SRA1_MOUSE
ID SRA1_MOUSE Reviewed; 220 AA.
AC Q80VJ2; E9QM44; Q8R0S3; Q9CWU7; Q9D973;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 4.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Steroid receptor RNA activator 1 {ECO:0000305};
DE AltName: Full=Steroid receptor RNA activator protein;
DE Short=SRAP;
GN Name=Sra1 {ECO:0000312|MGI:MGI:1344414};
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] {ECO:0000305, ECO:0000312|EMBL:BAB26893.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB26893.1}, and
RC NOD {ECO:0000312|EMBL:BAE32451.1};
RC TISSUE=Embryonic stem cell {ECO:0000312|EMBL:BAB26893.1}, and
RC Testis {ECO:0000312|EMBL:BAB24943.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH48362.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH48362.1};
RC TISSUE=Eye {ECO:0000312|EMBL:AAH26480.1},
RC Mammary gland {ECO:0000312|EMBL:AAH48362.1}, and 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] {ECO:0000305}
RP IDENTIFICATION IN A COMPLEX WITH PUS1 AND RARG.
RX PubMed=15327771; DOI=10.1016/j.molcel.2004.06.044;
RA Zhao X., Patton J.R., Davis S.L., Florence B., Ames S.J., Spanjaard R.A.;
RT "Regulation of nuclear receptor activity by a pseudouridine synthase
RT through posttranscriptional modification of steroid receptor RNA
RT activator.";
RL Mol. Cell 15:549-558(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Liver, Lung, Pancreas, 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).
RN [6]
RP STRUCTURE BY NMR OF 87-195.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of mouse steroid receptor RNA activator 1 (SRA1)
RT protein.";
RL Submitted (APR-2008) to the PDB data bank.
CC -!- FUNCTION: Functional RNA which acts as a transcriptional coactivator
CC that selectively enhances steroid receptor-mediated transactivation
CC ligand-independently through a mechanism involving the modulating N-
CC terminal domain (AF-1) of steroid receptors. Also mediates
CC transcriptional coactivation of steroid receptors ligand-dependently
CC through the steroid-binding domain (AF-2). Enhances cellular
CC proliferation and differentiation and promotes apoptosis in vivo. May
CC play a role in tumorigenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q9HD15}.
CC -!- SUBUNIT: SRA1 RNA exists in a ribonucleoprotein complex containing
CC NCOA1. The RNA also forms a complex with PUS1 and RARG in the nucleus.
CC Interacts with AR. {ECO:0000250|UniProtKB:Q6QGW5,
CC ECO:0000250|UniProtKB:Q9HD15, ECO:0000269|PubMed:15327771}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HD15}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9HD15}.
CC -!- MISCELLANEOUS: Appears to be the first example of a new class of
CC functional RNAs also able to encode a protein.
CC {ECO:0000250|UniProtKB:Q9HD15}.
CC -!- SIMILARITY: Belongs to the SRA1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26480.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH26480.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC115631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK007302; BAB24943.1; -; mRNA.
DR EMBL; AK010375; BAB26893.1; -; mRNA.
DR EMBL; AK154232; BAE32451.1; -; mRNA.
DR EMBL; BC026480; AAH26480.1; ALT_SEQ; mRNA.
DR EMBL; BC048362; AAH48362.1; -; mRNA.
DR RefSeq; NP_001157878.1; NM_001164406.1.
DR RefSeq; NP_079567.2; NM_025291.3.
DR PDB; 2YRU; NMR; -; A=90-194.
DR PDBsum; 2YRU; -.
DR AlphaFoldDB; Q80VJ2; -.
DR BioGRID; 204880; 27.
DR STRING; 10090.ENSMUSP00000133360; -.
DR iPTMnet; Q80VJ2; -.
DR PhosphoSitePlus; Q80VJ2; -.
DR REPRODUCTION-2DPAGE; IPI00317966; -.
DR EPD; Q80VJ2; -.
DR MaxQB; Q80VJ2; -.
DR PaxDb; Q80VJ2; -.
DR PeptideAtlas; Q80VJ2; -.
DR PRIDE; Q80VJ2; -.
DR ProteomicsDB; 257392; -.
DR Antibodypedia; 26969; 215 antibodies from 32 providers.
DR DNASU; 24068; -.
DR GeneID; 24068; -.
DR KEGG; mmu:24068; -.
DR UCSC; uc008eny.2; mouse.
DR CTD; 10011; -.
DR MGI; MGI:1344414; Sra1.
DR VEuPathDB; HostDB:ENSMUSG00000006050; -.
DR eggNOG; ENOG502RZ38; Eukaryota.
DR InParanoid; Q80VJ2; -.
DR OMA; KDRGWND; -.
DR OrthoDB; 1577322at2759; -.
DR TreeFam; TF314789; -.
DR BioGRID-ORCS; 24068; 1 hit in 60 CRISPR screens.
DR ChiTaRS; Sra1; mouse.
DR EvolutionaryTrace; Q80VJ2; -.
DR PRO; PR:Q80VJ2; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q80VJ2; protein.
DR Bgee; ENSMUSG00000006050; Expressed in right kidney and 270 other tissues.
DR ExpressionAtlas; Q80VJ2; baseline and differential.
DR Genevisible; Q80VJ2; MM.
DR GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0031209; C:SCAR complex; ISO:MGI.
DR GO; GO:0005831; C:steroid hormone aporeceptor complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:MGI.
DR GO; GO:0002153; F:steroid receptor RNA activator RNA binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; ISO:MGI.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR IDEAL; IID50292; -.
DR InterPro; IPR009917; SRA1/Sec31.
DR InterPro; IPR040243; Steroid_recept_RNA_1.
DR PANTHER; PTHR18834; PTHR18834; 1.
DR Pfam; PF07304; SRA1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Apoptosis; Cytoplasm; Nucleus; Phosphoprotein;
KW Receptor; Reference proteome; Ribonucleoprotein; Transcription;
KW Transcription regulation.
FT CHAIN 1..220
FT /note="Steroid receptor RNA activator 1"
FT /id="PRO_0000234106"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HD15"
FT CONFLICT 15
FT /note="W -> G (in Ref. 1; BAB24943)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="A -> V (in Ref. 3; AAH48362)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="H -> Y (in Ref. 3; AAH48362)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="K -> R (in Ref. 3; AAH48362)"
FT /evidence="ECO:0000305"
FT HELIX 97..112
FT /evidence="ECO:0007829|PDB:2YRU"
FT HELIX 117..136
FT /evidence="ECO:0007829|PDB:2YRU"
FT HELIX 141..156
FT /evidence="ECO:0007829|PDB:2YRU"
FT HELIX 159..171
FT /evidence="ECO:0007829|PDB:2YRU"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:2YRU"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:2YRU"
FT HELIX 181..194
FT /evidence="ECO:0007829|PDB:2YRU"
SQ SEQUENCE 220 AA; 24325 MW; 3BFCB2B7A7ED6563 CRC64;
MAELYVKPGN KERGWNDPPQ FSYGLQTQTG GPKRTPLTKR VAAPQDGSPR APETSGPPPV
DHPPPSSKAS RPPPMGSCPA TGVEPPSSPV IESETLIEDV LRPLEQALED CHGHTKKQVC
DDISRRLALL REQWAGGKLS IPVKKRMALL VQELLHHQWD AADDIHRSLM VDHVTEVSQW
MVGVKRLIAE KKSLSSEETK EEKFTVEPEN QTIPGFQQPS
