SMN1_DANRE
ID SMN1_DANRE Reviewed; 281 AA.
AC Q9W6S8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Survival motor neuron protein 1;
GN Name=smn1; Synonyms=smn;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10196366; DOI=10.1093/hmg/8.5.775;
RA Bertrandy S., Burlet P., Clermont O., Huber C., Fondrat C.,
RA Thierry-Mieg D., Munnich A., Lefebvre S.;
RT "The RNA-binding properties of SMN: deletion analysis of the zebrafish
RT orthologue defines domains conserved in evolution.";
RL Hum. Mol. Genet. 8:775-782(1999).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-17 AND SER-20, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23063131; DOI=10.1016/j.cell.2012.09.012;
RA Lotti F., Imlach W.L., Saieva L., Beck E.S., Hao le T., Li D.K., Jiao W.,
RA Mentis G.Z., Beattie C.E., McCabe B.D., Pellizzoni L.;
RT "An SMN-dependent U12 splicing event essential for motor circuit
RT function.";
RL Cell 151:440-454(2012).
RN [4]
RP FUNCTION, INTERACTION WITH ELAVL4, AND DISRUPTION PHENOTYPE.
RX PubMed=29061699; DOI=10.1523/jneurosci.1528-17.2017;
RA Hao le T., Duy P.Q., An M., Talbot J., Iyer C.C., Wolman M., Beattie C.E.;
RT "HuD and the Survival Motor Neuron Protein Interact in Motoneurons and Are
RT Essential for Motoneuron Development, Function, and mRNA Regulation.";
RL J. Neurosci. 37:11559-11571(2017).
CC -!- FUNCTION: The SMN complex plays an essential role in spliceosomal snRNP
CC assembly in the cytoplasm and is required for pre-mRNA splicing in the
CC nucleus (PubMed:23063131). It may also play a role in the metabolism of
CC snoRNPs (PubMed:23063131). Required in motor neurons and proprioceptive
CC neurons to ensure correct U12 intron splicing and proper levels of
CC tmem41b mRNA (PubMed:23063131). Required for the maturation of motor
CC neuron axonal branches and dendrites (PubMed:23063131,
CC PubMed:29061699). {ECO:0000269|PubMed:23063131,
CC ECO:0000269|PubMed:29061699}.
CC -!- SUBUNIT: Homodimer. Component of an import snRNP complex composed of
CC kpnb1, rnut1, smn1 and znf259. Part of the core SMN complex that
CC contains smn1, gemin2/sip1, ddx20/gemin3, gemin4, gemin5, gemin6,
CC gemin7, gemin8 and strap/unrip. Interacts with ddx20, fbl, nola1,
CC rnut1, syncrip and with several spliceosomal snRNP core Sm proteins,
CC including snrpb, snrpd1, snrpd2, snrpd3, snrpe and ilf3 (By
CC similarity). Interacts with elavl4 (PubMed:29061699).
CC {ECO:0000250|UniProtKB:Q16637, ECO:0000269|PubMed:29061699}.
CC -!- SUBCELLULAR LOCATION: Nucleus, gem {ECO:0000250|UniProtKB:Q16637}.
CC Nucleus, Cajal body {ECO:0000250|UniProtKB:Q16637}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q16637}. Cytoplasmic granule
CC {ECO:0000250|UniProtKB:Q16637}. Perikaryon
CC {ECO:0000250|UniProtKB:Q16637}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:Q16637}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:P97801}.
CC -!- DOMAIN: The Tudor domain mediates association with dimethylarginines,
CC which are common in snRNP proteins. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Decreased axonal branches and decreased dendrites
CC in motor neurons (PubMed:29061699). Decreased GAP43 mRNA levels
CC (PubMed:29061699). Morpholino knockdown of the protein causes severe
CC defects in motor neuron axonal outgrowth, including truncations and
CC abnormal branching (PubMed:23063131). {ECO:0000269|PubMed:23063131,
CC ECO:0000269|PubMed:29061699}.
CC -!- SIMILARITY: Belongs to the SMN family. {ECO:0000305}.
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DR EMBL; Y17256; CAB41938.1; -; mRNA.
DR RefSeq; NP_571266.1; NM_131191.1.
DR AlphaFoldDB; Q9W6S8; -.
DR SMR; Q9W6S8; -.
DR STRING; 7955.ENSDARP00000017636; -.
DR iPTMnet; Q9W6S8; -.
DR PaxDb; Q9W6S8; -.
DR Ensembl; ENSDART00000028099; ENSDARP00000017636; ENSDARG00000018494.
DR GeneID; 30432; -.
DR KEGG; dre:30432; -.
DR CTD; 6606; -.
DR ZFIN; ZDB-GENE-990715-16; smn1.
DR eggNOG; KOG4327; Eukaryota.
DR GeneTree; ENSGT00940000153352; -.
DR HOGENOM; CLU_077852_0_0_1; -.
DR InParanoid; Q9W6S8; -.
DR OMA; LMAWYMS; -.
DR OrthoDB; 1316275at2759; -.
DR PhylomeDB; Q9W6S8; -.
DR TreeFam; TF318390; -.
DR Reactome; R-DRE-191859; snRNP Assembly.
DR PRO; PR:Q9W6S8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000018494; Expressed in ovary and 29 other tissues.
DR ExpressionAtlas; Q9W6S8; baseline and differential.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISS:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IPI:ZFIN.
DR GO; GO:0032797; C:SMN complex; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0061564; P:axon development; IMP:ZFIN.
DR GO; GO:0048675; P:axon extension; IMP:ZFIN.
DR GO; GO:0007409; P:axonogenesis; IMP:ZFIN.
DR GO; GO:0016358; P:dendrite development; IMP:ZFIN.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:ZFIN.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:ZFIN.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:ZFIN.
DR GO; GO:0048936; P:peripheral nervous system neuron axonogenesis; IMP:ZFIN.
DR GO; GO:1903862; P:positive regulation of oxidative phosphorylation; IMP:ZFIN.
DR GO; GO:0048841; P:regulation of axon extension involved in axon guidance; IMP:ZFIN.
DR GO; GO:1904396; P:regulation of neuromuscular junction development; IMP:ZFIN.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IBA:GO_Central.
DR CDD; cd04508; TUDOR; 1.
DR InterPro; IPR010304; SMN_Tudor.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF06003; SMN; 1.
DR SMART; SM00333; TUDOR; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; mRNA processing; mRNA splicing; Neurogenesis;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Spliceosome.
FT CHAIN 1..281
FT /note="Survival motor neuron protein 1"
FT /id="PRO_0000218906"
FT DOMAIN 80..140
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..252
FT /note="P2 (binding site for SNRPB)"
FT /evidence="ECO:0000250"
FT REGION 264..279
FT /note="Required for interaction with SYNCRIP"
FT /evidence="ECO:0000250"
FT COMPBIAS 145..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..198
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..237
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
SQ SEQUENCE 281 AA; 30986 MW; BCDD2C998D23C759 CRC64;
MANGAEDVVF CRGTGQSDDS DIWDDTALIK AYDKAVASFK NALKGEDGAT PQENDNPGKK
RKNNKKNKSR KRCNAAPDKE WQVGDSCYAF WSEDGNLYTA TITSVDQEKG TCVVFYTDYG
NEEEQNLSDL LTEPPDMDED ALKTANVKET ESSTEESDRS FTPQKSGHAK HKSKSNFPMG
PPSWFPSFPP GPPPPPPHFK KMDGRRGEGP GPSFPGWPPM IPLGPPMIPP PPPMSPDFGE
DDEALGSMLI SWYMSGYHTG YYMGLRQGRK EAAASKKSHR K
