RMR2_ORYSJ
ID RMR2_ORYSJ Reviewed; 461 AA.
AC Q69U49;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 2.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Receptor homology region, transmembrane domain- and RING domain-containing protein 2;
DE Short=OsRMR2;
DE Flags: Precursor;
GN Name=RMR1; OrderedLocusNames=Os08g0104300, LOC_Os08g01360;
GN ORFNames=P0015C07.39-1;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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=BAD33177.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF22691.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG95114.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP004654; BAD33177.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008214; BAF22691.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP014964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK101543; BAG95114.1; ALT_INIT; mRNA.
DR RefSeq; XP_015650612.1; XM_015795126.1.
DR AlphaFoldDB; Q69U49; -.
DR SMR; Q69U49; -.
DR STRING; 4530.OS08T0104300-02; -.
DR PaxDb; Q69U49; -.
DR GeneID; 4344437; -.
DR KEGG; osa:4344437; -.
DR eggNOG; KOG4628; Eukaryota.
DR HOGENOM; CLU_035275_2_0_1; -.
DR InParanoid; Q69U49; -.
DR OrthoDB; 1487241at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; Q69U49; OS.
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 2: Evidence at transcript level;
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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..461
FT /note="Receptor homology region, transmembrane domain- and
FT RING domain-containing protein 2"
FT /id="PRO_0000425116"
FT TOPO_DOM 27..167
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 67..147
FT /note="PA"
FT ZN_FING 236..278
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 319..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 68..91
FT /evidence="ECO:0000255"
SQ SEQUENCE 461 AA; 50303 MW; 182105B4670478E0 CRC64;
MNCTKGGGFP LLFCAVICLM AQQGACNVVL IANNTTLSFD DVEATFTPEV KDSGVNGAIY
AVEPLDACSP LRKKAANGPV SPFALVIRGG CQFDDKVRNA QNAGFKAVIV YDDEDSGVLV
SMAGSSSGIY IYAVFLSKAS GEVLKKYSGQ SDVEVWILPV YENSAWSIMA ISFTSLLAMA
AVLATCFFVR RHQIRRDRGR IPVTREFHGM SSQLVKAMPS LIFTKVQEDN STSSSCAICL
EDYSFGEKLR VLPCRHKFHA TCVDMWLTSW KTFCPVCKRD ASAGTSKPPA SESTPLLSSV
IHLSAESTAL SSFRSTVAVS PPRPIRRHPS SQSTSRAYSI SSAPRNYNLQ RYYTNSPYIS
TSRSNVDLAN MSSQWSHTPH QASMHSLRSG HLSLPINIRY TIPHVSRSDY GSASLGLSHD
SCSHHGSPSY YHSSLGQQRS YLMHRTESGP SLSTMVLQSP Q
