RMR3_ARATH
ID RMR3_ARATH Reviewed; 422 AA.
AC F4I2Y3; O80554;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Receptor homology region, transmembrane domain- and RING domain-containing protein 3;
DE Short=AtRMR3;
DE Flags: Precursor;
GN Name=RMR3; OrderedLocusNames=At1g22670; ORFNames=T22J18.16;
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).
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: Prevacuolar compartment membrane {ECO:0000250}.
CC Protein storage vacuole membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC25519.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC003979; AAC25519.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30268.1; -; Genomic_DNA.
DR PIR; T00777; T00777.
DR RefSeq; NP_173681.1; NM_102114.2.
DR AlphaFoldDB; F4I2Y3; -.
DR SMR; F4I2Y3; -.
DR STRING; 3702.AT1G22670.1; -.
DR PaxDb; F4I2Y3; -.
DR PRIDE; F4I2Y3; -.
DR EnsemblPlants; AT1G22670.1; AT1G22670.1; AT1G22670.
DR GeneID; 838873; -.
DR Gramene; AT1G22670.1; AT1G22670.1; AT1G22670.
DR KEGG; ath:AT1G22670; -.
DR Araport; AT1G22670; -.
DR TAIR; locus:2199665; AT1G22670.
DR eggNOG; KOG4628; Eukaryota.
DR HOGENOM; CLU_035275_2_0_1; -.
DR InParanoid; F4I2Y3; -.
DR OMA; FEYKVRN; -.
DR OrthoDB; 1487241at2759; -.
DR PRO; PR:F4I2Y3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I2Y3; baseline and differential.
DR Genevisible; F4I2Y3; AT.
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: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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Membrane; Metal-binding; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport;
KW Vacuole; Zinc; Zinc-finger.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..422
FT /note="Receptor homology region, transmembrane domain- and
FT RING domain-containing protein 3"
FT /id="PRO_0000425117"
FT TOPO_DOM 23..168
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 81..146
FT /note="PA"
FT ZN_FING 232..274
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 344..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 64..89
FT /evidence="ECO:0000255"
SQ SEQUENCE 422 AA; 46257 MW; 2EEA736B9834196D CRC64;
MNLVVLLILT LLLFIVSYVV DAGQVILVDS NITRSFVDME ADFSPSVTTV ETGVVYVAEP
LNACRNLRNK PEQSPYGTSP LVLIIRGGCS FEYKVRNAQR SGFKAAIVYD NVDRNFLSAM
GGDSDGIKIQ AVFVMKRAGE MLKKYAGSEE MEVMLVPPNT EDSVWSLYAS IALILSLAIF
CVMVTCVFFY RYCSTIRNST SQFNGMCRRT VKAMPSVTFT CAKIDNTTGF SCAICLEDYI
VGDKLRVLPC SHKFHVACVD SWLISWRTFC PVCKRDARTT ADEPLATEST PFLSSSIATS
SLVCIDSPPL GSSVSFSPAH VSSSFIHQFV RSSPMNGSRI SENLRRQASP LQSSSQRSHL
SMKSSHSLGY STMSPLNAMG MSPYRPYPSN ASPGLFSSTN HLLSNYTANT FSHFASAHSL
PD
