RMD5B_MOUSE
ID RMD5B_MOUSE Reviewed; 393 AA.
AC Q91YQ7;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=E3 ubiquitin-protein transferase RMND5B;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q96G75};
DE AltName: Full=Protein RMD5 homolog B;
GN Name=Rmnd5b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Core component of the CTLH E3 ubiquitin-protein ligase
CC complex that selectively accepts ubiquitin from UBE2H and mediates
CC ubiquitination and subsequent proteasomal degradation of the
CC transcription factor HBP1. MAEA and RMND5A are both required for
CC catalytic activity of the CTLH E3 ubiquitin-protein ligase complex.
CC Catalytic activity of the complex is required for normal cell
CC proliferation. The CTLH E3 ubiquitin-protein ligase complex is not
CC required for the degradation of enzymes involved in gluconeogenesis,
CC such as FBP1. {ECO:0000250|UniProtKB:Q96G75}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q96G75};
CC -!- SUBUNIT: Identified in the CTLH complex that contains GID4, RANBP9
CC and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog
CC RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA,
CC RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9
CC and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and
CC YPEL5 have ancillary roles. {ECO:0000250|UniProtKB:Q96G75}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q96G75}.
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DR EMBL; AK075599; BAC35848.1; -; mRNA.
DR EMBL; BC016075; AAH16075.1; -; mRNA.
DR CCDS; CCDS24656.1; -.
DR RefSeq; NP_079622.1; NM_025346.1.
DR AlphaFoldDB; Q91YQ7; -.
DR SMR; Q91YQ7; -.
DR STRING; 10090.ENSMUSP00000001081; -.
DR PhosphoSitePlus; Q91YQ7; -.
DR EPD; Q91YQ7; -.
DR PaxDb; Q91YQ7; -.
DR PRIDE; Q91YQ7; -.
DR ProteomicsDB; 300523; -.
DR Antibodypedia; 46079; 101 antibodies from 23 providers.
DR DNASU; 66089; -.
DR Ensembl; ENSMUST00000001081; ENSMUSP00000001081; ENSMUSG00000001054.
DR GeneID; 66089; -.
DR KEGG; mmu:66089; -.
DR UCSC; uc007iud.1; mouse.
DR CTD; 64777; -.
DR MGI; MGI:1913339; Rmnd5b.
DR VEuPathDB; HostDB:ENSMUSG00000001054; -.
DR eggNOG; KOG2817; Eukaryota.
DR GeneTree; ENSGT00940000153203; -.
DR HOGENOM; CLU_020227_3_1_1; -.
DR InParanoid; Q91YQ7; -.
DR OMA; CRQGMDD; -.
DR OrthoDB; 987270at2759; -.
DR PhylomeDB; Q91YQ7; -.
DR TreeFam; TF315176; -.
DR BioGRID-ORCS; 66089; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Rmnd5b; mouse.
DR PRO; PR:Q91YQ7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q91YQ7; protein.
DR Bgee; ENSMUSG00000001054; Expressed in granulocyte and 245 other tissues.
DR ExpressionAtlas; Q91YQ7; baseline and differential.
DR Genevisible; Q91YQ7; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS: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; cd16795; dRING_RMD5B; 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; IPR037681; RMD5B_dRING.
DR InterPro; IPR044063; ZF_RING_GID.
DR PANTHER; PTHR12170; PTHR12170; 1.
DR Pfam; PF10607; CLTH; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS51867; ZF_RING_GID; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..393
FT /note="E3 ubiquitin-protein transferase RMND5B"
FT /id="PRO_0000065710"
FT DOMAIN 116..148
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 155..212
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT ZN_FING 338..379
FT /note="RING-Gid-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96G75"
SQ SEQUENCE 393 AA; 44421 MW; 87AE6F88DC3A2311 CRC64;
MEQCACVERE LDKVLHKFLT YGQHCEQSLE ELLHSVGQLR AELASAALQG TPLSATLSLV
MSQCCRKIRD TVQKLASDHK DIHSSVSRVG KAIDRNFDSE ICGVVSDAVW DSREKQQQIL
QMAIVEHLYQ QGMLSVAEEL CQESTLNVDL DFKQPFLELN RILEALHEQD LGPALEWAVS
HRQRLLELNS SLEFKLHRLH FIRLLAGGPE KQLEALSYAR HFQPFARLHQ REIQVMMGSL
VYLRLGLEKS PYCHLLDNSH WAEICETFTR DACSLLGLSV ESPLSVSFAS GCVALPVLMN
IKAVIEQRQC TGVWSHKDEL PIEIELGMKC WYHSVFACPI LRQQTSDSNP PIKLICGHVI
SRDALNKLIN GGKLKCPYCP MEQNPADGKR IIF
