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RMR4_ARATH
ID   RMR4_ARATH              Reviewed;         448 AA.
AC   Q0WPW5; Q9M0N7;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Receptor homology region, transmembrane domain- and RING domain-containing protein 4;
DE            Short=AtRMR4;
DE   Flags: Precursor;
GN   Name=RMR4; OrderedLocusNames=At4g09560; ORFNames=T15G18.20;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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=CAB78079.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL161515; CAB78079.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE82765.1; -; Genomic_DNA.
DR   EMBL; AK228945; BAF00834.1; -; mRNA.
DR   PIR; F85097; F85097.
DR   RefSeq; NP_192694.2; NM_117024.4.
DR   AlphaFoldDB; Q0WPW5; -.
DR   SMR; Q0WPW5; -.
DR   STRING; 3702.AT4G09560.1; -.
DR   iPTMnet; Q0WPW5; -.
DR   PaxDb; Q0WPW5; -.
DR   PRIDE; Q0WPW5; -.
DR   EnsemblPlants; AT4G09560.1; AT4G09560.1; AT4G09560.
DR   GeneID; 826540; -.
DR   Gramene; AT4G09560.1; AT4G09560.1; AT4G09560.
DR   KEGG; ath:AT4G09560; -.
DR   Araport; AT4G09560; -.
DR   TAIR; locus:2133697; AT4G09560.
DR   eggNOG; KOG4628; Eukaryota.
DR   HOGENOM; CLU_035275_2_0_1; -.
DR   InParanoid; Q0WPW5; -.
DR   OMA; QETKVEM; -.
DR   OrthoDB; 1487241at2759; -.
DR   PhylomeDB; Q0WPW5; -.
DR   PRO; PR:Q0WPW5; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q0WPW5; baseline and differential.
DR   Genevisible; Q0WPW5; 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   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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..448
FT                   /note="Receptor homology region, transmembrane domain- and
FT                   RING domain-containing protein 4"
FT                   /id="PRO_0000425118"
FT   TOPO_DOM        21..165
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..448
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          74..146
FT                   /note="PA"
FT   ZN_FING         234..276
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          281..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        62..89
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   448 AA;  49723 MW;  7D1A0DAEB690DACD CRC64;
     MIRSSIVILS LLLISHLVSA KVLLIGNSTS LSFDDVEATF TPMIKRSDQG GVLYVAEPLD
     ACSDLVNTVN VKNGTTVSPP YVLIIRGGCS FEDKIRNAQK AGYKAAIVYD YEDFGFLVSM
     AGNPSGVLIY GTFVSKATGE VLKEYAGRTD FEVWLMPSFE TSAWSIMAIS FISLLAMSAV
     LATCFFVRRH RVRRRRILAL NGNDFHRMPK SMIIRMPTTI FNGICDEATT SILCCICLEN
     YEKGDKLRIL PCHHKFHVAC VDLWLGQRKS FCPVCKRDAR SISTDKPPSE HTPFLSRTPS
     MTPTSSFLLS SSSTTPLQSS HELPISIRVD PSLPSTSMQP HTVPMYLSHS RSHTSFQNGS
     NRFSRPIPVS RSSADLRNAV SQRSYNSPHQ VSLPRFLHSR YTHILGPGNA SRSQVVGLLT
     SQREHSLHQN DSRRSFIHFA SASSLPGW
 
 
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