RBM7_DANRE
ID RBM7_DANRE Reviewed; 252 AA.
AC Q6P0F4;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=RNA-binding protein 7 {ECO:0000250|UniProtKB:Q9Y580};
DE AltName: Full=RNA-binding motif protein 7 {ECO:0000250|UniProtKB:Q9Y580};
GN Name=rbm7 {ECO:0000250|UniProtKB:Q9Y580}; ORFNames=zgc:77304;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=27193168; DOI=10.1093/hmg/ddw149;
RA Giunta M., Edvardson S., Xu Y., Schuelke M., Gomez-Duran A., Boczonadi V.,
RA Elpeleg O., Mueller J.S., Horvath R.;
RT "Altered RNA metabolism due to a homozygous RBM7 mutation in a patient with
RT spinal motor neuropathy.";
RL Hum. Mol. Genet. 25:2985-2996(2016).
CC -!- FUNCTION: RNA-binding subunit of the trimeric nuclear exosome targeting
CC (NEXT) complex, a complex that functions as an RNA exosome cofactor
CC that directs a subset of non-coding short-lived RNAs for exosomal
CC degradation. NEXT is involved in surveillance and turnover of aberrant
CC transcripts and non-coding RNAs. Binds preferentially polyuridine
CC sequences and associates with newly synthesized RNAs, including pre-
CC mRNAs and short-lived exosome substrates such as promoter upstream
CC transcripts (PROMPTs), enhancer RNAs (eRNAs), and 3'-extended products
CC from small nuclear RNAs (snRNAs). {ECO:0000250|UniProtKB:Q9Y580}.
CC -!- SUBUNIT: Component of the nuclear exosome targeting (NEXT) complex
CC composed of MTREX, ZCCHC8, and RBM7 that directs a subset of non-coding
CC short-lived RNAs for exosomal degradation.
CC {ECO:0000250|UniProtKB:Q9Y580}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9Y580}. Nucleus {ECO:0000250|UniProtKB:Q9CQT2}.
CC Note=Excluded from the nucleolus. {ECO:0000250|UniProtKB:Q9Y580}.
CC -!- DOMAIN: The RRM domain mediates RNA binding; the RNA must have four
CC nucleotides for efficient binding. Mediates the interaction of NEXT
CC complex with promoter upstream transcripts (PROMPTs) and potentially
CC aberrant forms of other non coding RNAs, such as snRNAs. The RRM domain
CC exhibits specificity for polyuridine sequences.
CC {ECO:0000250|UniProtKB:Q9Y580}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of rbm7 causes several
CC degrees of the severity in the phenotype. Mildly affected fish are
CC unable to swim away normally upon touch stimulation. The body shape is
CC slightly shorter and sporadically brain edema could be observed. The
CC moderately affected fish have a curved body shape, smaller head and
CC eyes. Heart and brain edema are frequently observed. In fish with
CC severe phenotype the body shape is completely altered, the tail is
CC absent, and the head and eyes are smaller.
CC {ECO:0000269|PubMed:27193168}.
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; CU633933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065641; AAH65641.1; -; mRNA.
DR AlphaFoldDB; Q6P0F4; -.
DR SMR; Q6P0F4; -.
DR STRING; 7955.ENSDARP00000007431; -.
DR PaxDb; Q6P0F4; -.
DR Ensembl; ENSDART00000009775; ENSDARP00000007431; ENSDARG00000020841.
DR ZFIN; ZDB-GENE-030131-6724; rbm7.
DR eggNOG; KOG4454; Eukaryota.
DR GeneTree; ENSGT00870000136493; -.
DR HOGENOM; CLU_087967_0_0_1; -.
DR InParanoid; Q6P0F4; -.
DR OMA; PDNLQKH; -.
DR PhylomeDB; Q6P0F4; -.
DR TreeFam; TF323596; -.
DR PRO; PR:Q6P0F4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000020841; Expressed in cleaving embryo and 27 other tissues.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; IMP:ZFIN.
DR GO; GO:0021693; P:cerebellar Purkinje cell layer structural organization; IMP:ZFIN.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Nucleus; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y580"
FT CHAIN 2..252
FT /note="RNA-binding protein 7"
FT /id="PRO_0000448488"
FT DOMAIN 9..86
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 88..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 252 AA; 28710 MW; 4BCC5FEF1B2C00F4 CRC64;
MGIADEADRT LFVGNLDPQV TEEVIFELFL QAGPLIKVKI PKDNEGKSKL FAFVNFKHEV
SVPYALNLLN GIRLHGRQLN IKFKTGSSHI NQEGKSPANS QNPSPANTPG HRGGRTPEQM
GSPSYSPPQH MQRPFSSPDT LQRQAMMNNM WQVQMQQLQM LSGTFQQGMQ QLRGNADGGW
SGHRGQRHSP QDNNNHQGRD QRHGNGANNY ERNRRDGQRG DFYHHDDRSG GHNRNYPPDR
RRDSREGRWK HF
