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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
 
 
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