RTNLD_ARATH
ID RTNLD_ARATH Reviewed; 257 AA.
AC Q9FFS0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Reticulon-like protein B4;
DE Short=AtRTNLB4;
DE AltName: Full=VirB2-interacting protein 3;
GN Name=RTNLB4; Synonyms=BTI3; OrderedLocusNames=At5g41600; ORFNames=MBK23.13;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [6]
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 [7]
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; AB005233; BAB11466.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94696.1; -; Genomic_DNA.
DR EMBL; AY035169; AAK59673.1; -; mRNA.
DR EMBL; AY057638; AAL15269.1; -; mRNA.
DR EMBL; AY150449; AAN12890.1; -; mRNA.
DR RefSeq; NP_198975.1; NM_123524.4.
DR AlphaFoldDB; Q9FFS0; -.
DR BioGRID; 19413; 29.
DR IntAct; Q9FFS0; 36.
DR STRING; 3702.AT5G41600.1; -.
DR iPTMnet; Q9FFS0; -.
DR PaxDb; Q9FFS0; -.
DR PRIDE; Q9FFS0; -.
DR ProteomicsDB; 228051; -.
DR EnsemblPlants; AT5G41600.1; AT5G41600.1; AT5G41600.
DR GeneID; 834162; -.
DR Gramene; AT5G41600.1; AT5G41600.1; AT5G41600.
DR KEGG; ath:AT5G41600; -.
DR Araport; AT5G41600; -.
DR TAIR; locus:2160447; AT5G41600.
DR eggNOG; KOG1792; Eukaryota.
DR HOGENOM; CLU_066344_1_0_1; -.
DR InParanoid; Q9FFS0; -.
DR OMA; CHFAIFA; -.
DR OrthoDB; 1106300at2759; -.
DR PhylomeDB; Q9FFS0; -.
DR PRO; PR:Q9FFS0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFS0; baseline and differential.
DR Genevisible; Q9FFS0; 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:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA: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 Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..257
FT /note="Reticulon-like protein B4"
FT /id="PRO_0000371285"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 68..257
FT /note="Reticulon"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT REGION 19..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 257 AA; 28949 MW; 29B47FB77C64DB04 CRC64;
MVEDHKHEES ILEKIVEKIH GHGDSSSLSD SDDDKKSTSS SSSSFKSKIY RLFGREKPVH
KVLGGGKPAD IFLWRNKKVS GGVLGAVTAS WVLFELFEYH LLAFLCHFAI FALAALFLWS
NACTFIHKST PHIPEVHIPE DPILQLVSGL RIEINRGLTL LRNIASGKDV KKFILVIAGL
WVLSIIGSCY NFLTLFYTAT VLLFTIPVLY EKYEDKVDAY GEKAMREIKK QYAVLDEKVL
RKVISKIPRG ALNKKKD
