ID   SYF2_CAEEL              Reviewed;         234 AA.
AC   Q09385; Q09386;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 3.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Pre-mRNA-splicing factor syf-2;
GN   Name=syf-2 {ECO:0000312|WormBase:K04G7.11};
GN   ORFNames=K04G7.11 {ECO:0000312|WormBase:K04G7.11};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
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]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25204677; DOI=10.1186/s12915-014-0064-6;
RA   Crook-McMahon H.M., Olahova M., Button E.L., Winter J.J., Veal E.A.;
RT   "Genome-wide screening identifies new genes required for stress-induced
RT   phase 2 detoxification gene expression in animals.";
RL   BMC Biol. 12:64-64(2014).
CC   -!- FUNCTION: May be involved in pre-mRNA splicing (By similarity). May
CC       confer protection against toxicity induced by heavy metals such as
CC       arsenite, possibly by negatively regulating the expression of phase II
CC       detoxification genes such as gcs-1 in intestinal cells
CC       (PubMed:25204677). {ECO:0000250|UniProtKB:P53277,
CC       ECO:0000269|PubMed:25204677}.
CC   -!- SUBUNIT: May be part of a spliceosome complex.
CC       {ECO:0000250|UniProtKB:P53277}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95926}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in increased
CC       sensitivity to the heavy metal arsenite. {ECO:0000269|PubMed:25204677}.
CC   -!- SIMILARITY: Belongs to the SYF2 family. {ECO:0000305}.
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DR   EMBL; BX284603; CCD61619.1; -; Genomic_DNA.
DR   PIR; A88500; A88500.
DR   PIR; H88499; H88499.
DR   RefSeq; NP_498566.3; NM_066165.6.
DR   AlphaFoldDB; Q09385; -.
DR   SMR; Q09385; -.
DR   BioGRID; 41215; 3.
DR   STRING; 6239.K04G7.11; -.
DR   EPD; Q09385; -.
DR   PaxDb; Q09385; -.
DR   PeptideAtlas; Q09385; -.
DR   EnsemblMetazoa; K04G7.11.1; K04G7.11.1; WBGene00019402.
DR   WormBase; K04G7.11; CE39587; WBGene00019402; syf-2.
DR   eggNOG; KOG2609; Eukaryota.
DR   GeneTree; ENSGT00390000017845; -.
DR   HOGENOM; CLU_051065_3_0_1; -.
DR   InParanoid; Q09385; -.
DR   OMA; RRRMHND; -.
DR   OrthoDB; 1565402at2759; -.
DR   PhylomeDB; Q09385; -.
DR   Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR   PRO; PR:Q09385; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00019402; Expressed in embryo and 4 other tissues.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0000974; C:Prp19 complex; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR013260; mRNA_splic_SYF2.
DR   PANTHER; PTHR13264; PTHR13264; 1.
DR   Pfam; PF08231; SYF2; 1.
PE   3: Inferred from homology;
KW   Coiled coil; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   Spliceosome.
FT   CHAIN           1..234
FT                   /note="Pre-mRNA-splicing factor syf-2"
FT                   /id="PRO_0000065400"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          19..78
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..113
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   234 AA;  27660 MW;  1380F817F186FCEA CRC64;
     MSSESQSSSS GPSSSGSKMK DFNQRFRDLH KLRQRARKEN HEQVVEEDRR SKLPKNHEAK
     KERDQWQVKE LQDRKAAEDK GLDYERVRSL EMSADVTEKL EQKRKRKKNP DQGFTSYEDM
     TLRQHTRLTA ALDPDLDSYK KMRECVGGEQ FYPTADTLIH GNHYPTTAAM DKLTKDVHGQ
     VKRREQYHRR RLYDPDAPID YINEKNKKFN KKLDKYYGKY TEDIKDDLER GTAI