RMD5_ARATH
ID RMD5_ARATH Reviewed; 388 AA.
AC Q9T075;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 169.
DE RecName: Full=Protein RMD5 homolog {ECO:0000305};
GN Name=RMD5 {ECO:0000305};
GN OrderedLocusNames=At4g37880 {ECO:0000312|Araport:AT4G37880};
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 Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RANBPM, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22676313; DOI=10.1186/1471-2229-12-83;
RA Tomastikova E., Cenklova V., Kohoutova L., Petrovska B., Vachova L.,
RA Halada P., Kocarova G., Binarova P.;
RT "Interactions of an Arabidopsis RanBPM homologue with LisH-CTLH domain
RT proteins revealed high conservation of CTLH complexes in eukaryotes.";
RL BMC Plant Biol. 12:83-83(2012).
CC -!- SUBUNIT: Interacts with RANBPM. {ECO:0000269|PubMed:22676313}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22676313}.
CC Note=Associates predominantly in the form of large cytoplasmic
CC complexes. {ECO:0000269|PubMed:22676313}.
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DR EMBL; AL035709; CAB38936.1; -; Genomic_DNA.
DR EMBL; AL161592; CAB80453.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86848.1; -; Genomic_DNA.
DR EMBL; BT020222; AAV66093.1; -; mRNA.
DR EMBL; BT021138; AAX22273.1; -; mRNA.
DR PIR; T06035; T06035.
DR RefSeq; NP_195501.1; NM_119949.5.
DR AlphaFoldDB; Q9T075; -.
DR SMR; Q9T075; -.
DR STRING; 3702.AT4G37880.1; -.
DR PaxDb; Q9T075; -.
DR PRIDE; Q9T075; -.
DR ProteomicsDB; 228151; -.
DR EnsemblPlants; AT4G37880.1; AT4G37880.1; AT4G37880.
DR GeneID; 829944; -.
DR Gramene; AT4G37880.1; AT4G37880.1; AT4G37880.
DR KEGG; ath:AT4G37880; -.
DR Araport; AT4G37880; -.
DR TAIR; locus:2137604; AT4G37880.
DR eggNOG; KOG2817; Eukaryota.
DR HOGENOM; CLU_020227_1_0_1; -.
DR InParanoid; Q9T075; -.
DR OMA; CRQGMDD; -.
DR OrthoDB; 987270at2759; -.
DR PhylomeDB; Q9T075; -.
DR PRO; PR:Q9T075; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T075; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0034657; C:GID complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16652; dRing_Rmd5p_like; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR045098; Fyv10_fam.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR037683; Rmd5_dRing.
DR InterPro; IPR044063; ZF_RING_GID.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12170; PTHR12170; 1.
DR Pfam; PF10607; CLTH; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS51867; ZF_RING_GID; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..388
FT /note="Protein RMD5 homolog"
FT /id="PRO_0000442062"
FT DOMAIN 112..144
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 150..207
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT ZN_FING 330..374
FT /note="RING-Gid-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
SQ SEQUENCE 388 AA; 44359 MW; EF70CAD0BD72D377 CRC64;
MELKSIKDAF DRVATKQKLS YSKTNEIVHM LSQEIDKALS ILEETPSSDT MLLDHRSILA
DVKKVFMEIA PITQLEATEK ELHAALTKYP KVLEKQLNPD ISKAYRHNVE FDTHIVNQII
ANFFYRQGMF DIGDCFVAET GESECSTRQS FVEMYRILEA MKRRDLEPAL NWAVSNSDKL
KEARSDLEMK LHSLHFLEIA RGKNSKEAID YARKHIATFA DSCLPEIQKL MCSLLWNRKL
DKSPYSEFLS PALWNNAVKE LTRQYCNLLG ESSESPLSIT VTAGTQALPV LLKYMNVVMA
NKKLDWQTME QLPVDAQLSE EFQFHSVFVC PVSKEQSSDD NPPMMMSCGH VLCKQTINKM
SKNGSKSSFK CPYCPTDVDI SRCRQLHF
