RBM42_RAT
ID RBM42_RAT Reviewed; 478 AA.
AC Q6AXT7; G3V8X1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=RNA-binding protein 42;
DE AltName: Full=RNA-binding motif protein 42;
GN Name=Rbm42;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000312|EMBL:EDM07728.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
RN [4]
RP FUNCTION, INTERACTION WITH HNRNPK, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=19170760; DOI=10.1111/j.1365-2443.2008.01256.x;
RA Fukuda T., Naiki T., Saito M., Irie K.;
RT "hnRNP K interacts with RNA binding motif protein 42 and functions in the
RT maintenance of cellular ATP level during stress conditions.";
RL Genes Cells 14:113-128(2009).
CC -!- FUNCTION: Binds (via the RRM domain) to the 3' untranslated region
CC (UTR) of p21 mRNA. {ECO:0000269|PubMed:19170760}.
CC -!- SUBUNIT: Interacts with HNRNPK. {ECO:0000269|PubMed:19170760}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19170760}. Cytoplasm
CC {ECO:0000269|PubMed:19170760}. Note=Upon stress response, localizes
CC with HNRNPK in cytoplasmic aggregates of stalled translational
CC preinitiation complexes called stress granules.
CC -!- SIMILARITY: Belongs to the RRM RBM42 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH79321.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC141526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473979; EDM07728.1; -; Genomic_DNA.
DR EMBL; BC079321; AAH79321.1; ALT_INIT; mRNA.
DR RefSeq; NP_001014181.2; NM_001014159.2.
DR AlphaFoldDB; Q6AXT7; -.
DR SMR; Q6AXT7; -.
DR STRING; 10116.ENSRNOP00000029729; -.
DR iPTMnet; Q6AXT7; -.
DR PhosphoSitePlus; Q6AXT7; -.
DR jPOST; Q6AXT7; -.
DR PaxDb; Q6AXT7; -.
DR PRIDE; Q6AXT7; -.
DR Ensembl; ENSRNOT00000031254; ENSRNOP00000029729; ENSRNOG00000024278.
DR GeneID; 361545; -.
DR KEGG; rno:361545; -.
DR UCSC; RGD:1306184; rat.
DR CTD; 79171; -.
DR RGD; 1306184; Rbm42.
DR eggNOG; KOG0226; Eukaryota.
DR GeneTree; ENSGT00930000151055; -.
DR InParanoid; Q6AXT7; -.
DR OMA; RMPMMRG; -.
DR OrthoDB; 1249623at2759; -.
DR PhylomeDB; Q6AXT7; -.
DR TreeFam; TF313946; -.
DR PRO; PR:Q6AXT7; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000024278; Expressed in thymus and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISO:RGD.
DR CDD; cd12383; RRM_RBM42; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034215; RBM42_RRM.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..478
FT /note="RNA-binding protein 42"
FT /id="PRO_0000307752"
FT DOMAIN 379..457
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..478
FT /note="Necessary for interaction with HNRNPK"
FT /evidence="ECO:0000269|PubMed:19170760"
FT REGION 317..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..209
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..336
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000305"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTD8"
FT MOD_RES 151
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTD8"
FT MOD_RES 156
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTD8"
FT MOD_RES 166
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTD8"
FT MOD_RES 179
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTD8"
SQ SEQUENCE 478 AA; 50266 MW; 0EC198772F4C00FC CRC64;
MASAMAGAGP APGLPVAGGP VVPGPGVGIP GKSGEERLKE MEAEMALFEQ EVLGAPVTGI
PTAVPAVPTV EAMQVPPAPV IRPIIATNTY QQVQQTLEAR AAAAATVVPP MVGGPPFVGP
VGFGPADRSH LDSPEAREAM FLRRAAVAPQ RAPILRPAFV PHVLQRADSA LSSAAGGPRP
MALRPPHQAL VGPPLPGPPG PPMMLPPMAR APGPPLGSMA ALRPPLEEPA APRDLGLGLG
LGLKEKEEAV VAAAAGLEEA SAAVAVGAGG APAGPAVIGP SLPLALAMPL PEPEPLPLPL
EVVRGLLPPL RIPELLSLRP RPRPPRPEPP PGLMALEVPE PLGEDKKKGK PEKLKRCIRT
AAGSSWEDPS LLEWDADDFR IFCGDLGNEV NDDILARAFS RFPSFLKAKV IRDKRTGKTK
GYGFVSFKDP SDYVRAMREM NGKYVGSRPI KLRKSMWKDR NLDVVRKKQK EKKKLGLR
