PSPC1_MOUSE
ID PSPC1_MOUSE Reviewed; 523 AA.
AC Q8R326; Q3TUK2; Q9CYH1; Q9D0M8;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Paraspeckle component 1;
DE AltName: Full=Paraspeckle protein 1;
DE Short=mPSP1;
GN Name=Pspc1; Synonyms=Psp1;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Head;
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 MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP INTERACTION WITH NONO AND SFPQ, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15140795; DOI=10.1095/biolreprod.104.028159;
RA Myojin R., Kuwahara S., Yasaki T., Matsunaga T., Sakurai T., Kimura M.,
RA Uesugi S., Kurihara Y.;
RT "Expression and functional significance of mouse paraspeckle protein 1 on
RT spermatogenesis.";
RL Biol. Reprod. 71:926-932(2004).
RN [4]
RP IDENTIFICATION IN A RNP COMPLEX WITH CTN-RNA.
RX PubMed=16239143; DOI=10.1016/j.cell.2005.08.033;
RA Prasanth K.V., Prasanth S.G., Xuan Z., Hearn S., Freier S.M., Bennett C.F.,
RA Zhang M.Q., Spector D.L.;
RT "Regulating gene expression through RNA nuclear retention.";
RL Cell 123:249-263(2005).
RN [5]
RP FUNCTION, INTERACTION WITH NONO AND SFPQ, MUTAGENESIS OF PHE-118; PHE-120;
RP LYS-197 AND PHE-199, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16641145; DOI=10.1095/biolreprod.106.051136;
RA Kuwahara S., Ikei A., Taguchi Y., Tabuchi Y., Fujimoto N., Obinata M.,
RA Uesugi S., Kurihara Y.;
RT "PSPC1, NONO, and SFPQ are expressed in mouse Sertoli cells and may
RT function as coregulators of androgen receptor-mediated transcription.";
RL Biol. Reprod. 75:352-359(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, 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 [7]
RP FUNCTION.
RX PubMed=22966205; DOI=10.1128/mcb.00334-12;
RA Kowalska E., Ripperger J.A., Muheim C., Maier B., Kurihara Y., Fox A.H.,
RA Kramer A., Brown S.A.;
RT "Distinct roles of DBHS family members in the circadian transcriptional
RT feedback loop.";
RL Mol. Cell. Biol. 32:4585-4594(2012).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-507, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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 ECO:0000269|PubMed:16641145, ECO:0000269|PubMed:22966205}.
CC -!- SUBUNIT: Forms heterodimers with NONO; this involves formation of a
CC coiled coil domain by helices from both proteins (By similarity).
CC Interaction with NONO is required for its targeting to paraspeckles and
CC perinucleolar caps (By similarity). Found in a RNP complex with CAT2
CC transcribed nuclear RNA (CTN-RNA). Interacts with NONO and SFPQ. Part
CC of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5,
CC XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and
CC NEAT1 RNA. {ECO:0000250|UniProtKB:Q8WXF1, ECO:0000269|PubMed:15140795,
CC ECO:0000269|PubMed:16239143, ECO:0000269|PubMed:16641145}.
CC -!- INTERACTION:
CC Q8R326; O88609: Lmx1b; NbExp=3; IntAct=EBI-309927, EBI-13951208;
CC Q8R326; Q8VIJ6: Sfpq; NbExp=2; IntAct=EBI-309927, EBI-6094576;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Note=In
CC punctate subnuclear structures localized adjacent to nuclear splicing
CC speckles, called paraspeckles. Colocalizes with NONO and SFPQ in
CC paraspeckles and perinucleolar caps in an RNA-dependent manner. May
CC cycle between paraspeckles and nucleolus. In telophase, when daughter
CC nuclei form, localizes to perinucleolar caps. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus matrix. Cytoplasm. Nucleus
CC speckle {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PSP1-alpha;
CC IsoId=Q8R326-1; Sequence=Displayed;
CC Name=2; Synonyms=PSP1-beta;
CC IsoId=Q8R326-2; Sequence=VSP_027276, VSP_027277;
CC -!- TISSUE SPECIFICITY: Isoform 1 is strongly expressed in testis (leptoten
CC spermatocytes, round spematids and Sertoli cells) and moderately in
CC cerebrum, cerebellum, lung, spleen and ovary (at protein level).
CC Isoform 2 is strongly expressed in kidney and moderately in salivary
CC gland (at protein level). {ECO:0000269|PubMed:15140795,
CC ECO:0000269|PubMed:16641145}.
CC -!- SIMILARITY: Belongs to the PSPC family. {ECO:0000305}.
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DR EMBL; AK011272; BAB27509.2; -; mRNA.
DR EMBL; AK017689; BAB30876.2; -; mRNA.
DR EMBL; AK150823; BAE29885.1; -; mRNA.
DR EMBL; AK160722; BAE35969.1; -; mRNA.
DR EMBL; BC026772; AAH26772.1; -; mRNA.
DR CCDS; CCDS27151.1; -. [Q8R326-1]
DR RefSeq; NP_079958.3; NM_025682.3. [Q8R326-1]
DR AlphaFoldDB; Q8R326; -.
DR SMR; Q8R326; -.
DR BioGRID; 211618; 44.
DR IntAct; Q8R326; 6.
DR MINT; Q8R326; -.
DR STRING; 10090.ENSMUSP00000022507; -.
DR iPTMnet; Q8R326; -.
DR PhosphoSitePlus; Q8R326; -.
DR EPD; Q8R326; -.
DR MaxQB; Q8R326; -.
DR PaxDb; Q8R326; -.
DR PeptideAtlas; Q8R326; -.
DR PRIDE; Q8R326; -.
DR ProteomicsDB; 301999; -. [Q8R326-1]
DR ProteomicsDB; 302000; -. [Q8R326-2]
DR Antibodypedia; 22257; 71 antibodies from 20 providers.
DR DNASU; 66645; -.
DR Ensembl; ENSMUST00000022507; ENSMUSP00000022507; ENSMUSG00000021938. [Q8R326-1]
DR Ensembl; ENSMUST00000163924; ENSMUSP00000133038; ENSMUSG00000021938. [Q8R326-2]
DR GeneID; 66645; -.
DR KEGG; mmu:66645; -.
DR UCSC; uc007ucj.1; mouse. [Q8R326-1]
DR UCSC; uc007uck.1; mouse. [Q8R326-2]
DR CTD; 55269; -.
DR MGI; MGI:1913895; Pspc1.
DR VEuPathDB; HostDB:ENSMUSG00000021938; -.
DR eggNOG; KOG0115; Eukaryota.
DR GeneTree; ENSGT00940000157358; -.
DR HOGENOM; CLU_027185_2_1_1; -.
DR InParanoid; Q8R326; -.
DR OMA; GDGYNQA; -.
DR OrthoDB; 1274880at2759; -.
DR PhylomeDB; Q8R326; -.
DR TreeFam; TF315795; -.
DR BioGRID-ORCS; 66645; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Pspc1; mouse.
DR PRO; PR:Q8R326; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8R326; protein.
DR Bgee; ENSMUSG00000021938; Expressed in embryonic post-anal tail and 260 other tissues.
DR ExpressionAtlas; Q8R326; baseline and differential.
DR Genevisible; Q8R326; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042382; C:paraspeckles; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0002218; P:activation of innate immune response; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP: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; Alternative splicing; Biological rhythms;
KW Coiled coil; Cytoplasm; Immunity; Innate immunity; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding;
KW Transcription; Transcription regulation.
FT CHAIN 1..523
FT /note="Paraspeckle component 1"
FT /id="PRO_0000297541"
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 460..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 282..376
FT /evidence="ECO:0000255"
FT COMPBIAS 470..492
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 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXF1"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXF1"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXF1"
FT MOD_RES 507
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXF1"
FT VAR_SEQ 463..466
FT /note="HNDR -> VMYH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027276"
FT VAR_SEQ 467..523
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027277"
FT MUTAGEN 118
FT /note="F->A: Abolishes RNA-binding activity but not AR-
FT mediated transcription coactivation; when associated with
FT A-120; A-197 and A-199."
FT /evidence="ECO:0000269|PubMed:16641145"
FT MUTAGEN 120
FT /note="F->A: Abolishes RNA-binding activity but not AR-
FT mediated transcription coactivation; when associated with
FT A-118; A-197 and A-199."
FT /evidence="ECO:0000269|PubMed:16641145"
FT MUTAGEN 197
FT /note="K->A: Abolishes RNA-binding activity but not AR-
FT mediated transcription coactivation; when associated with
FT A-118; A-120 and A-199."
FT /evidence="ECO:0000269|PubMed:16641145"
FT MUTAGEN 199
FT /note="F->A: Abolishes RNA-binding activity but not AR-
FT mediated transcription coactivation; when associated with
FT A-118; A-120 and A-197."
FT /evidence="ECO:0000269|PubMed:16641145"
FT CONFLICT 349
FT /note="L -> Q (in Ref. 1; BAB30876)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 58758 MW; 1F6804934C98432B CRC64;
MMLRGNLKQV RIEKNPARLR ALESAAGESE PVAAAAMALT LAGEQAPPPA PSEEHPDEEL
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 LRRQQEGGFK PNYMENREQE MRMGDMGPRG AINMGDAFSP APAGTQGPPP
MMGMNMNNRG TIPGPPMGPG PAMGPEGAAN MGTPMIPDNG AVHNDRFPQG PPSQMGSPMG
NRTGSETPQA PMSGVGPVSG GPGGFGRGSQ GGNFEGPNKR RRY
