RMR1_ARATH
ID RMR1_ARATH Reviewed; 310 AA.
AC Q9M622;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Receptor homology region, transmembrane domain- and RING domain-containing protein 1;
DE Short=AtRMR1;
DE AltName: Full=ReMembR-H2 protein JR700;
DE Flags: Precursor;
GN Name=RMR1; Synonyms=JR700; OrderedLocusNames=At5g66160; ORFNames=K2A18.24;
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].
RX PubMed=10953001; DOI=10.1083/jcb.150.4.755;
RA Jiang L., Phillips T.E., Rogers S.W., Rogers J.C.;
RT "Biogenesis of the protein storage vacuole crystalloid.";
RL J. Cell Biol. 150:755-770(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16115960; DOI=10.1083/jcb.200504112;
RA Park M., Lee D., Lee G.J., Hwang I.;
RT "AtRMR1 functions as a cargo receptor for protein trafficking to the
RT protein storage vacuole.";
RL J. Cell Biol. 170:757-767(2005).
RN [6]
RP FUNCTION.
RX DOI=10.1016/j.plantsci.2006.12.008;
RA Park J.H., Oufattole M., Rogers J.C.;
RT "Golgi-mediated vacuolar sorting in plant cells: RMR proteins are sorting
RT receptors for the protein aggregation/membrane internalization pathway.";
RL Plant Sci. 172:728-745(2007).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17696967; DOI=10.1111/j.1600-0854.2007.00625.x;
RA Hinz G., Colanesi S., Hillmer S., Rogers J.C., Robinson D.G.;
RT "Localization of vacuolar transport receptors and cargo proteins in the
RT Golgi apparatus of developing Arabidopsis embryos.";
RL Traffic 8:1452-1464(2007).
CC -!- FUNCTION: Involved in the trafficking of vacuolar proteins. Functions
CC probably as a sorting receptor for protein trafficking to the protein
CC storage vacuole (PSV) by binding the C-terminal vacuolar sorting
CC determinant (VSD) of vacuolar-sorted proteins.
CC {ECO:0000269|PubMed:16115960, ECO:0000269|PubMed:17696967,
CC ECO:0000269|Ref.6}.
CC -!- SUBCELLULAR LOCATION: Prevacuolar compartment membrane. Protein storage
CC vacuole membrane. Golgi apparatus membrane {ECO:0000305}; Single-pass
CC type I membrane protein {ECO:0000305}. Note=Localizes mainly to the
CC prevacuolar compartment of the protein storage vacuole, but a minor
CC portion also localizes to the Golgi complex.
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=Q9M622-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers and siliques.
CC {ECO:0000269|PubMed:16115960}.
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DR EMBL; AF218807; AAF32325.1; -; mRNA.
DR EMBL; AB011474; BAB10421.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98167.1; -; Genomic_DNA.
DR EMBL; AY035089; AAK59594.1; -; mRNA.
DR EMBL; AY051036; AAK93713.1; -; mRNA.
DR RefSeq; NP_201417.1; NM_126014.4. [Q9M622-1]
DR PDB; 7BVW; X-ray; 2.10 A; A/B=206-283.
DR PDBsum; 7BVW; -.
DR AlphaFoldDB; Q9M622; -.
DR SMR; Q9M622; -.
DR BioGRID; 21990; 12.
DR IntAct; Q9M622; 12.
DR STRING; 3702.AT5G66160.1; -.
DR iPTMnet; Q9M622; -.
DR PaxDb; Q9M622; -.
DR PRIDE; Q9M622; -.
DR ProteomicsDB; 228213; -. [Q9M622-1]
DR EnsemblPlants; AT5G66160.1; AT5G66160.1; AT5G66160. [Q9M622-1]
DR GeneID; 836748; -.
DR Gramene; AT5G66160.1; AT5G66160.1; AT5G66160. [Q9M622-1]
DR KEGG; ath:AT5G66160; -.
DR Araport; AT5G66160; -.
DR TAIR; locus:2156872; AT5G66160.
DR eggNOG; KOG4628; Eukaryota.
DR InParanoid; Q9M622; -.
DR OMA; RIPTHKF; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q9M622; -.
DR PRO; PR:Q9M622; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9M622; baseline and differential.
DR Genevisible; Q9M622; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0000306; C:extrinsic component of vacuolar membrane; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032586; C:protein storage vacuole membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IDA:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd02123; PA_C_RZF_like; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR044744; ZNRF4/RNF13/RNF167_PA.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein;
KW Golgi apparatus; Membrane; Metal-binding; Protein transport; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport;
KW Vacuole; Zinc; Zinc-finger.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..310
FT /note="Receptor homology region, transmembrane domain- and
FT RING domain-containing protein 1"
FT /id="PRO_0000425113"
FT TOPO_DOM 26..168
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 81..149
FT /note="PA"
FT ZN_FING 232..274
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 284..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 65..92
FT /evidence="ECO:0000255"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:7BVW"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:7BVW"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:7BVW"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:7BVW"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:7BVW"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:7BVW"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:7BVW"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:7BVW"
SQ SEQUENCE 310 AA; 34429 MW; AC8F2B7C701B066F CRC64;
MRLVVSSCLL VAAPFLSSLL RVSLATVVLN SISASFADLP AKFDGSVTKN GICGALYVAD
PLDGCSPLLH AAASNWTQHR TTKFALIIRG ECSFEDKLLN AQNSGFQAVI VYDNIDNEDL
IVMKVNPQDI TVDAVFVSNV AGEILRKYAR GRDGECCLNP PDRGSAWTVL AISFFSLLLI
VTFLLIAFFA PRHWTQWRGR HTRTIRLDAK LVHTLPCFTF TDSAHHKAGE TCAICLEDYR
FGESLRLLPC QHAFHLNCID SWLTKWGTSC PVCKHDIRTE TMSSEVHKRE SPRTDTSTSR
FAFAQSSQSR
