SLIRP_MOUSE
ID SLIRP_MOUSE Reviewed; 112 AA.
AC Q9D8T7; Q497G4; Q99JH3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=SRA stem-loop-interacting RNA-binding protein, mitochondrial;
DE Flags: Precursor;
GN Name=Slirp;
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] (ISOFORM 2).
RC TISSUE=Skeletal muscle;
RA Ievolella C., Zara I., Millino C., Faulkner G., Lanfranchi G.;
RT "Full length sequencing of some human and murine muscular transcripts
RT (Telethon Italy project B41).";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-112 (ISOFORM 1).
RC TISSUE=Pancreas;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104 AND SER-105, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, and
RC 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: RNA-binding protein that acts as a nuclear receptor
CC corepressor. Probably acts by binding the SRA RNA, and repressing the
CC SRA-mediated nuclear receptor coactivation. Binds the STR7 loop of SRA
CC RNA. Also able to repress glucocorticoid (GR), androgen (AR), thyroid
CC (TR) and VDR-mediated transactivation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Nucleus
CC {ECO:0000250}. Note=Predominantly mitochondrial. Some fraction is
CC nuclear. In the nucleus, it is recruited to nuclear receptor target
CC promoters (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D8T7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D8T7-2; Sequence=VSP_019907;
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC34586.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ293625; CAC34586.1; ALT_FRAME; mRNA.
DR EMBL; AK007699; BAB25197.1; -; mRNA.
DR EMBL; BC100567; AAI00568.1; -; mRNA.
DR CCDS; CCDS36503.1; -. [Q9D8T7-1]
DR RefSeq; NP_081234.2; NM_026958.3. [Q9D8T7-1]
DR AlphaFoldDB; Q9D8T7; -.
DR SMR; Q9D8T7; -.
DR BioGRID; 237642; 4.
DR IntAct; Q9D8T7; 1.
DR MINT; Q9D8T7; -.
DR STRING; 10090.ENSMUSP00000125341; -.
DR iPTMnet; Q9D8T7; -.
DR PhosphoSitePlus; Q9D8T7; -.
DR SwissPalm; Q9D8T7; -.
DR EPD; Q9D8T7; -.
DR jPOST; Q9D8T7; -.
DR MaxQB; Q9D8T7; -.
DR PaxDb; Q9D8T7; -.
DR PeptideAtlas; Q9D8T7; -.
DR PRIDE; Q9D8T7; -.
DR ProteomicsDB; 257196; -. [Q9D8T7-1]
DR ProteomicsDB; 257197; -. [Q9D8T7-2]
DR Antibodypedia; 13187; 119 antibodies from 21 providers.
DR DNASU; 380773; -.
DR Ensembl; ENSMUST00000160488; ENSMUSP00000124174; ENSMUSG00000021040. [Q9D8T7-2]
DR Ensembl; ENSMUST00000161023; ENSMUSP00000125341; ENSMUSG00000021040. [Q9D8T7-1]
DR GeneID; 380773; -.
DR KEGG; mmu:380773; -.
DR UCSC; uc007ojd.2; mouse. [Q9D8T7-1]
DR UCSC; uc007oje.2; mouse. [Q9D8T7-2]
DR CTD; 81892; -.
DR MGI; MGI:1916394; Slirp.
DR VEuPathDB; HostDB:ENSMUSG00000021040; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00390000008624; -.
DR HOGENOM; CLU_012062_28_10_1; -.
DR InParanoid; Q9D8T7; -.
DR OMA; RNRRPFA; -.
DR PhylomeDB; Q9D8T7; -.
DR TreeFam; TF319527; -.
DR BioGRID-ORCS; 380773; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Slirp; mouse.
DR PRO; PR:Q9D8T7; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9D8T7; protein.
DR Bgee; ENSMUSG00000021040; Expressed in facial nucleus and 266 other tissues.
DR ExpressionAtlas; Q9D8T7; baseline and differential.
DR Genevisible; Q9D8T7; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0036126; C:sperm flagellum; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:MGI.
DR GO; GO:0000961; P:negative regulation of mitochondrial RNA catabolic process; IGI:MGI.
DR GO; GO:0007338; P:single fertilization; IMP:MGI.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR CDD; cd12242; RRM_SLIRP; 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; IPR000504; RRM_dom.
DR InterPro; IPR034152; SLIRP_RRM.
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 Alternative splicing; Mitochondrion; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; RNA-binding; Transcription;
KW Transcription regulation; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..112
FT /note="SRA stem-loop-interacting RNA-binding protein,
FT mitochondrial"
FT /id="PRO_0000247052"
FT DOMAIN 19..98
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZT3"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT VAR_SEQ 89..112
FT /note="IHVQAQRAKALHGAQTSDEERFLR -> VSISDVCSTSL (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019907"
FT CONFLICT 51
FT /note="P -> H (in Ref. 2; BAB25197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 112 AA; 12605 MW; 3A03B372E1DA05DB CRC64;
MAASAIKGLS ALRSSTGRPI AFVRKIPWTA AASELREHFA QFGHVRRCTV PFDKETGFHR
GMGWVQFSSQ EELQNALQQE HHIIDGVKIH VQAQRAKALH GAQTSDEERF LR
