GRSF1_MOUSE
ID GRSF1_MOUSE Reviewed; 479 AA.
AC Q8C5Q4; Q8BR05; Q8BRG7;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=G-rich sequence factor 1;
DE Short=GRSF-1;
DE Flags: Precursor;
GN Name=Grsf1;
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=Corpora quadrigemina, and Thymus;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Regulator of post-transcriptional mitochondrial gene
CC expression, required for assembly of the mitochondrial ribosome and for
CC recruitment of mRNA and lncRNA. Binds RNAs containing the 14 base G-
CC rich element. Preferentially binds RNAs transcribed from three
CC contiguous genes on the light strand of mtDNA, the ND6 mRNA, and the
CC long non-coding RNAs for MT-CYB and MT-ND5, each of which contains
CC multiple consensus binding sequences. Involved in the degradosome-
CC mediated decay of non-coding mitochondrial transcripts (MT-ncRNA) and
CC tRNA-like molecules. Acts by unwinding G-quadruplex RNA structures in
CC MT-ncRNA, thus facilitating their degradation by the degradosome. G-
CC quadruplexes (G4) are non-canonical 4 stranded structures formed by
CC transcripts from the light strand of mtDNA.
CC {ECO:0000250|UniProtKB:Q12849}.
CC -!- SUBUNIT: Monomer. Found in a complex with DDX28, DHX30, FASTKD2 and
CC FASTKD5. Interacts with the mitochondrial RNase P complex subunit
CC TRMT10C/MRPP1. Interacts with the 2 components of the mitochondrial
CC degradosome complex, PNPT1 and SUPV3L1, in an RNA-dependent manner.
CC {ECO:0000250|UniProtKB:Q12849}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q12849}. Note=Localizes to mitochondrial RNA
CC granules found in close proximity to the mitochondrial nucleoids.
CC {ECO:0000250|UniProtKB:Q12849}.
CC -!- DOMAIN: The RRM domains mediate RNA-binding.
CC {ECO:0000250|UniProtKB:Q12849}.
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DR EMBL; AK044889; BAC32129.1; -; mRNA.
DR EMBL; AK045986; BAC32561.1; -; mRNA.
DR EMBL; AK077782; BAC37006.1; -; mRNA.
DR CCDS; CCDS19404.1; -.
DR RefSeq; NP_001091946.1; NM_001098476.2.
DR RefSeq; NP_848815.2; NM_178700.5.
DR AlphaFoldDB; Q8C5Q4; -.
DR SMR; Q8C5Q4; -.
DR BioGRID; 231118; 16.
DR IntAct; Q8C5Q4; 1.
DR STRING; 10090.ENSMUSP00000077972; -.
DR iPTMnet; Q8C5Q4; -.
DR PhosphoSitePlus; Q8C5Q4; -.
DR EPD; Q8C5Q4; -.
DR MaxQB; Q8C5Q4; -.
DR PaxDb; Q8C5Q4; -.
DR PeptideAtlas; Q8C5Q4; -.
DR PRIDE; Q8C5Q4; -.
DR ProteomicsDB; 271460; -.
DR Antibodypedia; 24367; 160 antibodies from 21 providers.
DR DNASU; 231413; -.
DR Ensembl; ENSMUST00000078945; ENSMUSP00000077972; ENSMUSG00000044221.
DR GeneID; 231413; -.
DR KEGG; mmu:231413; -.
DR UCSC; uc008yac.2; mouse.
DR CTD; 2926; -.
DR MGI; MGI:106479; Grsf1.
DR VEuPathDB; HostDB:ENSMUSG00000044221; -.
DR eggNOG; KOG4211; Eukaryota.
DR GeneTree; ENSGT00940000158529; -.
DR HOGENOM; CLU_032003_0_1_1; -.
DR InParanoid; Q8C5Q4; -.
DR OMA; DIINFFM; -.
DR OrthoDB; 603679at2759; -.
DR PhylomeDB; Q8C5Q4; -.
DR TreeFam; TF316157; -.
DR BioGRID-ORCS; 231413; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Grsf1; mouse.
DR PRO; PR:Q8C5Q4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8C5Q4; protein.
DR Bgee; ENSMUSG00000044221; Expressed in primitive streak and 257 other tissues.
DR ExpressionAtlas; Q8C5Q4; baseline and differential.
DR Genevisible; Q8C5Q4; MM.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0035770; C:ribonucleoprotein granule; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000962; P:positive regulation of mitochondrial RNA catabolic process; ISO:MGI.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd12730; RRM1_GRSF1; 1.
DR CDD; cd12505; RRM2_GRSF1; 1.
DR CDD; cd12733; RRM3_GRSF1; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR034424; GRSF-1_RRM2.
DR InterPro; IPR033106; GRSF1.
DR InterPro; IPR034425; GRSF1_RRM1.
DR InterPro; IPR034426; GRSF1_RRM3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR13976:SF42; PTHR13976:SF42; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Mitochondrion; mRNA processing; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Transit peptide; tRNA processing.
FT TRANSIT 1..116
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 117..479
FT /note="G-rich sequence factor 1"
FT /id="PRO_0000081598"
FT DOMAIN 149..245
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 249..325
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 400..479
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12849"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12849"
FT CONFLICT 15
FT /note="C -> Y (in Ref. 1; BAC37006)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="A -> T (in Ref. 1; BAC37006)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="S -> C (in Ref. 1; BAC32561)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="R -> T (in Ref. 1; BAC37006)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 53076 MW; 4203BA99671C7BF1 CRC64;
MAGTRWVLGA LLRGCGCNCS SCRRTGAACL PFYSAAGTFP SGVSGRRRLL LLLGAAAAAA
SQTRGLQLGP AAAGRLAGPI PARPSAAAAA AASYSALRAP LFPRSLAAAA GPARGYSQES
KTTYLEDLPP LPEYELSPSK LGDEVDDVYL IRAQGLPWSC TVEDVLNFFS DCRIRNSENG
IHFLLNRDGK RRGDALIEME SEQDVQKALE KHRMYMGQRY VEVYEINNED VDALMKSLQV
KPSPVLSDGV VRLRGLPYSC NEKDIVDFFA GLNIVDITFV MDYRGRRKTG EAYVQFEEPE
MANQALLKHR EEIGNRYIEI FPSRRNEVRT HVGSHKGKKM TSSPPTKYIT EPEVVFEEHE
VNEDIRPMTA FESDKEIELP KEMSEKLPEA VDFGTLPSLH FVHMRGLPFQ ANAQDIINFF
APLKPVRITM EYSSSGKATG EADVHFDTHE DAVAAMLKDR SHVQHRYIEL FLNSCPKGK
