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Receptor homology region, transmembrane domain- and RING domain-containing protein 1 (AtRMR1) (ReMembR-H2 protein JR700)

 RMR1_ARATH              Reviewed;         310 AA.
Q9M622;
22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 126.
RecName: Full=Receptor homology region, transmembrane domain- and RING domain-containing protein 1;
Short=AtRMR1;
AltName: Full=ReMembR-H2 protein JR700;
Flags: Precursor;
Name=RMR1; Synonyms=JR700; OrderedLocusNames=At5g66160;
ORFNames=K2A18.24;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10953001; DOI=10.1083/jcb.150.4.755;
Jiang L., Phillips T.E., Rogers S.W., Rogers J.C.;
"Biogenesis of the protein storage vacuole crystalloid.";
J. Cell Biol. 150:755-770(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9679202; DOI=10.1093/dnares/5.2.131;
Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
features of the regions of 1,381,565 bp covered by twenty one
physically assigned P1 and TAC clones.";
DNA Res. 5:131-145(1998).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16115960; DOI=10.1083/jcb.200504112;
Park M., Lee D., Lee G.J., Hwang I.;
"AtRMR1 functions as a cargo receptor for protein trafficking to the
protein storage vacuole.";
J. Cell Biol. 170:757-767(2005).
[6]
FUNCTION.
DOI=10.1016/j.plantsci.2006.12.008;
Park J.H., Oufattole M., Rogers J.C.;
"Golgi-mediated vacuolar sorting in plant cells: RMR proteins are
sorting receptors for the protein aggregation/membrane internalization
pathway.";
Plant Sci. 172:728-745(2007).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17696967; DOI=10.1111/j.1600-0854.2007.00625.x;
Hinz G., Colanesi S., Hillmer S., Rogers J.C., Robinson D.G.;
"Localization of vacuolar transport receptors and cargo proteins in
the Golgi apparatus of developing Arabidopsis embryos.";
Traffic 8:1452-1464(2007).
-!- FUNCTION: Involved in the trafficking of vacuolar proteins.
Functions probably as a sorting receptor for protein trafficking
to the protein storage vacuole (PSV) by binding the C-terminal
vacuolar sorting determinant (VSD) of vacuolar-sorted proteins.
{ECO:0000269|PubMed:16115960, ECO:0000269|PubMed:17696967,
ECO:0000269|Ref.6}.
-!- SUBCELLULAR LOCATION: Prevacuolar compartment membrane. Protein
storage vacuole membrane. Golgi apparatus membrane {ECO:0000305};
Single-pass type I membrane protein {ECO:0000305}. Note=Localizes
mainly to the prevacuolar compartment of the protein storage
vacuole, but a minor portion also localizes to the Golgi complex.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q9M622-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers and
siliques. {ECO:0000269|PubMed:16115960}.
-----------------------------------------------------------------------
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EMBL; AF218807; AAF32325.1; -; mRNA.
EMBL; AB011474; BAB10421.1; -; Genomic_DNA.
EMBL; CP002688; AED98167.1; -; Genomic_DNA.
EMBL; AY035089; AAK59594.1; -; mRNA.
EMBL; AY051036; AAK93713.1; -; mRNA.
RefSeq; NP_201417.1; NM_126014.4. [Q9M622-1]
UniGene; At.24500; -.
UniGene; At.67847; -.
UniGene; At.9220; -.
ProteinModelPortal; Q9M622; -.
SMR; Q9M622; -.
BioGrid; 21990; 6.
IntAct; Q9M622; 6.
STRING; 3702.AT5G66160.1; -.
iPTMnet; Q9M622; -.
PaxDb; Q9M622; -.
EnsemblPlants; AT5G66160.1; AT5G66160.1; AT5G66160. [Q9M622-1]
GeneID; 836748; -.
Gramene; AT5G66160.1; AT5G66160.1; AT5G66160.
KEGG; ath:AT5G66160; -.
Araport; AT5G66160; -.
TAIR; locus:2156872; AT5G66160.
eggNOG; KOG4628; Eukaryota.
eggNOG; ENOG410Z5DF; LUCA.
HOGENOM; HOG000242534; -.
InParanoid; Q9M622; -.
KO; K15692; -.
OMA; NMTESSE; -.
OrthoDB; EOG09360KRN; -.
PhylomeDB; Q9M622; -.
PRO; PR:Q9M622; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9M622; baseline and differential.
Genevisible; Q9M622; AT.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0000306; C:extrinsic component of vacuolar membrane; IDA:TAIR.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0032586; C:protein storage vacuole membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043621; F:protein self-association; IPI:TAIR.
GO; GO:0006886; P:intracellular protein transport; IDA:TAIR.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR003137; PA_domain.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF02225; PA; 1.
Pfam; PF13639; zf-RING_2; 1.
SMART; SM00184; RING; 1.
PROSITE; PS50089; ZF_RING_2; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
Golgi apparatus; Membrane; Metal-binding; Protein transport; Receptor;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Transport; Vacuole; Zinc; Zinc-finger.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 310 Receptor homology region, transmembrane
domain- and RING domain-containing
protein 1.
/FTId=PRO_0000425113.
TOPO_DOM 26 168 Lumenal. {ECO:0000255}.
TRANSMEM 169 189 Helical. {ECO:0000255}.
TOPO_DOM 190 310 Cytoplasmic. {ECO:0000255}.
DOMAIN 81 149 PA.
ZN_FING 232 274 RING-type; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
CARBOHYD 75 75 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 65 92 {ECO:0000255}.
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


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