RTNLB_ARATH
ID RTNLB_ARATH Reviewed; 271 AA.
AC Q9SUT9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Reticulon-like protein B2;
DE Short=AtRTNLB2;
DE AltName: Full=VirB2-interacting protein 2;
GN Name=RTNLB2; Synonyms=BTI2; OrderedLocusNames=At4g11220; ORFNames=F8L21.10;
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=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 FUNCTION, AND INTERACTION WITH VIRB2.
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 [6]
RP GENE FAMILY, NOMENCLATURE, AND SUBCELLULAR LOCATION.
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).
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:0000269|PubMed:17604024}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17604024}.
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DR EMBL; AL096882; CAB51406.1; -; Genomic_DNA.
DR EMBL; AL161531; CAB81223.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82986.1; -; Genomic_DNA.
DR EMBL; AY034901; AAK59408.1; -; mRNA.
DR EMBL; AY048273; AAK82535.1; -; mRNA.
DR EMBL; AY057606; AAL14401.1; -; mRNA.
DR EMBL; BT002368; AAN86201.1; -; mRNA.
DR EMBL; AY086294; AAM64366.1; -; mRNA.
DR PIR; T13013; T13013.
DR RefSeq; NP_192861.1; NM_117193.3.
DR AlphaFoldDB; Q9SUT9; -.
DR BioGRID; 12023; 26.
DR IntAct; Q9SUT9; 5.
DR STRING; 3702.AT4G11220.1; -.
DR iPTMnet; Q9SUT9; -.
DR PaxDb; Q9SUT9; -.
DR PRIDE; Q9SUT9; -.
DR ProteomicsDB; 228053; -.
DR EnsemblPlants; AT4G11220.1; AT4G11220.1; AT4G11220.
DR GeneID; 826724; -.
DR Gramene; AT4G11220.1; AT4G11220.1; AT4G11220.
DR KEGG; ath:AT4G11220; -.
DR Araport; AT4G11220; -.
DR TAIR; locus:2128238; AT4G11220.
DR eggNOG; KOG1792; Eukaryota.
DR HOGENOM; CLU_066344_1_0_1; -.
DR InParanoid; Q9SUT9; -.
DR OMA; LLCHGLM; -.
DR OrthoDB; 1106300at2759; -.
DR PhylomeDB; Q9SUT9; -.
DR PRO; PR:Q9SUT9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUT9; baseline and differential.
DR Genevisible; Q9SUT9; 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:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0071458; C:integral component of cytoplasmic side of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEA:InterPro.
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; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O82352"
FT CHAIN 2..271
FT /note="Reticulon-like protein B2"
FT /id="PRO_0000371283"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 85..271
FT /note="Reticulon"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..58
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 271 AA; 30280 MW; BEFDCD910C9DA732 CRC64;
MADEHKHEES SPNLDPAVEV VERESLMEKL SEKIHHKGDS SSSSSSDDEN EKKSSSSSPK
SLKSKVYRLF GRERPVHKVL GGGKPADIFM WKDKKMSGGV FGGATVAWVL FELMEYHLLT
LLCHVMIVAL AVLFLWSNAT MFIHKSPPKI PEVHIPEEPL LQLASGLRIE INRGISSLRE
IASGRDIKKF LSAIAGLWVL SILGGCYSFL TLAYIALVLL FTVPLFYDKY EDKVDSYGEK
AMAELKKQYA VLDAKVFSKI PRGPLKDKKK D
