RMXRL_RAT
ID RMXRL_RAT Reviewed; 388 AA.
AC P84586;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=RNA-binding motif protein, X chromosome retrogene-like;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein G retrogene-like;
DE Short=hnRNP G;
DE AltName: Full=RNA-binding motif protein, X chromosome retrogene;
DE Contains:
DE RecName: Full=RNA-binding motif protein, X chromosome retrogene-like, N-terminally processed;
GN Name=Rbmxrtl;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
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]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: RNA-binding protein that plays several role in the regulation
CC of pre- and post-transcriptional processes. Implicated in tissue-
CC specific regulation of gene transcription and alternative splicing of
CC pre-mRNAs. Associates with chromatin. Associates with nascent mRNAs
CC transcribed by RNA polymerase II. Component of the supraspliceosome
CC complex that regulates pre-mRNA alternative splice site selection.
CC Binds non-specifically to pre-mRNAs (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Component of
CC ribonucleosomes. {ECO:0000250}.
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DR EMBL; AABR03113401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001100890.1; NM_001107420.1.
DR AlphaFoldDB; P84586; -.
DR BMRB; P84586; -.
DR SMR; P84586; -.
DR BioGRID; 258804; 2.
DR IntAct; P84586; 1.
DR STRING; 10116.ENSRNOP00000016184; -.
DR iPTMnet; P84586; -.
DR PhosphoSitePlus; P84586; -.
DR jPOST; P84586; -.
DR PRIDE; P84586; -.
DR GeneID; 307779; -.
DR KEGG; rno:307779; -.
DR UCSC; RGD:1306751; rat.
DR CTD; 494115; -.
DR RGD; 1306751; Rbmxrtl.
DR InParanoid; P84586; -.
DR OrthoDB; 1248417at2759; -.
DR PhylomeDB; P84586; -.
DR TreeFam; TF331833; -.
DR PRO; PR:P84586; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISS:UniProtKB.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0044530; C:supraspliceosomal complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:UniProtKB.
DR GO; GO:0006376; P:mRNA splice site selection; IDA:UniProtKB.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR012604; RBM1CTR.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF08081; RBM1CTR; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Developmental protein; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome;
KW Transcription; Ubl conjugation.
FT CHAIN 1..388
FT /note="RNA-binding motif protein, X chromosome retrogene-
FT like"
FT /id="PRO_0000081856"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT CHAIN 2..388
FT /note="RNA-binding motif protein, X chromosome retrogene-
FT like, N-terminally processed"
FT /id="PRO_0000414744"
FT DOMAIN 8..86
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 61..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..164
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine; in RNA binding motif protein, X-
FT linked-like-1; alternate"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 2
FT /note="N-acetylvaline; in RNA binding motif protein, X-
FT linked-like-1, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96E39"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 122
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 141
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 161
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 169
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38159"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96E39"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38159"
SQ SEQUENCE 388 AA; 42204 MW; AFE8746592E44CF4 CRC64;
MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEILLM KDRETNKSRG FAFVTFESPA
DAKDVARDMN GKSLDGKAIK VEQATKPSFE SGRRGPPPPP RSRGPPRGLR GGSGGTRGPP
SRGGYMDDGG YSMNFNMSSS RGPLPVKRGP PPRSGGPPPK RSTPSGPVRS SSGMGGRTPV
SRGRDSYGGP PRREPLPSRR DVYLSPRDDG YSTKDSYSSR DYPSSRDTRD YAPPPRDYTY
RDYSHSSSRD DYPSRGYGDR DGYGRDREYS DHPSGGSYRD SYESYGNSRS APPTRGPPPS
YGGSSRYDDY SSSRDGYGGS RDSYSSSRSD LYSSGRDRVG RQERGLPPSM ERGYPPPRDS
YSSSSRGAPR GGGRGGSRSD RGGGRSRY
