CASC3_XENTR
ID CASC3_XENTR Reviewed; 678 AA.
AC Q5CZI8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=Protein MLN 51 homolog;
DE Short=StMLN51;
GN Name=casc3; Synonyms=mln51;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION.
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).
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; CR855779; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BN000153; CAD88273.1; -; mRNA.
DR RefSeq; NP_001012670.1; NM_001012652.1.
DR AlphaFoldDB; Q5CZI8; -.
DR PaxDb; Q5CZI8; -.
DR GeneID; 503560; -.
DR KEGG; xtr:503560; -.
DR CTD; 22794; -.
DR Xenbase; XB-GENE-969211; casc3.
DR eggNOG; KOG4264; Eukaryota.
DR InParanoid; Q5CZI8; -.
DR OrthoDB; 486761at2759; -.
DR Reactome; R-XTR-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-XTR-72187; mRNA 3'-end processing.
DR Reactome; R-XTR-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR Proteomes; UP000008143; Chromosome 10.
DR Proteomes; UP000790000; Unplaced.
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 2: Evidence at transcript level;
KW Cell projection; 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..678
FT /note="Protein CASC3"
FT /id="PRO_0000379476"
FT REGION 1..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..87
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..663
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 75986 MW; B9B6FEBEF0B33BC9 CRC64;
MADRRRRRRR AFQDSEEEED EESGSESAGS GGQPAAPSRQ ESREPGTKRA EPPREGKESE
CESEDGIEGD AVLSDYESAE SEEEEAHLSE EEPLKTTLKQ ENNVEEAPAT REQKPKSKGA
VTGERQSGDG QESTEPEENK TSKKSQKQLD DDEDRKNPAY IPRKGLFFEH DLRGHVNDEE
VRPKGRHPRK LWKDEGRWEH DRFREDEQAP KSREELISIY GYDIRSSKNS EEIRPRRPRK
PRFGSPTRRE EISEKPSRPS NRYQDSGISQ PLRPYTNRNA PPSNKVGPSR TYSRQGGYKE
NRSSYQSEEE APPHPSERRQ DYGGHRARST EQGPAPPREF SPEADPIIKE EPVIEKQAAE
PSPPPPDRPV EKKSYSRVRR SRIKVGDTGK SMEDTTVTEL PPPPPVPPAV AAEFTPAPLN
VKQGNWEPPS EGGMSGIEEE LSQMNLSEQS WNPGQPAYIS PRGIPNPMHM GGGPPQYNRM
EGMAVQGGRV KRYSTQRQRP VPDPAAMHIS LMESHYYDPL QFQGPIYAHG DSPSSMPPQG
MIVQPEMHLS HPGIHPHQPP ATISTPNLYP APVSLPPGQP PPQQLLPPPY FTAPPNVMNF
GNPTYPYPPG ALPPPPAHLY PNAQAQSQVY GGVTYYNPVQ QQVQPKPSPP RRTSQPVTIK
PPPPEENRHV KMKEKSNS
