CASC3_XENLA
ID CASC3_XENLA Reviewed; 686 AA.
AC A0JMU8; B7ZRY2;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 51.
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=XlMLN51;
GN Name=casc3; Synonyms=mln51;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
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; BC126013; AAI26014.1; -; mRNA.
DR EMBL; BC170329; AAI70329.1; -; mRNA.
DR RefSeq; NP_001128538.1; NM_001135066.1.
DR AlphaFoldDB; A0JMU8; -.
DR DNASU; 100189566; -.
DR GeneID; 100189566; -.
DR KEGG; xla:100189566; -.
DR CTD; 100189566; -.
DR Xenbase; XB-GENE-17335605; casc3.L.
DR OrthoDB; 486761at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 100189566; Expressed in blastula and 19 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; IEA:InterPro.
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..686
FT /note="Protein CASC3"
FT /id="PRO_0000379475"
FT REGION 1..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..686
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 43..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..78
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..671
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 121
FT /note="Q -> K (in Ref. 1; AAI70329)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="V -> D (in Ref. 1; AAI70329)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="L -> P (in Ref. 1; AAI70329)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="T -> A (in Ref. 1; AAI70329)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 686 AA; 76962 MW; A76640CA2B1C7311 CRC64;
MADRRRRRRR ASQDSEGEEE EEESGSDSVG SGGESGAPVR QERSEQGNRK AEPPREGKES
ECESEDGIEG DAVLSDYESA DESEIVPTKE VEEAHYNEEE PLKATLKQEN NVEEAPAARD
QKPKSKGTVT GERQSGDGQE SNEPEEDKTI QKSQKQLDDD EDRKNPAYIP RKGLFFEHDL
RGHVNDEEVR PKGRHPRKLW KDEGRWVHDR FHEDEQAPKS REELISIYGY DIRSSKNPEE
IRPRRPRKPR FSSPSRREEN NEKASWPLNR YQDSGDAQPL RPYTNRSAPP SNKVVPSRTY
SRQGGYKENR ASYQSEEEAS LHTYERRQVY GGHRARSSEQ GPPPPREFSP EADPIVKEEA
VIEKQAAEPS PPPPDRPVEK KSYSRARRSR IKVGDTGKSM EDTTAAELPP PPLMPPAVAA
EFTPAPLNVK QGNWEPPAEG GMSGIDEELS QMNLTEQSWN QGQPAYISPR GIPNPMHMGN
GPPQYSRMEG MAVQGGRVKR YSSQRQRPVP DPAAMHISLM ESHYYDPLQF QGPIYTHGDS
SSSMPPQGMI VPPEMHLSHP GMHPHPSPAT MSTPNLYPAP VSLPPGQQPP QQLLPPPYFP
APPNVMNFGN PTYPYPPGAL PPPPAHLYPN AQAQSQVYGG VTYYNPVQQQ VQPKPSPPRR
TSQPVTIKPP PPEENRHLKM NEKINS
