SYDN_CAEEL
ID SYDN_CAEEL Reviewed; 578 AA.
AC Q95XQ1;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 4.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Synaptic defective enhancer 1 {ECO:0000303|PubMed:20530551};
GN Name=sydn-1 {ECO:0000303|PubMed:20530551,
GN ECO:0000312|WormBase:Y39G10AR.17};
GN ORFNames=Y39G10AR.17 {ECO:0000312|WormBase:Y39G10AR.17};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20530551; DOI=10.1242/dev.049692;
RA Van Epps H., Dai Y., Qi Y., Goncharov A., Jin Y.;
RT "Nuclear pre-mRNA 3'-end processing regulates synapse and axon development
RT in C. elegans.";
RL Development 137:2237-2250(2010).
RN [3] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH SSUP-72.
RX PubMed=26588990; DOI=10.1101/gad.266650.115;
RA Chen F., Zhou Y., Qi Y.B., Khivansara V., Li H., Chun S.Y., Kim J.K.,
RA Fu X.D., Jin Y.;
RT "Context-dependent modulation of Pol II CTD phosphatase SSUP-72 regulates
RT alternative polyadenylation in neuronal development.";
RL Genes Dev. 29:2377-2390(2015).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28087624; DOI=10.1242/dev.146001;
RA Chen F., Chisholm A.D., Jin Y.;
RT "Tissue-specific regulation of alternative polyadenylation represses
RT expression of a neuronal ankyrin isoform in C. elegans epidermal
RT development.";
RL Development 144:698-707(2017).
CC -!- FUNCTION: Acts as a negative regulator of nuclear pre-mRNA 3'-end
CC processing (mRNA polyadenylation) (Probable) (PubMed:26588990). Plays a
CC role in tissue-specific expression of protein isoforms by regulating
CC differential processing of pre-mRNA 3'-end (alternative
CC polyadenylation) (PubMed:26588990, PubMed:28087624). In neurons,
CC regulates alternative polyadenylation of specific mRNAs including unc-
CC 44 and dlk-1 by interacting with phosphatase ssup-72 and thus
CC preventing ssup-72 dephosphorylation of RNA polymerase II subunit ama-1
CC (PubMed:26588990). Specifically, alters the usage of internal
CC polyadenylation sites (PAS) to promote the production of neuron-
CC specific unc-44 isoform and dlk-1 isoform c, both required for normal
CC synapse and axon development (PubMed:26588990). Conversely, in the
CC epidermis, by inhibiting ssup-72 function, promotes the usage of an
CC internal PAS preventing the production of one of unc-44 isoforms
CC (PubMed:28087624). In neurons, also negatively regulates protein levels
CC of pre-RNA processing protein psf-2 (PubMed:20530551).
CC {ECO:0000269|PubMed:20530551, ECO:0000269|PubMed:26588990,
CC ECO:0000269|PubMed:28087624, ECO:0000305|PubMed:20530551}.
CC -!- SUBUNIT: May interact (via C-terminus) with ssup-72; the interaction
CC may prevent ssup-72 binding to RNA polymerase II subunit ama-1.
CC {ECO:0000269|PubMed:26588990}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28087624}. Nucleus
CC speckle {ECO:0000269|PubMed:20530551}. Note=Also localizes to a small
CC subnuclear ring in neurons. In neurons, partially co-localizes with
CC pfs-2 in the nucleus. {ECO:0000269|PubMed:20530551}.
CC -!- TISSUE SPECIFICITY: Expressed in germline, oocytes, epidermis,
CC pharyngeal bulb and neurons. {ECO:0000269|PubMed:26588990}.
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DR EMBL; BX284601; CCD69921.2; -; Genomic_DNA.
DR RefSeq; NP_490969.4; NM_058568.4.
DR AlphaFoldDB; Q95XQ1; -.
DR SMR; Q95XQ1; -.
DR DIP; DIP-24383N; -.
DR IntAct; Q95XQ1; 5.
DR MINT; Q95XQ1; -.
DR STRING; 6239.Y39G10AR.17; -.
DR EPD; Q95XQ1; -.
DR PaxDb; Q95XQ1; -.
DR EnsemblMetazoa; Y39G10AR.17.1; Y39G10AR.17.1; WBGene00021473.
DR UCSC; Y39G10AR.17; c. elegans.
DR WormBase; Y39G10AR.17; CE47864; WBGene00021473; sydn-1.
DR eggNOG; ENOG502QURU; Eukaryota.
DR GeneTree; ENSGT00940000171596; -.
DR HOGENOM; CLU_398630_0_0_1; -.
DR InParanoid; Q95XQ1; -.
DR OMA; SPQMKPP; -.
DR OrthoDB; 1741458at2759; -.
DR PRO; PR:Q95XQ1; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00021473; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0016607; C:nuclear speck; IDA:WormBase.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW mRNA processing; Nucleus; Reference proteome.
FT CHAIN 1..578
FT /note="Synaptic defective enhancer 1"
FT /id="PRO_0000447208"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..545
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 578 AA; 63234 MW; 73BB575666A2961D CRC64;
MGEPSPSRRR SITSGIPCPS PTKQVLPPPP PEELHNILRK RPRSSAIPTT SQTHVRAPRK
ETDVVDRIWH DIDEEQREKL ARRKEEAAKR KEQQPAQHIR DYLPLTATNL RNFRNEDSTI
SDFIHRQGMV DKLLGYKMLL GKMENCGTLG YEKMSEDEVQ QLSREWLKNF FPSEQAHVGP
RTPPSPAVDS DGGSYPKRPR RGPKTPPGSP GPSMDQAAVN RRELIEQLAR NFGISSYKVE
ETLGTGLDKA LEDCSKKLKN ELMETFKDQL LSQIDRKTKI RDDLSDQMEL VSDCSLSPDL
IKKEEPDVVY HMAVPPPPIP PPIQPPPYSY YPVAPAAAPQ VYHYAPPPPP PPPHPQQGLY
QQNMMAYPPP MQHFNAPPPP MAPYQHQAPP SIVLPPVNVP PPPIGVRIDT PIPTAVLPIP
TMVPPPPLPP PQAPFSGDCW RAQPAAPVPA SVPVSSAPPP SVVVNVQSTL FSALGLHHKP
PPPPPPPPPP TTSSTTTSHI PPPPPPPLPF SSAPPPPPPL PMVAAGPSPP SFVPPPPPPN
PNQNPSIVLS PSAVTGGGGY RHRVNQFPPQ QQQSFSNF
