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RBM8A_SALSA
ID   RBM8A_SALSA             Reviewed;         175 AA.
AC   B5DGI7; B9EPG0;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=RNA-binding protein 8A;
DE   AltName: Full=RNA-binding motif protein 8A;
DE   AltName: Full=Ribonucleoprotein RBM8A;
GN   Name=rbm8a; Synonyms=rbm8;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=White muscle;
RA   Andreassen R., Hoyheim B.;
RT   "Characterization of full-length sequenced inserts (FLIcs) from a salmo
RT   salar white muscle specific cDNA library.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus, and Thyroid;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
CC   -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC       spliceosome (By similarity). Core component of the splicing-dependent
CC       multiprotein exon junction complex (EJC) deposited at splice junctions
CC       on mRNAs. The EJC is a dynamic structure consisting of core proteins
CC       and several peripheral nuclear and cytoplasmic associated factors that
CC       join the complex only transiently either during EJC assembly or during
CC       subsequent mRNA metabolism. The EJC marks the position of the exon-exon
CC       junction in the mature mRNA for the gene expression machinery and the
CC       core components remain bound to spliced mRNAs throughout all stages of
CC       mRNA metabolism thereby influencing downstream processes including
CC       nuclear mRNA export, subcellular mRNA localization, translation
CC       efficiency and nonsense-mediated mRNA decay (NMD). Its removal from
CC       cytoplasmic mRNAs requires translation initiation from EJC-bearing
CC       spliced mRNAs. Associates preferentially with mRNAs produced by
CC       splicing. Does not interact with pre-mRNAs, introns, or mRNAs produced
CC       from intronless cDNAs. Associates with both nuclear mRNAs and newly
CC       exported cytoplasmic mRNAs (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y5S9}.
CC   -!- SUBUNIT: Part of the EJC core complex that contains casc3, eif4a3,
CC       magoh and rbm8a. Identified in the spliceosome C complex.
CC       {ECO:0000250|UniProtKB:Q9Y5S9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y5S9}. Nucleus
CC       speckle {ECO:0000250|UniProtKB:Q9Y5S9}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9Y5S9}. Note=Nucleocytoplasmic shuttling
CC       protein. Travels to the cytoplasm as part of the exon junction complex
CC       (EJC) bound to mRNA. {ECO:0000250|UniProtKB:Q9Y5S9}.
CC   -!- SIMILARITY: Belongs to the RBM8A family. {ECO:0000305}.
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DR   EMBL; BT043746; ACH70861.1; -; mRNA.
DR   EMBL; BT057056; ACM08928.1; -; mRNA.
DR   EMBL; BT057535; ACM09407.1; -; mRNA.
DR   EMBL; BT060093; ACN12453.1; -; mRNA.
DR   RefSeq; NP_001135168.1; NM_001141696.1.
DR   RefSeq; XP_014056156.1; XM_014200681.1.
DR   AlphaFoldDB; B5DGI7; -.
DR   SMR; B5DGI7; -.
DR   STRING; 8030.ENSSSAP00000014327; -.
DR   Ensembl; ENSSSAT00000180881; ENSSSAP00000154899; ENSSSAG00000112907.
DR   GeneID; 100196667; -.
DR   KEGG; sasa:100196667; -.
DR   CTD; 9939; -.
DR   OrthoDB; 1444995at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa05.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; ISS:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   CDD; cd12324; RRM_RBM8; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR008111; RNA-bd_8.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR033744; RRM_RBM8.
DR   PANTHER; PTHR45894; PTHR45894; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PRINTS; PR01738; RNABINDINGM8.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; mRNA processing; mRNA splicing; mRNA transport;
KW   Nonsense-mediated mRNA decay; Nucleus; Reference proteome; RNA-binding;
KW   Spliceosome; Translation regulation; Transport.
FT   CHAIN           1..175
FT                   /note="RNA-binding protein 8A"
FT                   /id="PRO_0000378565"
FT   DOMAIN          73..151
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..175
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        20..21
FT                   /note="Missing (in Ref. 2; ACM09407)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   175 AA;  19898 MW;  A626B6CA99B7D961 CRC64;
     MADVLDLHEA GGEDFAMDED GDDSIHKLKE KAKRRKGRGF GSEEGARSRV REDYDTVEQD
     GDEPGPQRSV EGWILFVTGV HEEATEEDIH DKFAEFGEIK NLHLNLDRRT GYLKGYALVE
     YETYKEAQAA MEGLNGQDMM GQPISVDWGF VRGPPKSKRR GGGRRRSRSP DRRRR
 
 
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