SRA1_RAT
ID SRA1_RAT Reviewed; 219 AA.
AC Q6QGW5; Q811X7;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 110.
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|RGD:621148};
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] {ECO:0000305, ECO:0000312|EMBL:AAO45011.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH AR, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAO45011.1};
RC TISSUE=Prostate {ECO:0000312|EMBL:AAO45011.1};
RX PubMed=12350225; DOI=10.1042/bj20020743;
RA Kawashima H., Takano H., Sugita S., Takahara Y., Sugimura K., Nakatani T.;
RT "A novel steroid receptor co-activator protein (SRAP) as an alternative
RT form of steroid receptor RNA-activator gene: expression in prostate cancer
RT cells and enhancement of androgen receptor activity.";
RL Biochem. J. 369:163-171(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAS48375.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=15147866; DOI=10.1016/j.febslet.2004.03.104;
RA Chooniedass-Kothari S., Emberley E., Hamedani M.K., Troup S., Wang X.,
RA Czosnek A., Hube F., Mutawe M., Watson P.H., Leygue E.;
RT "The steroid receptor RNA activator is the first functional RNA encoding a
RT protein.";
RL FEBS Lett. 566:43-47(2004).
RN [3]
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: 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. {ECO:0000250|UniProtKB:Q9HD15,
CC ECO:0000269|PubMed:12350225}.
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:Q80VJ2,
CC ECO:0000250|UniProtKB:Q9HD15, ECO:0000269|PubMed:12350225}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HD15}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9HD15}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15147866};
CC IsoId=Q6QGW5-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q6QGW5-3; Sequence=VSP_061414, VSP_061415;
CC -!- TISSUE SPECIFICITY: Expressed in various prostate cancer cell lines.
CC {ECO:0000269|PubMed:12350225}.
CC -!- MISCELLANEOUS: Appears to be the first example of a new class of
CC functional RNAs also able to encode a protein. Rat SRAP1 may act as a
CC protein rather than an RNA transcript.
CC -!- SIMILARITY: Belongs to the SRA1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS48375.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY026354; AAO45011.1; -; mRNA.
DR EMBL; AY542868; AAS48375.1; ALT_INIT; mRNA.
DR RefSeq; NP_899158.3; NM_183329.3.
DR AlphaFoldDB; Q6QGW5; -.
DR STRING; 10116.ENSRNOP00000024671; -.
DR iPTMnet; Q6QGW5; -.
DR PhosphoSitePlus; Q6QGW5; -.
DR jPOST; Q6QGW5; -.
DR PaxDb; Q6QGW5; -.
DR GeneID; 252891; -.
DR KEGG; rno:252891; -.
DR UCSC; RGD:621148; rat. [Q6QGW5-1]
DR CTD; 10011; -.
DR RGD; 621148; Sra1.
DR eggNOG; ENOG502RZ38; Eukaryota.
DR InParanoid; Q6QGW5; -.
DR OrthoDB; 1577322at2759; -.
DR PhylomeDB; Q6QGW5; -.
DR PRO; PR:Q6QGW5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0031209; C:SCAR complex; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0016922; F:nuclear receptor binding; IPI:RGD.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:RGD.
DR GO; GO:0002153; F:steroid receptor RNA activator RNA binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
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:RGD.
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; ISO:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISS:UniProtKB.
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 Activator; Alternative splicing; Apoptosis; Cytoplasm; Nucleus;
KW Phosphoprotein; Receptor; Reference proteome; Ribonucleoprotein;
KW Transcription; Transcription regulation.
FT CHAIN 1..219
FT /note="Steroid receptor RNA activator 1"
FT /id="PRO_0000234107"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
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 COMPBIAS 205..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HD15"
FT VAR_SEQ 1..74
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12350225"
FT /id="VSP_061414"
FT VAR_SEQ 116
FT /note="K -> KK (in isoform 3)"
FT /id="VSP_061415"
SQ SEQUENCE 219 AA; 24114 MW; FEE3558D5202376C CRC64;
MAELYVKPGN KERGWNDPPQ FSYGLQTQTG GTKRTPLTKR VAAPQDGSPR APETSGPPPV
DHPPPSSKAS RPPPMGSCPA SGVDPPSSPV IESETLIEDV LRPLEQALED CRGHTKQVCD
DISRRLALLH EQWDGGKLSV PVKKRMALLV QELLHHQWDT ADDIHRSLMV DHVTEVSQWM
VGVKRLIAEK RSLSSEENKE EKSTVAPENQ TIPGFQPSS
