VIRB2, INDUCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=15494553; DOI=10.1105/tpc.104.026476;
RA Hwang H.-H., Gelvin S.B.;
RT "Plant proteins that interact with VirB2, the Agrobacterium tumefaciens
RT pilin protein, mediate plant transformation.";
RL Plant Cell 16:3148-3167(2004).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17604024; DOI=10.1016/j.febslet.2007.06.032;
RA Nziengui H., Bouhidel K., Pillon D., Der C., Marty F., Schoefs B.;
RT "Reticulon-like proteins in Arabidopsis thaliana: structural organization
RT and ER localization.";
RL FEBS Lett. 581:3356-3362(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Plays a role in the Agrobacterium-mediated plant
CC transformation via its interaction with VirB2, the major component of
CC the T-pilus. {ECO:0000269|PubMed:15494553}.
CC -!- SUBUNIT: Interacts with VirB2. {ECO:0000269|PubMed:15494553}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9SH59}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:15060130}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:15060130}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in root tissues.
CC {ECO:0000269|PubMed:15494553}.
CC -!- INDUCTION: Up-regulated after Agrobacterium infection.
CC {ECO:0000269|PubMed:15494553}.
CC -!- DISRUPTION PHENOTYPE: Shows reduced levels of Agrobacterium-mediated
CC root transformation. {ECO:0000269|PubMed:15494553}.
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DR EMBL; AL035394; CAA23029.1; -; Genomic_DNA.
DR EMBL; AL161559; CAB79318.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84787.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66145.1; -; Genomic_DNA.
DR EMBL; AY050321; AAK91338.1; -; mRNA.
DR EMBL; AY133635; AAM91465.1; -; mRNA.
DR EMBL; AY087881; AAM65433.1; -; mRNA.
DR PIR; T05595; T05595.
DR RefSeq; NP_001328059.1; NM_001341623.1.
DR RefSeq; NP_194094.1; NM_118494.5.
DR AlphaFoldDB; Q9SUR3; -.
DR BioGRID; 13752; 6.
DR STRING; 3702.AT4G23630.1; -.
DR iPTMnet; Q9SUR3; -.
DR PaxDb; Q9SUR3; -.
DR PRIDE; Q9SUR3; -.
DR ProteomicsDB; 228050; -.
DR EnsemblPlants; AT4G23630.1; AT4G23630.1; AT4G23630.
DR EnsemblPlants; AT4G23630.2; AT4G23630.2; AT4G23630.
DR GeneID; 828463; -.
DR Gramene; AT4G23630.1; AT4G23630.1; AT4G23630.
DR Gramene; AT4G23630.2; AT4G23630.2; AT4G23630.
DR KEGG; ath:AT4G23630; -.
DR Araport; AT4G23630; -.
DR TAIR; locus:2128494; AT4G23630.
DR eggNOG; KOG1792; Eukaryota.
DR HOGENOM; CLU_066344_1_0_1; -.
DR InParanoid; Q9SUR3; -.
DR OMA; VCHFVIL; -.
DR OrthoDB; 1106300at2759; -.
DR PhylomeDB; Q9SUR3; -.
DR PRO; PR:Q9SUR3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUR3; baseline and differential.
DR Genevisible; Q9SUR3; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:UniProtKB.
DR GO; GO:0071458; C:integral component of cytoplasmic side of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IMP:TAIR.
DR InterPro; IPR003388; Reticulon.
DR InterPro; IPR045064; Reticulon-like_plant.
DR PANTHER; PTHR10994; PTHR10994; 1.
DR Pfam; PF02453; Reticulon; 1.
DR PROSITE; PS50845; RETICULON; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O82352"
FT CHAIN 2..275
FT /note="Reticulon-like protein B1"
FT /id="PRO_0000371282"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 89..274
FT /note="Reticulon"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O82352"
SQ SEQUENCE 275 AA; 30529 MW; EE165EFBB33258C6 CRC64;
MAEEHKHDES VIAPEPAVEV VERESLMDKI SEKIHHGGDS SSSSSSSDDE DEKKKTKKPS
SPSSSMKSKV YRLFGREQPV HKVLGGGKPA DIFMWKNKKM SGGVLGGATA AWVVFELMEY
HLLTLLCHVM IVVLAVLFLW SNATMFINKS PPKIPEVHIP EEPILQLASG LRIEINRGFS
SLREIASGRD LKKFLIAIAG LWVLSILGGC FNFLTLAYIA LVLLFTVPLA YDKYEDKVDP
LGEKAMIELK KQYAVLDEKV LSKIPLGPLK NKKKD
