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PSPC1_BOVIN
ID   PSPC1_BOVIN             Reviewed;         520 AA.
AC   Q1LZD9;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Paraspeckle component 1;
GN   Name=PSPC1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}. Nucleus matrix {ECO:0000250}. Nucleus speckle
CC       {ECO:0000250}. Note=In punctate subnuclear structures localized
CC       adjacent to nuclear splicing speckles, called paraspeckles. Colocalizes
CC       with NONO and SFPQ in paraspeckles and perinucleolar caps in an RNA-
CC       dependent manner. May cycle between paraspeckles and nucleolus. In
CC       telophase, when daughter nuclei form, localizes to perinucleolar caps
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PSPC family. {ECO:0000305}.
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DR   EMBL; BC116062; AAI16063.1; -; mRNA.
DR   RefSeq; NP_001068745.1; NM_001075277.1.
DR   AlphaFoldDB; Q1LZD9; -.
DR   SMR; Q1LZD9; -.
DR   STRING; 9913.ENSBTAP00000005134; -.
DR   PaxDb; Q1LZD9; -.
DR   PRIDE; Q1LZD9; -.
DR   Ensembl; ENSBTAT00000005134; ENSBTAP00000005134; ENSBTAG00000003934.
DR   GeneID; 506696; -.
DR   KEGG; bta:506696; -.
DR   CTD; 55269; -.
DR   VEuPathDB; HostDB:ENSBTAG00000003934; -.
DR   VGNC; VGNC:33482; PSPC1.
DR   eggNOG; KOG0115; Eukaryota.
DR   GeneTree; ENSGT00940000157358; -.
DR   HOGENOM; CLU_027185_2_1_1; -.
DR   InParanoid; Q1LZD9; -.
DR   OMA; GDGYNQA; -.
DR   OrthoDB; 1274880at2759; -.
DR   TreeFam; TF315795; -.
DR   Proteomes; UP000009136; Chromosome 12.
DR   Bgee; ENSBTAG00000003934; Expressed in spermatocyte and 107 other tissues.
DR   ExpressionAtlas; Q1LZD9; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0042382; C:paraspeckles; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0002218; P:activation of innate immune response; IEA:Ensembl.
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   2: Evidence at transcript 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..520
FT                   /note="Paraspeckle component 1"
FT                   /id="PRO_0000297539"
FT   DOMAIN          79..151
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          153..234
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          122..355
FT                   /note="Sufficient for paraspeckles localization"
FT                   /evidence="ECO:0000250"
FT   REGION          228..355
FT                   /note="Sufficient for perinucleolar caps localization and
FT                   interaction with NONO"
FT                   /evidence="ECO:0000250"
FT   REGION          457..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          280..374
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        467..489
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         406
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WXF1"
FT   MOD_RES         470
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WXF1"
FT   MOD_RES         474
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WXF1"
FT   MOD_RES         504
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WXF1"
FT   MOD_RES         506
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WXF1"
SQ   SEQUENCE   520 AA;  58275 MW;  42297292FE0C2A60 CRC64;
     MMLRGNLKQV RIEKNPARLR ALESAAGEGD PAALALALPG EPPVPAAPAG EDRPADEGGF
     TIDIKSFLKP GEKTYTQRCR LFVGNLPTDI TEDDFKRLFE RYGEPSEVFI NRDRGFGFIR
     LESRTLAEIA KAELDGTILK SRPLRIRFAT HGAALTVKNL SPVVSNELLE QAFSQFGPVE
     KAVVVVDDRG RATGKGFVEF AAKPPARKAL ERCGDGAFLL TTTPRPVIVE PMEQFDDEDG
     LPEKLMQKTQ QYHKEREQPP RFAQPGTFEF EYASRWKALD EMEKQQREQV DRNIREAKEK
     LEAEMEAARH EHQLMLMRQD LMRRQEELRR LEELRNQELQ KRKQIQLRHE EEHRRREEEM
     IRHREQEELR RQQEGFKPNY MENREQEMRM GDMGPRGAIN MGDAFSPAPA GNQGPPAMMG
     MNMNNRGTIP GPPMGPGPAM GPEGAANMGT PMMPDNGAVH NDRFPQGPPS QMGSPMGSRT
     GSETPQAPMS GVGPVSGGPG GFGRGSQGAN FEGPNKRRRY
 
 
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