NOVA1_RAT
ID NOVA1_RAT Reviewed; 474 AA.
AC Q80WA4;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=RNA-binding protein Nova-1 {ECO:0000305};
DE AltName: Full=Neuro-oncological ventral antigen 1;
DE Flags: Fragment;
GN Name=Nova1 {ECO:0000312|RGD:621345};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BDIX; TISSUE=Cerebellum;
RA Knudsen A., Monstad S.E., Vedeler C.A.;
RT "Nova-1, the paraneoplastic Ri antigen, is associated with breast cancer.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=12124753; DOI=10.1002/neu.10072;
RA Kumar D.V., Nighorn A., St John P.A.;
RT "Role of Nova-1 in regulating alpha2N, a novel glycine receptor splice
RT variant, in developing spinal cord neurons.";
RL J. Neurobiol. 52:156-165(2002).
CC -!- FUNCTION: Functions to regulate alternative splicing in neurons by
CC binding pre-mRNA in a sequence-specific manner to activate exon
CC inclusion or exclusion. It binds specifically to the sequences 5'-YCAY-
CC 3' and regulates splicing in only a subset of regulated exons. Binding
CC to an exonic 5'-YCAY-3' cluster changes the protein complexes assembled
CC on pre-mRNA, blocking U1 snRNP binding and exon inclusion, whereas
CC binding to an intronic 5'-YCAY-3' cluster enhances spliceosome assembly
CC and exon inclusion (PubMed:12124753). Binding to 5'-YCAY-3' clusters
CC results in a local and asymmetric action to regulate spliceosome
CC assembly and alternative splicing in neurons. Binding to an exonic 5'-
CC YCAY-3' cluster changed the protein complexes assembled on pre-mRNA,
CC blocking U1 snRNP (small nuclear ribonucleoprotein) binding and exon
CC inclusion, whereas binding to an intronic 5'-YCAY-3' cluster enhanced
CC spliceosome assembly and exon inclusion. With NOVA1, they perform
CC unique biological functions in different brain areas and cell types.
CC Autoregulates its own expression by acting as a splicing repressor.
CC Acts to activate the inclusion of exon E3A in the glycine receptor
CC alpha-2 chain and of exon E9 in gamma-aminobutyric-acid receptor gamma-
CC 2 subunit via a distal downstream UCAU-rich intronic splicing enhancer.
CC Acts to regulate a novel glycine receptor alpha-2 chain splice variant
CC (alpha-2N) in developing spinal cord. {ECO:0000269|PubMed:12124753}.
CC -!- SUBUNIT: Interacts with PTBP2; the interaction is direct.
CC {ECO:0000250|UniProtKB:Q9JKN6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9JKN6}.
CC -!- DOMAIN: The KH domain consists of approximately 70 amino acids and
CC includes a conserved hydrophobic core, an invariant Gly-X-X-Gly motif,
CC and an additional variable segment. The third KH domain (KH3) binds a
CC hairpin RNA loop containing the 5'-UCAY-3' motif on targeted molecules.
CC RNA binding by KH3 requires residues C-terminal to the KH domain.
CC {ECO:0000250|UniProtKB:P51513}.
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DR EMBL; AY262017; AAP20872.1; -; mRNA.
DR AlphaFoldDB; Q80WA4; -.
DR SMR; Q80WA4; -.
DR IntAct; Q80WA4; 2.
DR STRING; 10116.ENSRNOP00000045624; -.
DR jPOST; Q80WA4; -.
DR PRIDE; Q80WA4; -.
DR UCSC; RGD:621345; rat.
DR RGD; 621345; Nova1.
DR eggNOG; KOG2191; Eukaryota.
DR InParanoid; Q80WA4; -.
DR PhylomeDB; Q80WA4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:1990825; F:sequence-specific mRNA binding; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISO:RGD.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0050684; P:regulation of mRNA processing; IMP:RGD.
DR GO; GO:0051252; P:regulation of RNA metabolic process; ISO:RGD.
DR GO; GO:0021510; P:spinal cord development; IEP:RGD.
DR Gene3D; 3.30.1370.10; -; 3.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR033086; NOVA1.
DR PANTHER; PTHR10288:SF229; PTHR10288:SF229; 2.
DR Pfam; PF00013; KH_1; 3.
DR SMART; SM00322; KH; 3.
DR SUPFAM; SSF54791; SSF54791; 3.
DR PROSITE; PS50084; KH_TYPE_1; 3.
PE 2: Evidence at transcript level;
KW mRNA processing; mRNA splicing; Neurogenesis; Nucleus; Reference proteome;
KW Repeat; RNA-binding.
FT CHAIN 1..>474
FT /note="RNA-binding protein Nova-1"
FT /id="PRO_0000050118"
FT DOMAIN 48..115
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 146..212
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 396..463
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..474
FT /note="Required for RNA binding"
FT /evidence="ECO:0000250|UniProtKB:P51513"
FT MOTIF 26..42
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 19..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 474
SQ SEQUENCE 474 AA; 48444 MW; 70D0926B5BECD131 CRC64;
MAAAPIQQNG THTGVPIDLD PPDSRKRPLE APPEAGSTKR TNTGEDGQYF LKVLIPSYAA
GSIIGKGGQT IVQLQKETGA TIKLSKSKDF YPGTTERVCL IQGTIEALNA VHGFIAEKIR
EMPQNVAKTE PVSILQPQTT VNPDRIKQVK IIVPNSTAGL IIGKGGATVK AIMEQSGAWV
QLSQKPDGIN LQERVVTVSG EPEQNRKAVE LIIQKIQEDP QSGSCLNISY ANVTGPVANS
NPTGFPYANT AEVLPTAAAA AGLLGHANLA GVAAFPAVLS GFTGNDLVAI TSALNTLASY
GYNLNTLGLG LSQAAATGAL AAAAASANPA AAAANLLATY ASEASASGST AGGTAGTFAL
GSLAAATAAT NGYFGAASPL AASAILGTEK STDGSKDVVE IAVPENLVGA ILGKGGKTLV
EYQELTGARI QISKKGEFVP GTRNRKVTIT GTPAATQAAQ YLITQRITYE QGVR
