位置:首页 > 蛋白库 > RMR1_ORYSJ
RMR1_ORYSJ
ID   RMR1_ORYSJ              Reviewed;         533 AA.
AC   Q10R93; Q10R92; Q8S7T8;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Receptor homology region, transmembrane domain- and RING domain-containing protein 1;
DE            Short=OsRMR1;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os03g0167500, LOC_Os03g07130; ORFNames=OSJNBa0091P11.36;
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=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21493745; DOI=10.1093/mp/ssr025;
RA   Shen Y., Wang J., Ding Y., Lo S.W., Gouzerh G., Neuhaus J.M., Jiang L.;
RT   "The rice RMR1 associates with a distinct prevacuolar compartment for the
RT   protein storage vacuole pathway.";
RL   Mol. Plant 4:854-868(2011).
CC   -!- FUNCTION: Involved in the trafficking of vacuolar proteins. Functions
CC       probably as a sorting receptor for protein trafficking to the protein
CC       storage vacuole (PSV) by binding the C-terminal vacuolar sorting
CC       determinant (VSD) of vacuolar-sorted proteins.
CC       {ECO:0000269|PubMed:21493745}.
CC   -!- SUBCELLULAR LOCATION: Prevacuolar compartment membrane
CC       {ECO:0000269|PubMed:21493745}. Protein storage vacuole membrane
CC       {ECO:0000269|PubMed:21493745}. Golgi apparatus membrane
CC       {ECO:0000305|PubMed:21493745}; Single-pass type I membrane protein
CC       {ECO:0000305|PubMed:21493745}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q10R93-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q10R93-2; Sequence=VSP_053580;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL84300.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC073556; AAL84300.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DP000009; ABF94172.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF94173.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF10996.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS82487.1; -; Genomic_DNA.
DR   EMBL; AK070468; BAG91973.1; -; mRNA.
DR   RefSeq; XP_015632382.1; XM_015776896.1. [Q10R93-1]
DR   RefSeq; XP_015632383.1; XM_015776897.1. [Q10R93-1]
DR   RefSeq; XP_015632384.1; XM_015776898.1. [Q10R93-2]
DR   AlphaFoldDB; Q10R93; -.
DR   SMR; Q10R93; -.
DR   STRING; 4530.OS03T0167500-01; -.
DR   PaxDb; Q10R93; -.
DR   PRIDE; Q10R93; -.
DR   EnsemblPlants; Os03t0167500-01; Os03t0167500-01; Os03g0167500. [Q10R93-2]
DR   EnsemblPlants; Os03t0167500-02; Os03t0167500-02; Os03g0167500. [Q10R93-1]
DR   GeneID; 4331745; -.
DR   Gramene; Os03t0167500-01; Os03t0167500-01; Os03g0167500. [Q10R93-2]
DR   Gramene; Os03t0167500-02; Os03t0167500-02; Os03g0167500. [Q10R93-1]
DR   KEGG; osa:4331745; -.
DR   eggNOG; KOG4628; Eukaryota.
DR   OMA; FMIVRCI; -.
DR   OrthoDB; 1487241at2759; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0044260; P:cellular macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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   Alternative splicing; Disulfide bond; Glycoprotein; Golgi apparatus;
KW   Membrane; Metal-binding; Protein transport; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Transport; Vacuole; Zinc; Zinc-finger.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..533
FT                   /note="Receptor homology region, transmembrane domain- and
FT                   RING domain-containing protein 1"
FT                   /id="PRO_0000425114"
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..533
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          84..145
FT                   /note="PA"
FT   ZN_FING         236..278
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          309..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..476
FT                   /note="Polar residues"
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"
FT   VAR_SEQ         395..428
FT                   /note="RYASPHMSHSGYASPSPHVSSSYVSNSGYGSSSY -> SY (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:12869764"
FT                   /id="VSP_053580"
SQ   SEQUENCE   533 AA;  57168 MW;  7B04C66FA33DB434 CRC64;
     MNRRRTMLLL ICLCATFCLM TQLGAANVVL MGTNLTLSFD DVEASFAPGV KGSGFEGVVY
     TAEPLDACSP LTSKAEKGPP SPFALIIRGG CTFDEKVKNA QDAGFKAAIV YDNENSGVLI
     SMAGSSGGIH IYAVFISKAS GEVLKKFSGH TDVEVWILPA FENSAWSIMA ISFISLLAMS
     AVLATCFFVR RHHIRRDRPR IPEAREFHGM SSQLVKAMPS LIFTKVQEDN CTSSMCAICL
     EDYNVGEKLR VLPCRHKFHA ACVDLWLTTW RTFCPVCKRD ASTGIPDPPA SETTPLLSSA
     VRLPSQSSSF RSSVAASPPR PISRRPSSQS ISRIYAASGT PNSPNPIRSF TNSTAMSISR
     SNVDLSNMSS RPRASHLASA HSLVGSHLSP PINIRYASPH MSHSGYASPS PHVSSSYVSN
     SGYGSSSYYL GSSSQHRSYL RRCGESGPSL STMAPQSPQQ SQLRHGGESD LNLAGASSGQ
     SFRQSYLRHC ADSEVNLAGA SSGQSFRQSY LRHCADSDAS LSAMASAQSL PGC
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024