CASC3_BOVIN
ID CASC3_BOVIN Reviewed; 703 AA.
AC A5D7H5;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Protein CASC3;
DE AltName: Full=Cancer susceptibility candidate gene 3 protein;
DE AltName: Full=Metastatic lymph node gene 51 protein homolog;
DE Short=MLN 51 homolog;
DE AltName: Full=Protein barentsz;
DE Short=Btz;
GN Name=CASC3; Synonyms=MLN51;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) 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). Stimulates the
CC ATPase and RNA-helicase activities of EIF4A3. Plays a role in the
CC stress response by participating in cytoplasmic stress granules
CC assembly and by favoring cell recovery following stress. Component of
CC the dendritic ribonucleoprotein particles (RNPs) in hippocampal
CC neurons. May play a role in mRNA transport. Binds spliced mRNA in
CC sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-
CC exon junctions. Binds poly(G) and poly(U) RNA homomer.
CC {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/Y14. Identified in a complex
CC composed of the EJC core, UPF3B and UPF2. The EJC core can also
CC interact with UPF3A (in vitro) (By similarity). Forms homooligomers (By
CC similarity). Interacts with STAU in an RNA-dependent manner (By
CC similarity). Interacts with DHX34; the interaction is RNA-independent
CC (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. In nuclear speckles, colocalizes with MAGOH. Under
CC stress conditions, colocalizes with FMR1 and TIA1, but not MAGOH and
CC RBM8A EJC core factors, in cytoplasmic stress granules (By similarity).
CC In the dendrites of hippocampal neurons, localizes to dendritic
CC ribonucleoprotein granules (By similarity).
CC {ECO:0000250|UniProtKB:O15234, ECO:0000250|UniProtKB:Q8K3X0}.
CC -!- DOMAIN: The coiled coil domain may be involved in oligomerization.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated
CC protein is recognized by RNF146, followed by ubiquitination (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its
CC degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CASC3 family. {ECO:0000305}.
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DR EMBL; BC140556; AAI40557.1; -; mRNA.
DR RefSeq; NP_001091538.1; NM_001098069.1.
DR RefSeq; XP_005220789.1; XM_005220732.3.
DR RefSeq; XP_005220790.1; XM_005220733.3.
DR RefSeq; XP_015314320.1; XM_015458834.1.
DR AlphaFoldDB; A5D7H5; -.
DR STRING; 9913.ENSBTAP00000008203; -.
DR PaxDb; A5D7H5; -.
DR PRIDE; A5D7H5; -.
DR Ensembl; ENSBTAT00000008203; ENSBTAP00000008203; ENSBTAG00000006250.
DR GeneID; 531673; -.
DR KEGG; bta:531673; -.
DR CTD; 22794; -.
DR VEuPathDB; HostDB:ENSBTAG00000006250; -.
DR VGNC; VGNC:54702; CASC3.
DR eggNOG; KOG4264; Eukaryota.
DR GeneTree; ENSGT00390000006930; -.
DR HOGENOM; CLU_018976_0_0_1; -.
DR InParanoid; A5D7H5; -.
DR OMA; MIQDPHM; -.
DR OrthoDB; 486761at2759; -.
DR TreeFam; TF329663; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000006250; Expressed in pigment epithelium of eye and 106 other tissues.
DR ExpressionAtlas; A5D7H5; baseline.
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 ADP-ribosylation; Cell projection; Coiled coil; Cytoplasm; mRNA processing;
KW mRNA splicing; mRNA transport; Nonsense-mediated mRNA decay; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Spliceosome;
KW Stress response; Translation regulation; Transport; Ubl conjugation.
FT CHAIN 1..703
FT /note="Protein CASC3"
FT /id="PRO_0000378550"
FT REGION 1..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..283
FT /note="Necessary for RNA-binding, interaction with MAGOH
FT and localization in nucleus speckles"
FT /evidence="ECO:0000250"
FT REGION 137..283
FT /note="Sufficient to form the EJC"
FT /evidence="ECO:0000250"
FT REGION 377..703
FT /note="Necessary for localization in cytoplasmic stress
FT granules"
FT /evidence="ECO:0000250"
FT REGION 633..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 102..125
FT /evidence="ECO:0000255"
FT MOTIF 204..210
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255"
FT MOTIF 254..262
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255"
FT MOTIF 462..471
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..108
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..443
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..653
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..694
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3W3"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15234"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15234"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15234"
FT MOD_RES 357
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15234"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15234"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15234"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15234"
SQ SEQUENCE 703 AA; 76147 MW; 4CC0AB3F984B99A2 CRC64;
MADRRRQRAS QDTEDEESGA SGSDSGGSPA RGGGSCSGSV GGGGSGSLPS QRGGRAGALH
LRRVESGGAK SAEESECESE DGIEGDAVLS DYESAEDSEG DDGEYSEEEN SKVELKSEAN
DAANSSAKDE KGEEKPDTKG TVTGERQSGD GQESTEPVEN KVGKKGPKHL DDDEDRKNPA
YIPRKGLFFE HDLRGQTQEE EVRPKGRQRK LWKDEGRWEH DKFREDEQAP KSRQELIALY
GYDIRSAHNP DDIKPRRIRK PRFGSPPQRD PSWIGERPNK SHRHQGPGGT LPPRTFINRN
AAGTGRMSAP RNYSRSGGFK EGRTGFRPAE AGGQHAGRSG ETVKHETSYR SRHLEQTPVR
DPSPEADAQV LGSPEKEEVA PEIPNPAPDT APPVPDRPVE KKSYSRARRT RIKAGDAGKV
AEEVPPPPEG LTPAPPVPEA TPPTPAKTGN WEAPVDSTTG GLEQDVAQLN ITEQNWSPGQ
PAFLQSRELR GMPNHIHMGA GPPPQFNRME EMGVQGGRAK RYSSQRQRPV PEPPAPPVHI
SIMEGHYYDP LQFQGPIYTH GDSPAPLPPQ GMIVQPEMHL PHPGLHPHQT PAPLPNPGLY
PPPVSMSPGQ PPPQQLLAPT YFSAPGVMNF GNPSYPYAPG ALPPPPPPHL YPNTQAPSQV
YGGVTYYNPA QQQVQPKPSP PRRTPQPVTI KPPPPEVVSR GSS
