SIG7_CAEEL
ID SIG7_CAEEL Reviewed; 427 AA.
AC G5EEW6; Q8I4J2;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase sig-7 {ECO:0000305};
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:Q08752};
DE AltName: Full=Cyclophilin-like protein sig-7 {ECO:0000305};
DE AltName: Full=Silencer in germline 7 {ECO:0000303|PubMed:27541139};
GN Name=sig-7 {ECO:0000312|WormBase:F39H2.2a};
GN ORFNames=F39H2.2 {ECO:0000312|WormBase:F39H2.2a};
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, INTERACTION WITH AMA-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=27541139; DOI=10.1371/journal.pgen.1006227;
RA Ahn J.H., Rechsteiner A., Strome S., Kelly W.G.;
RT "A conserved nuclear cyclophilin is required for both RNA polymerase II
RT elongation and co-transcriptional splicing in Caenorhabditis elegans.";
RL PLoS Genet. 12:E1006227-E1006227(2016).
CC -!- FUNCTION: Probable PPIase that accelerates the folding of proteins (By
CC similarity). It catalyzes the cis-trans isomerization of proline imidic
CC peptide bonds in oligopeptides (By similarity). Involved in RNA
CC polymerase II (RNA pol II)-mediated transcription elongation, and in
CC primary transcript splicing, including co-transcriptional trans-
CC splicing, in association with the catalytic subunit of the RNA pol II
CC complex ama-1 (PubMed:27541139). Also plays a role in the regulation of
CC elongation-dependent phosphorylation of ama-1 to control transcription
CC (PubMed:27541139). Involved in the transcription of several genes
CC during embryogenesis and in particular, of genes related to
CC developmental processes such as gastrulation, and also regulates
CC transcription in germ cells from embryogenesis to adulthood
CC (PubMed:27541139). {ECO:0000250|UniProtKB:Q08752,
CC ECO:0000269|PubMed:27541139}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000250|UniProtKB:Q08752};
CC -!- SUBUNIT: Interacts with ama-1, the catalytic subunit of the RNA
CC polymerase II (RNA pol II) complex. {ECO:0000269|PubMed:27541139}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:27541139}. Chromosome
CC {ECO:0000269|PubMed:27541139}. Note=Co-localizes with transcriptionally
CC active chromatin in all autosomes of mitotic and meiotic nuclei in germ
CC cells. In transcriptionally inactive diakinetic oocytes, diffusely
CC localized in the nucleoplasm. {ECO:0000269|PubMed:27541139}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F39H2.2a};
CC IsoId=G5EEW6-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F39H2.2b};
CC IsoId=G5EEW6-2; Sequence=VSP_058676;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:27541139}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages from
CC embryogenesis to adulthood. {ECO:0000269|PubMed:27541139}.
CC -!- DISRUPTION PHENOTYPE: Lethal during the early stages of larval
CC development. RNAi-mediated knockdown results in 95% embryonic lethality
CC with 86.15% of embryos exhibiting gastrulation defects with decreased
CC expression of genes involved in gastrulation, and an increased
CC abundance of unspliced RNAs, decreased levels of phosphorylated ama-1
CC at the 3' end of genes and decreased histone H3 modifications, which
CC mark transcription elongation, in embryos. Rare survivors of lethality
CC have multiple developmental defects in the soma and germline including
CC a protruding vulva, multiple vulvae and failure to transition from
CC spermatogenesis to oogenesis (also called masculinization of the
CC germline or Mog phenotype). {ECO:0000269|PubMed:27541139}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL4
CC subfamily. {ECO:0000305}.
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DR EMBL; BX284601; CAB03088.2; -; Genomic_DNA.
DR EMBL; BX284601; CAD56584.1; -; Genomic_DNA.
DR PIR; T22008; T22008.
DR RefSeq; NP_492343.2; NM_059942.5. [G5EEW6-1]
DR RefSeq; NP_871805.1; NM_182005.4.
DR AlphaFoldDB; G5EEW6; -.
DR SMR; G5EEW6; -.
DR STRING; 6239.F39H2.2a; -.
DR EPD; G5EEW6; -.
DR PaxDb; G5EEW6; -.
DR PeptideAtlas; G5EEW6; -.
DR EnsemblMetazoa; F39H2.2a.1; F39H2.2a.1; WBGene00000890. [G5EEW6-1]
DR EnsemblMetazoa; F39H2.2b.1; F39H2.2b.1; WBGene00000890. [G5EEW6-2]
DR GeneID; 172664; -.
DR KEGG; cel:CELE_F39H2.2; -.
DR UCSC; F39H2.2a; c. elegans.
DR CTD; 172664; -.
DR WormBase; F39H2.2a; CE32410; WBGene00000890; sig-7. [G5EEW6-1]
DR WormBase; F39H2.2b; CE32411; WBGene00000890; sig-7. [G5EEW6-2]
DR eggNOG; KOG0415; Eukaryota.
DR GeneTree; ENSGT00940000156283; -.
DR HOGENOM; CLU_018791_2_0_1; -.
DR InParanoid; G5EEW6; -.
DR OMA; APKCCEN; -.
DR OrthoDB; 1436035at2759; -.
DR PhylomeDB; G5EEW6; -.
DR Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:G5EEW6; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000890; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IMP:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IMP:UniProtKB.
DR GO; GO:0048639; P:positive regulation of developmental growth; IMP:UniProtKB.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IMP:UniProtKB.
DR GO; GO:2000543; P:positive regulation of gastrulation; IMP:UniProtKB.
DR GO; GO:2001255; P:positive regulation of histone H3-K36 trimethylation; IMP:UniProtKB.
DR GO; GO:1905437; P:positive regulation of histone H3-K4 trimethylation; IMP:UniProtKB.
DR GO; GO:1905473; P:positive regulation of histone H3-K79 dimethylation; IMP:UniProtKB.
DR GO; GO:0050685; P:positive regulation of mRNA processing; IMP:UniProtKB.
DR GO; GO:0060282; P:positive regulation of oocyte development; IMP:UniProtKB.
DR GO; GO:2001165; P:positive regulation of phosphorylation of RNA polymerase II C-terminal domain serine 2 residues; IMP:UniProtKB.
DR GO; GO:0033120; P:positive regulation of RNA splicing; IMP:UniProtKB.
DR GO; GO:0040026; P:positive regulation of vulval development; IMP:UniProtKB.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR GO; GO:1901407; P:regulation of phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
DR CDD; cd01921; cyclophilin_RRM; 1.
DR Gene3D; 2.40.100.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR035542; CRIP.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR035538; Cyclophilin_PPIL4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR45843; PTHR45843; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Coiled coil; Isomerase; Nucleus;
KW Reference proteome; RNA-binding; Rotamase; Transcription;
KW Transcription regulation.
FT CHAIN 1..427
FT /note="Peptidyl-prolyl cis-trans isomerase sig-7"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438531"
FT DOMAIN 6..161
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT DOMAIN 241..319
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 322..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 195..227
FT /evidence="ECO:0000255"
FT COMPBIAS 331..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..378
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..69
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058676"
SQ SEQUENCE 427 AA; 50406 MW; A47D7E492615CC80 CRC64;
MAVLIETTLG DLIIDLFVKE RPRCSLNFLK LCKKKYYNLN QFHSIERNYV AQTGDPTGTG
KGGESVYSDM YGEQGRYFER EDLPKMRHTR MGIVSFVNNG DNMLGSQFFI TLGENLDYLD
DQHTIFGQVT EGLETLEKLN EQLADTNNRP FKDIRISHTI VLDDPFDEDA RISFPPRSPS
PTYEMLVKTD QIALDEKEDE DEGKTAEEIA EELQQREMAE QAQILEMVGD LKDADEVPPE
NVLFVCKLNP VTTDEDLEII FSRFGKINNC EIVRDRRSGD SLQYAFIEFD NAKSCEQAFF
KMDNVLIDDR RIHVDFSQSV SQNYKYKPKS QQQEAPKRRQ SPQRRPEVKR SHQRSPSPRR
RRSPSPKKDK KRDYRREPAR RRRSSDNHRD RDRSYRDNNR DRRDNHRDSD RDRRRHDRSP
DRRRDRR
