RMR2_ARATH
ID RMR2_ARATH Reviewed; 448 AA.
AC Q8VZ14; Q9C8W4; Q9M621;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Receptor homology region, transmembrane domain- and RING domain-containing protein 2;
DE Short=AtRMR2;
DE AltName: Full=ReMembR-H2 protein JR702;
DE Flags: Precursor;
GN Name=RMR2; Synonyms=JR702; OrderedLocusNames=At1g71980; ORFNames=F17M19.13;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 [MRNA] OF 5-448, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Involved in the trafficking of vacuolar proteins. May
CC function as a sorting receptor for protein trafficking to the protein
CC storage vacuole (PSV) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Protein storage vacuole membrane
CC {ECO:0000269|PubMed:10953001}. Golgi apparatus membrane
CC {ECO:0000305|PubMed:10953001}; Single-pass type I membrane protein
CC {ECO:0000305|PubMed:10953001}. Note=Traffics through the Golgi
CC apparatus before reaching the vacuolar compartment.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52220.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC021665; AAG52220.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE35260.1; -; Genomic_DNA.
DR EMBL; AY065385; AAL38826.1; -; mRNA.
DR EMBL; AY133843; AAM91777.1; -; mRNA.
DR EMBL; AF218808; AAF32326.1; -; mRNA.
DR PIR; G96742; G96742.
DR RefSeq; NP_177343.2; NM_105856.7.
DR AlphaFoldDB; Q8VZ14; -.
DR SMR; Q8VZ14; -.
DR STRING; 3702.AT1G71980.1; -.
DR iPTMnet; Q8VZ14; -.
DR PaxDb; Q8VZ14; -.
DR PRIDE; Q8VZ14; -.
DR ProteomicsDB; 227961; -.
DR EnsemblPlants; AT1G71980.1; AT1G71980.1; AT1G71980.
DR GeneID; 843529; -.
DR Gramene; AT1G71980.1; AT1G71980.1; AT1G71980.
DR KEGG; ath:AT1G71980; -.
DR Araport; AT1G71980; -.
DR TAIR; locus:2016044; AT1G71980.
DR eggNOG; KOG4628; Eukaryota.
DR HOGENOM; CLU_035275_2_0_1; -.
DR InParanoid; Q8VZ14; -.
DR OMA; FMIVRCI; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q8VZ14; -.
DR PRO; PR:Q8VZ14; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VZ14; baseline and differential.
DR Genevisible; Q8VZ14; AT.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000326; C:protein storage vacuole; IDA:UniProtKB.
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:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Membrane; Metal-binding;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport; Vacuole; Zinc; Zinc-finger.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..448
FT /note="Receptor homology region, transmembrane domain- and
FT RING domain-containing protein 2"
FT /id="PRO_0000425115"
FT TOPO_DOM 21..163
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 60..144
FT /note="PA"
FT ZN_FING 232..274
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 344..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..87
FT /evidence="ECO:0000255"
FT CONFLICT 40
FT /note="F -> I (in Ref. 4; AAF32326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 448 AA; 48811 MW; EB1FD5B6EBBEC6CC CRC64;
MNRALVLLLY VCTVSCLASS KVILMRNNIT LSFDDIEANF APSVKGTGEI GVVYVAEPLD
ACQNLMNKPE QSSNETSPFV LIVRGGCSFE EKVRKAQRAG FKAAIIYDNE DRGTLIAMAG
NSGGIRIHAV FVTKETGEVL KEYAGFPDTK VWLIPSFENS AWSIMAVSFI SLLAMSAVLA
TCFFVRRHRI RRRTSRSSRV REFHGMSRRL VKAMPSLIFS SFHEDNTTAF TCAICLEDYT
VGDKLRLLPC CHKFHAACVD SWLTSWRTFC PVCKRDARTS TGEPPASEST PLLSSAASSF
TSSSLHSSVR SSALLIGPSL GSLPTSISFS PAYASSSYIR QSFQSSSNRR SPPISVSRSS
VDLRQQAASP SPSPSQRSYI SHMASPQSLG YPTISPFNTR YMSPYRPSPS NASPAMAGSS
NYPLNPLRYS ESAGTFSPYA SANSLPDC
