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NOVA1_MACFA
ID   NOVA1_MACFA             Reviewed;         483 AA.
AC   Q2PFW9; Q4R7W5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=RNA-binding protein Nova-1;
DE   AltName: Full=Neuro-oncological ventral antigen 1;
DE   AltName: Full=Ventral neuron-specific protein 1;
GN   Name=NOVA1; ORFNames=QflA-17531, QtsA-14227;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Frontal cortex;
RA   Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S.,
RA   Hashimoto K.;
RT   "Analysis of gene expression in cynomolgus monkey tissues by macaque cDNA
RT   oligo-chips.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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. Binding to 5'-YCAY-3' clusters results in a local
CC       and asymmetric action to regulate spliceosome assembly and alternative
CC       splicing in neurons. Binding to an exonic 5'-YCAY-3' cluster changed
CC       the protein complexes assembled on pre-mRNA, blocking U1 snRNP (small
CC       nuclear ribonucleoprotein) binding and exon inclusion, whereas binding
CC       to an intronic 5'-YCAY-3' cluster enhanced spliceosome assembly and
CC       exon inclusion. With NOVA1, they perform unique biological functions in
CC       different brain areas and cell types. Autoregulates its own expression
CC       by acting as a splicing repressor. Acts to activate the inclusion of
CC       exon E3A in the glycine receptor alpha-2 chain and of exon E9 in gamma-
CC       aminobutyric-acid receptor gamma-2 subunit via a distal downstream
CC       UCAU-rich intronic splicing enhancer. Acts to regulate a novel glycine
CC       receptor alpha-2 chain splice variant (alpha-2N) in developing spinal
CC       cord. {ECO:0000250|UniProtKB:Q9JKN6}.
CC   -!- SUBUNIT: Interacts with PTBP2; the interaction is direct.
CC       {ECO:0000250|UniProtKB:Q9JKN6}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9JKN6}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q2PFW9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q2PFW9-2; Sequence=VSP_022134, VSP_022135;
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; AB168696; BAE00807.1; -; mRNA.
DR   EMBL; AB220468; BAE73001.1; -; mRNA.
DR   RefSeq; NP_001274225.1; NM_001287296.1. [Q2PFW9-1]
DR   AlphaFoldDB; Q2PFW9; -.
DR   SMR; Q2PFW9; -.
DR   STRING; 9541.XP_005561061.1; -.
DR   Ensembl; ENSMFAT00000077592; ENSMFAP00000052981; ENSMFAG00000035425. [Q2PFW9-1]
DR   GeneID; 102134094; -.
DR   CTD; 4857; -.
DR   VEuPathDB; HostDB:ENSMFAG00000035425; -.
DR   eggNOG; KOG2191; Eukaryota.
DR   GeneTree; ENSGT00940000155573; -.
DR   OMA; MTTLANY; -.
DR   Proteomes; UP000233100; Chromosome 7.
DR   Bgee; ENSMFAG00000035425; Expressed in cerebellum and 8 other tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; IEA:InterPro.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
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   Alternative splicing; mRNA processing; mRNA splicing; Neurogenesis;
KW   Nucleus; Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..483
FT                   /note="RNA-binding protein Nova-1"
FT                   /id="PRO_0000270145"
FT   DOMAIN          49..116
FT                   /note="KH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          147..213
FT                   /note="KH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          397..464
FT                   /note="KH 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..479
FT                   /note="Required for RNA binding"
FT                   /evidence="ECO:0000250|UniProtKB:P51513"
FT   MOTIF           27..43
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        20..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..141
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_022134"
FT   VAR_SEQ         142..148
FT                   /note="VNPDRIK -> MTTSRAN (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_022135"
SQ   SEQUENCE   483 AA;  49267 MW;  2D4352D3DE9BFCFB CRC64;
     MMAAAPIQQN GTHTGVPIDL DPPDSRKRPL EAPPEAGSTK RTNTGEDGQY FLKVLIPSYA
     AGSIIGKGGQ TIVQLQKETG ATIKLSKSKD FYPGTTERVC LIQGTVEALN AVHGFIAEKI
     REMPQNVAKT EPVSILQPQT TVNPDRIKQV KIIVPNSTAG LIIGKGGATV KAIMEQSGAW
     VQLSQKPDGI NLQERVVTVS GEPEQNRKAV ELIIQKIQED PQSGSCLNIS YANVTGPVAN
     SNPTGSPYAN TAEVLPTAAA AAGLLGHANL AGVAAFPAVL SGFTGNDLVA ITSALNTLAS
     YGYNLNTLGL GLSQAAATGA LAAAAASANP AAAAANLLAT YASEASASGS TAGGTAGTFA
     LGSLAAATAA TNGYFGAASP LAASAILGTE KSTDGSKDVV EIAVPENLVG AILGKGGKTL
     VEYQELTGAR IQISKKGEFV PGTRNRKVTI TGTPAATQAA QYLITQRITY EQGVRAANPQ
     KVG
 
 
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