P84586 (RMXRL_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RNA-binding motif protein, X chromosome retrogene-like

Alternative name(s):
Heterogeneous nuclear ribonucleoprotein G retrogene-like
Short name=hnRNP G
RNA-binding motif protein, X chromosome retrogene

Cleaved into the following chain:

1. RNA-binding motif protein, X chromosome retrogene-like, N-terminally processed

Gene names

Name:

Rbmxrtl

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	388 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of pre-mRNAs. Associates with chromatin. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Binds non-specifically to pre-mRNAs By similarity.
Subcellular location	Nucleus By similarity. Note: Component of ribonucleosomes By similarity.
Sequence similarities	Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Biological process	Transcription mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Ligand	RNA-binding
Molecular function	Developmental protein Ribonucleoprotein
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to interleukin-1 Inferred from sequence or structural similarity. Source: UniProtKB mRNA splice site selection Inferred from direct assay PubMed 19282290. Source: UniProtKB membrane protein ectodomain proteolysis Inferred from sequence or structural similarity. Source: UniProtKB multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of mRNA splicing, via spliceosome Inferred from direct assay PubMed 15009664. Source: UniProtKB positive regulation of mRNA splicing, via spliceosome Inferred from direct assay PubMed 19282290. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB protein homooligomerization Inferred from direct assay PubMed 19282290. Source: UniProtKB regulation of alternative mRNA splicing, via spliceosome Inferred from direct assay PubMed 19282290. Source: UniProtKB transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	catalytic step 2 spliceosome Inferred from sequence or structural similarity. Source: UniProtKB extracellular vesicular exosome Inferred from sequence or structural similarity. Source: UniProtKB nuclear euchromatin Inferred from sequence or structural similarity. Source: UniProtKB supraspliceosomal complex Inferred from direct assay PubMed 19282290. Source: UniProtKB
Molecular_function	mRNA binding Inferred from sequence or structural similarity. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 388	388	RNA-binding motif protein, X chromosome retrogene-like		PRO_0000081856
	Initiator methionine	1	1	Removed; alternate By similarity
	Chain	2 – 388	387	RNA-binding motif protein, X chromosome retrogene-like, N-terminally processed		PRO_0000414744
Regions
	Domain	8 – 86	79	RRM
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine; in RNA binding motif protein, X-linked-like-1; alternate By similarity
	Modified residue	2	1	N-acetylvaline; in RNA binding motif protein, X-linked-like-1, N-terminally processed By similarity

Sequences

	Sequence		Length	Mass (Da)
	P84586 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: AFE8746592E44CF4	FASTA	388	42,204
	10 20 30 40 50 60 MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEILLM KDRETNKSRG FAFVTFESPA 70 80 90 100 110 120 DAKDVARDMN GKSLDGKAIK VEQATKPSFE SGRRGPPPPP RSRGPPRGLR GGSGGTRGPP 130 140 150 160 170 180 SRGGYMDDGG YSMNFNMSSS RGPLPVKRGP PPRSGGPPPK RSTPSGPVRS SSGMGGRTPV 190 200 210 220 230 240 SRGRDSYGGP PRREPLPSRR DVYLSPRDDG YSTKDSYSSR DYPSSRDTRD YAPPPRDYTY 250 260 270 280 290 300 RDYSHSSSRD DYPSRGYGDR DGYGRDREYS DHPSGGSYRD SYESYGNSRS APPTRGPPPS 310 320 330 340 350 360 YGGSSRYDDY SSSRDGYGGS RDSYSSSRSD LYSSGRDRVG RQERGLPPSM ERGYPPPRDS 370 380 YSSSSRGAPR GGGRGGSRSD RGGGRSRY

References

[1]

"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AABR03113401 Genomic DNA. No translation available.
IPI	IPI00559910.
RefSeq	NP_001100890.1. NM_001107420.1.
UniGene	Rn.19966.
3D structure databases
ProteinModelPortal	P84586.
SMR	P84586. Positions 1-105.
ModBase	Search...
PTM databases
PhosphoSite	P84586.
Proteomic databases
PaxDb	P84586.
PRIDE	P84586.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	307779.
KEGG	rno:307779.
UCSC	RGD:1306751. rat.
Organism-specific databases
CTD	307779.
RGD	1306751. Rbmxrtl.
Phylogenomic databases
eggNOG	COG0724.
HOGENOM	HOG000276235.
HOVERGEN	HBG063314.
InParanoid	P84586.
KO	K12885.
OMA	ILLMKDR.
OrthoDB	EOG4001KF.
Gene expression databases
Genevestigator	P84586.
GermOnline	ENSRNOG00000012138. Rattus norvegicus.
Family and domain databases
Gene3D	3.30.70.330. 1 hit.
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR012604. RBM1CTR. IPR000504. RRM_dom. [Graphical view]
Pfam	PF08081. RBM1CTR. 1 hit. PF00076. RRM_1. 1 hit. [Graphical view]
SMART	SM00360. RRM. 1 hit. [Graphical view]
PROSITE	PS50102. RRM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	657858.

Entry information

Entry name

RMXRL_RAT

Accession

Primary (citable) accession number: P84586

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program