CASC3_DANRE
ID CASC3_DANRE Reviewed; 754 AA.
AC Q1ECZ4; Q7T1P0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Protein CASC3;
DE AltName: Full=Cancer susceptibility candidate gene 3 protein homolog;
DE AltName: Full=Metastatic lymph node protein 51 homolog;
DE Short=DrMLN51;
DE Short=Protein MLN 51 homolog;
GN Name=casc3; Synonyms=mln51;
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 [MRNA].
RC TISSUE=Embryo;
RX PubMed=15166247; DOI=10.1074/jbc.m402754200;
RA Degot S., Le Hir H., Alpy F., Kedinger V., Stoll I., Wendling C.,
RA Seraphin B., Rio M.-C., Tomasetto C.;
RT "Association of the breast cancer protein MLN51 with the exon junction
RT complex via its speckle localizer and RNA binding module.";
RL J. Biol. Chem. 279:33702-33715(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-481 AND SER-483, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome. Core component of the splicing-dependent multiprotein exon
CC junction complex (EJC) deposited at splice junctions on mRNAs. The EJC
CC is a dynamic structure consisting of core proteins and several
CC peripheral nuclear and cytoplasmic associated factors that join the
CC 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). Binds spliced mRNA
CC in sequence-independent manner, 20-24 nucleotides upstream of mRNA
CC exon-exon junctions. {ECO:0000250|UniProtKB:O15234}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Component of the mRNA
CC splicing-dependent exon junction complex (EJC), which contains at least
CC casc3, eif4a3, magoh, nxf1 and rbm8a (By similarity). Forms
CC homooligomers (By similarity). {ECO:0000250|UniProtKB:O15234,
CC ECO:0000250|UniProtKB:Q8K3X0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15234}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K3W3}. Nucleus
CC {ECO:0000250|UniProtKB:O15234}. Nucleus speckle
CC {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Cytoplasmic
CC ribonucleoprotein granule {ECO:0000250|UniProtKB:Q8K3X0}. Cell
CC projection, dendrite {ECO:0000250|UniProtKB:Q8K3X0}. Note=Shuttles
CC between the nucleus and the cytoplasm in a xpo1/crm1-dependent manner.
CC Transported to the cytoplasm as part of the exon junction complex (EJC)
CC bound to mRNA (By similarity). In the dendrites of hippocampal neurons,
CC localizes to dendritic ribonucleoprotein granules (By similarity).
CC {ECO:0000250|UniProtKB:O15234, ECO:0000250|UniProtKB:Q8K3X0}.
CC -!- SIMILARITY: Belongs to the CASC3 family. {ECO:0000305}.
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DR EMBL; AJ555546; CAD88256.1; -; mRNA.
DR EMBL; BC117611; AAI17612.1; -; mRNA.
DR RefSeq; NP_991279.1; NM_205716.1.
DR AlphaFoldDB; Q1ECZ4; -.
DR SMR; Q1ECZ4; -.
DR STRING; 7955.ENSDARP00000040064; -.
DR iPTMnet; Q1ECZ4; -.
DR PaxDb; Q1ECZ4; -.
DR PRIDE; Q1ECZ4; -.
DR Ensembl; ENSDART00000040065; ENSDARP00000040064; ENSDARG00000029911.
DR GeneID; 403025; -.
DR KEGG; dre:403025; -.
DR CTD; 22794; -.
DR ZFIN; ZDB-GENE-040308-2; casc3.
DR eggNOG; KOG4264; Eukaryota.
DR GeneTree; ENSGT00390000006930; -.
DR HOGENOM; CLU_018976_0_0_1; -.
DR InParanoid; Q1ECZ4; -.
DR OMA; SHYRNNE; -.
DR OrthoDB; 486761at2759; -.
DR PhylomeDB; Q1ECZ4; -.
DR TreeFam; TF329663; -.
DR Reactome; R-DRE-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DRE-72187; mRNA 3'-end processing.
DR Reactome; R-DRE-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-DRE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:Q1ECZ4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000029911; Expressed in cleaving embryo and 28 other tissues.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0035145; C:exon-exon junction complex; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
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:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR InterPro; IPR018545; Btz_dom.
DR InterPro; IPR028544; CASC3.
DR PANTHER; PTHR13434; PTHR13434; 1.
DR Pfam; PF09405; Btz; 1.
DR SMART; SM01044; Btz; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; mRNA processing; mRNA splicing; mRNA transport;
KW Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Spliceosome; Translation regulation; Transport.
FT CHAIN 1..754
FT /note="Protein CASC3"
FT /id="PRO_0000378551"
FT REGION 1..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT CONFLICT 99
FT /note="H -> R (in Ref. 1; CAD88256)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 754 AA; 82743 MW; 595AFF46922A97E7 CRC64;
MADRRRRRRR ASQDSEEEDE SASGSESGRS FSASRKTRGR EPEPVESPAE RVAAKSDDES
ECVSEDGVGE AVLSDYDSAD LEENGSHTEG GEEEEEAEHF SEEEASRPAA ESKPVADAPT
EELVEGEERD ESVKEVKADE KGNLAGERQS GDGQESTEDP ENKGSKGQKL DDDEDRKNPA
YIPRKGLFFE HDVRGQATEE ERPKGRNRKL WKDEGRWEHD KFREEEQAPK SRDELIAFYG
YDIRNGTGPS DGRSYRSRKP RHAGSPSREP RRYREGDKSV RSSWQGPPPG HRNAPQSVTV
QSGQPLAPLS APKPSGRPST QPPQRSFQGS RAPSAPHRTE GRGPSKPSLD GAPLRGPRSQ
PVEGERGPRL RGRSSHAVHA DRSPSLVVED ICSEEEEEEG EIPTATTTYT AHHYKTEKER
VPSPRKQDSG MVMEGGSAAG QVRELSPPQE RQVEKKSYSR ARRATRTRPS DLSKQASLDD
SSSAVQQAPV AAKSESWQEQ SEAGTQSGLT GLDQDLARLS LTGQNWAQNP PSYLQAEMRG
IRGSMHMAGG PPQYGNMEDM GVGGGRAKRY SSQRQRPVPE PAPMHIGVME GHYYEPMTFQ
GPIYTHGESP AALPPQGMLV QPEMHLPHPT HPGLHPHQSG GPLPNPAIYA APPVSLSPGQ
PPPQQLLPPP FYPPPGVMTF GNTNYPYPAG GTLPPMYPNP QAQSQVYGGV TYYDTIQQQA
QPKRSPPRRS SNPVTVRPPP PEDQSRKAAE EIRS
