PSPC1_RAT
ID PSPC1_RAT Reviewed; 522 AA.
AC Q4KLH4;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Paraspeckle component 1;
GN Name=Pspc1;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408 AND SER-476, AND
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: Together with NONO, required for the formation of nuclear
CC paraspeckles. Regulates, cooperatively with NONO and SFPQ, androgen
CC receptor-mediated gene transcription activity in Sertoli cell line.
CC Binds to poly(A), poly(G) and poly(U) RNA homopolymers. Regulates the
CC circadian clock by repressing the transcriptional activator activity of
CC the CLOCK-ARNTL/BMAL1 heterodimer. Plays a role in the regulation of
CC DNA virus-mediated innate immune response by assembling into the HDP-
CC RNP complex, a complex that serves as a platform for IRF3
CC phosphorylation and subsequent innate immune response activation
CC through the cGAS-STING pathway. {ECO:0000250|UniProtKB:Q8WXF1}.
CC -!- SUBUNIT: Forms heterodimers with NONO; this involves formation of a
CC coiled coil domain by helices from both proteins. Found in a RNP
CC complex with CAT2 transcribed nuclear RNA (CTN-RNA). Interacts with
CC NONO and SFPQ. Interaction with NONO is required for its targeting to
CC paraspeckles and perinucleolar caps. Part of the HDP-RNP complex
CC composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins
CC (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA. Part of the HDP-
CC RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6,
CC paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1
CC RNA. {ECO:0000250|UniProtKB:Q8WXF1}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus matrix. Cytoplasm.
CC Nucleus speckle {ECO:0000250}. Note=In punctate subnuclear structures
CC localized adjacent to nuclear splicing speckles, called paraspeckles.
CC Colocalizes with NONO and SFPQ in paraspeckles and perinucleolar caps
CC in an RNA-dependent manner. May cycle between paraspeckles and
CC nucleolus. In telophase, when daughter nuclei form, localizes to
CC perinucleolar caps (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PSPC family. {ECO:0000305}.
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DR EMBL; BC099204; AAH99204.1; -; mRNA.
DR RefSeq; NP_001020843.1; NM_001025672.1.
DR AlphaFoldDB; Q4KLH4; -.
DR SMR; Q4KLH4; -.
DR BioGRID; 258303; 1.
DR STRING; 10116.ENSRNOP00000028219; -.
DR iPTMnet; Q4KLH4; -.
DR PhosphoSitePlus; Q4KLH4; -.
DR jPOST; Q4KLH4; -.
DR PaxDb; Q4KLH4; -.
DR PRIDE; Q4KLH4; -.
DR Ensembl; ENSRNOT00000028219; ENSRNOP00000028219; ENSRNOG00000020782.
DR GeneID; 305910; -.
DR KEGG; rno:305910; -.
DR UCSC; RGD:1310122; rat.
DR CTD; 55269; -.
DR RGD; 1310122; Pspc1.
DR eggNOG; KOG0115; Eukaryota.
DR GeneTree; ENSGT00940000157358; -.
DR InParanoid; Q4KLH4; -.
DR OMA; GDGYNQA; -.
DR OrthoDB; 1274880at2759; -.
DR PhylomeDB; Q4KLH4; -.
DR TreeFam; TF315795; -.
DR PRO; PR:Q4KLH4; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000020782; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; Q4KLH4; baseline and differential.
DR Genevisible; Q4KLH4; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042382; C:paraspeckles; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0002218; P:activation of innate immune response; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd12586; RRM1_PSP1; 1.
DR CDD; cd12589; RRM2_PSP1; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012975; NOPS.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034522; PSP1_RRM1.
DR InterPro; IPR034523; PSP1_RRM2.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF08075; NOPS; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Biological rhythms; Coiled coil; Cytoplasm;
KW Immunity; Innate immunity; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..522
FT /note="Paraspeckle component 1"
FT /id="PRO_0000297542"
FT DOMAIN 81..153
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 155..236
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 124..357
FT /note="Sufficient for paraspeckles localization"
FT /evidence="ECO:0000250"
FT REGION 230..357
FT /note="Sufficient for perinucleolar caps localization and
FT interaction with NONO"
FT /evidence="ECO:0000250"
FT REGION 459..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 282..376
FT /evidence="ECO:0000255"
FT COMPBIAS 469..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXF1"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXF1"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 506
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXF1"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXF1"
SQ SEQUENCE 522 AA; 58760 MW; 766E587063B87B53 CRC64;
MMLRGNLKQV RIEKNPARLR ALESAAGESE PVAAAAMALT LAGEQPPPPA PSEEHPDEEM
GFTIDIKSFL KPGEKTYTQR CRLFVGNLPT DITEEDFKRL FERYGEPSEV FINRDRGFGF
IRLESRTLAE IAKAELDGTI LKSRPLRIRF ATHGAALTVK NLSPVVSNEL LEQAFSQFGP
VEKAVVVVDD RGRATGKGFV EFAAKPPARK ALERCGDGAF LLTTTPRPVI VEPMEQFDDE
DGLPEKLMQK TQQYHKEREQ PPRFAQPGTF EFEYASRWKA LDEMEKQQRE QVDRNIREAK
EKLEAEMEAA RHEHQLMLMR QDLMRRQEEL RRLEELRNQE LQKRKQIQLR HEEEHRRREE
EMIRHREQEE LRRQQEGFKP NYMENREQEM RMGDMGPRGA INMGDAFSPA PAGTQGPPPM
MGMNMNNRGT IPGPPMGPGP AMGPEGAANM GTPMIPDNGA VHNDRFPQGP PSQMGSPMGN
RTGSETPQAP MSAVGPVSGG PGGFGRGSQG GNFEGPNKRR RY
