RMR6_ARATH
ID RMR6_ARATH Reviewed; 318 AA.
AC F4HZZ4;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Receptor homology region, transmembrane domain- and RING domain-containing protein 6;
DE Short=AtRMR6;
DE Flags: Precursor;
GN Name=RMR6; OrderedLocusNames=At1g35625; ORFNames=F15O4;
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}.
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DR EMBL; AC007887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE31819.2; -; Genomic_DNA.
DR RefSeq; NP_001319153.1; NM_001333165.1.
DR AlphaFoldDB; F4HZZ4; -.
DR SMR; F4HZZ4; -.
DR STRING; 3702.AT1G35625.1; -.
DR PaxDb; F4HZZ4; -.
DR PRIDE; F4HZZ4; -.
DR EnsemblPlants; AT1G35625.1; AT1G35625.1; AT1G35625.
DR GeneID; 840462; -.
DR Gramene; AT1G35625.1; AT1G35625.1; AT1G35625.
DR KEGG; ath:AT1G35625; -.
DR Araport; AT1G35625; -.
DR TAIR; locus:2824666; AT1G35625.
DR eggNOG; KOG4628; Eukaryota.
DR HOGENOM; CLU_1646794_0_0_1; -.
DR InParanoid; F4HZZ4; -.
DR OrthoDB; 1487241at2759; -.
DR PRO; PR:F4HZZ4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HZZ4; baseline and differential.
DR Genevisible; F4HZZ4; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..318
FT /note="Receptor homology region, transmembrane domain- and
FT RING domain-containing protein 6"
FT /id="PRO_0000425120"
FT TOPO_DOM 22..162
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 70..143
FT /note="PA"
FT ZN_FING 233..275
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..87
FT /evidence="ECO:0000255"
SQ SEQUENCE 318 AA; 35285 MW; 10F0B5F0786D9CA7 CRC64;
MNGSWITILS LLVISQLASS KVTLIGKNTF LSFDDVEANF TPVVRRSGEY GLLYAAEPLD
ACSYLTNMAE KGSKFRPSYV LIVRGGCSFE EKIRNAQEAG YKAAIVYNDR YEELLVRMAG
NSSGVYIHGV LVTRTSGEVL KEYTSRAEME LLLIPGFGIS SWSIMAITFV SLLVISAVLA
SYFSVRRHRI RQHVRDLHHG GQGHSRMPKD LLQSMPTEVY TGVLEEGSTS VTCAICIDDY
RVGEILRILP CKHKYHAVCI DSWLGRCRSF CPVCKQNPRT GNDVPPASET TPLISPGPNS
ITSLQSFYDL PIVVRVYL