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PSPC1_DANRE
ID   PSPC1_DANRE             Reviewed;         512 AA.
AC   Q1JPY8;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Paraspeckle component 1;
GN   Name=pspc1; ORFNames=zgc:136470;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Together with NONO, required for the formation of nuclear
CC       paraspeckles. Acts as a coactivator during transcriptional activation.
CC       Binds to RNA. May act as a regulator the circadian clock (By
CC       similarity). {ECO:0000250}.
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.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PSPC family. {ECO:0000305}.
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DR   EMBL; BC116549; AAI16550.1; -; mRNA.
DR   RefSeq; NP_001038723.1; NM_001045258.1.
DR   AlphaFoldDB; Q1JPY8; -.
DR   SMR; Q1JPY8; -.
DR   STRING; 7955.ENSDARP00000093111; -.
DR   PaxDb; Q1JPY8; -.
DR   PRIDE; Q1JPY8; -.
DR   Ensembl; ENSDART00000102335; ENSDARP00000093111; ENSDARG00000006621.
DR   GeneID; 692285; -.
DR   KEGG; dre:692285; -.
DR   CTD; 55269; -.
DR   ZFIN; ZDB-GENE-030131-9530; pspc1.
DR   eggNOG; KOG0115; Eukaryota.
DR   GeneTree; ENSGT00940000157358; -.
DR   InParanoid; Q1JPY8; -.
DR   OrthoDB; 1274880at2759; -.
DR   PhylomeDB; Q1JPY8; -.
DR   TreeFam; TF315795; -.
DR   PRO; PR:Q1JPY8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 1.
DR   Bgee; ENSDARG00000006621; Expressed in mature ovarian follicle and 26 other tissues.
DR   ExpressionAtlas; Q1JPY8; baseline and differential.
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:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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   Activator; Biological rhythms; Coiled coil; Cytoplasm; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; RNA-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..512
FT                   /note="Paraspeckle component 1"
FT                   /id="PRO_0000297544"
FT   DOMAIN          76..148
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          150..231
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          276..366
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   512 AA;  57698 MW;  F9D97F78F211FFBD CRC64;
     MANPNLKQVN IQNNATFPHQ QNVTRSTESP GDPKETMEAV APSPQDPSSA NSEPQEMTVD
     IKNFRRPGEK TFTQRCRLFV GNLPSDMADE DFKKLFFKYG DAKEVFINRD RGFGFIRLET
     RTLAEIAKAE LDGTVLGNRP IRIRFATHGA ALTVRNLSPV VSNELLEQAF SQFGPVERAI
     VIVDDRGRPT GKGIVEFANK PAARKALDHC ADGALLLTTS PRPVILEPTE QYDDEDGLPE
     KLLQKSAQYH KEREHKPHFA QPGTFEFEYS SRWKALDEMD KQQREQVERN IQEAKEKLET
     EMEAAKQEHQ LMMMRQDLMR RQEELRRLEE LRNQELQKRK QIELRHEEER RRREEDMIRH
     REQLDIRRQP DGFKSGFMES REQDMRMNEM GTRGAINIGD SFNPVTAISG NQGPTQMMGM
     GGRVGAMGPD GSSKMIPDNG VMPNERFSEG GPLQMGSPVG GQTGVDSPQP QQHSPMLVGA
     GSVPGVLGQS GFGRGSPVGG SFDGPNNKRR RY
 
 
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