SPT16_CAEEL
ID SPT16_CAEEL Reviewed; 1030 AA.
AC Q9N5R9;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=FACT complex subunit spt-16;
DE AltName: Full=Facilitates chromatin transcription complex subunit spt-16;
GN Name=spt-16 {ECO:0000303|PubMed:30336114, ECO:0000312|WormBase:F55A3.3};
GN ORFNames=F55A3.3 {ECO:0000312|WormBase:F55A3.3};
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=25446273; DOI=10.1016/j.ydbio.2014.10.014;
RA Krueger A.V., Jelier R., Dzyubachyk O., Zimmerman T., Meijering E.,
RA Lehner B.;
RT "Comprehensive single cell-resolution analysis of the role of chromatin
RT regulators in early C. elegans embryogenesis.";
RL Dev. Biol. 398:153-162(2015).
RN [3]
RP FUNCTION, IDENTIFICATION IN FACT COMPLEX, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=30336114; DOI=10.1016/j.ydbio.2018.10.002;
RA Suggs B.Z., Latham A.L., Dawes A.T., Chamberlin H.M.;
RT "FACT complex gene duplicates exhibit redundant and non-redundant functions
RT in C. elegans.";
RL Dev. Biol. 444:71-82(2018).
CC -!- FUNCTION: Component of the FACT complex, a general chromatin factor
CC that acts to reorganize nucleosomes. The FACT complex is involved in
CC multiple processes that require DNA as a template such as mRNA
CC elongation, DNA replication and DNA repair. During transcription
CC elongation the FACT complex acts as a histone chaperone that both
CC destabilizes and restores nucleosomal structure. It facilitates the
CC passage of RNA polymerase II and transcription by promoting the
CC dissociation of one histone H2A-H2B dimer from the nucleosome, then
CC subsequently promotes the reestablishment of the nucleosome following
CC the passage of RNA polymerase II (By similarity). In embryos, promotes
CC cell cycle progression and chromosomal segregation (PubMed:25446273,
CC PubMed:30336114). Plays a role in the development of the anterior
CC pharynx during embryonic development (PubMed:30336114).
CC {ECO:0000250|UniProtKB:Q9Y5B9, ECO:0000269|PubMed:25446273,
CC ECO:0000269|PubMed:30336114}.
CC -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of spt-16
CC and hmg-3 or hmg-4. {ECO:0000305|PubMed:30336114}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30336114}. Chromosome
CC {ECO:0000250|UniProtKB:Q9Y5B9}.
CC -!- TISSUE SPECIFICITY: Expressed in the germline and somatic cells.
CC {ECO:0000269|PubMed:30336114}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development
CC (PubMed:30336114). First expressed in embryos at the 1-cell stage
CC (PubMed:30336114). {ECO:0000269|PubMed:30336114}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in embryos results in
CC failed hatching in 83% of animals (PubMed:30336114). In addition, these
CC embryos lack the anterior pharynx (PubMed:30336114). RNAi-mediated
CC knockdown at the L4 larval stage results in failed development of the
CC anterior pharynx (PubMed:30336114). RNAi-mediated knockdown at this
CC stage results in defective cell cycle initiation, duration and
CC completion in embryos, and abnormalities in chromosome segregation
CC (PubMed:25446273, PubMed:30336114). {ECO:0000269|PubMed:25446273,
CC ECO:0000269|PubMed:30336114}.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Although related to the peptidase M24 family, this protein
CC lacks conserved active site residues suggesting that it may lack
CC peptidase activity. {ECO:0000305}.
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DR EMBL; BX284601; CCD66831.1; -; Genomic_DNA.
DR RefSeq; NP_492821.1; NM_060420.4.
DR AlphaFoldDB; Q9N5R9; -.
DR SMR; Q9N5R9; -.
DR BioGRID; 38394; 31.
DR ComplexPortal; CPX-3890; FACT complex hmg-3 variant.
DR ComplexPortal; CPX-3891; FACT complex hmg-4 variant.
DR STRING; 6239.F55A3.3; -.
DR iPTMnet; Q9N5R9; -.
DR EPD; Q9N5R9; -.
DR PaxDb; Q9N5R9; -.
DR PeptideAtlas; Q9N5R9; -.
DR EnsemblMetazoa; F55A3.3.1; F55A3.3.1; WBGene00018849.
DR GeneID; 172984; -.
DR KEGG; cel:CELE_F55A3.3; -.
DR UCSC; F55A3.3; c. elegans.
DR CTD; 172984; -.
DR WormBase; F55A3.3; CE17113; WBGene00018849; spt-16.
DR eggNOG; KOG1189; Eukaryota.
DR GeneTree; ENSGT00390000014495; -.
DR HOGENOM; CLU_004627_1_0_1; -.
DR InParanoid; Q9N5R9; -.
DR OMA; HQFFLDG; -.
DR OrthoDB; 145488at2759; -.
DR PhylomeDB; Q9N5R9; -.
DR Reactome; R-CEL-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-CEL-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-CEL-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-CEL-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-CEL-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:Q9N5R9; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00018849; Expressed in embryo and 4 other tissues.
DR GO; GO:0035101; C:FACT complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0034724; P:DNA replication-independent chromatin organization; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; IC:ComplexPortal.
DR GO; GO:0006337; P:nucleosome disassembly; IC:ComplexPortal.
DR GO; GO:0060465; P:pharynx development; IMP:UniProtKB.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IMP:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd01091; CDC68-like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR013719; DUF1747.
DR InterPro; IPR029148; FACT-Spt16_Nlobe.
DR InterPro; IPR013953; FACT_Spt16.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR040258; Spt16.
DR InterPro; IPR033825; Spt16_M24.
DR PANTHER; PTHR13980; PTHR13980; 1.
DR Pfam; PF14826; FACT-Spt16_Nlob; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF08512; Rtt106; 1.
DR Pfam; PF08644; SPT16; 1.
DR SMART; SM01285; FACT-Spt16_Nlob; 1.
DR SMART; SM01287; Rtt106; 1.
DR SMART; SM01286; SPT16; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; DNA damage; DNA repair; DNA replication; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1030
FT /note="FACT complex subunit spt-16"
FT /id="PRO_0000245173"
FT REGION 435..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 424..445
FT /evidence="ECO:0000255"
FT COILED 623..645
FT /evidence="ECO:0000255"
FT COILED 987..1007
FT /evidence="ECO:0000255"
FT COMPBIAS 435..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..990
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1018
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1030 AA; 116865 MW; 322B52675BEDAADD CRC64;
MSGKRAVLNK DLFFQRAERL YEHWEKGADG LDSIKSLAFV YGETDNPYTK TSALFTWLFG
HEIADTVLLL LKDHIYILGS NRKVEFFGSV TGDNQSSGKV PTVSTLLRDK TDKDAGNFEK
LIDHIKSAGG DVGNFVKEKF SSEFVSSWNK ALEEGGVNKN DVTLAFTHLF AVKDDKEMDL
IRKSAQATTA SWTAARARYV EIIDQEKRVR HSVLSNEFAA FMKDSKVQQA LAKYEADTCY
DPIVMSGGNY SFKWNHESSE SHLHSQFGTI ITSFGARLSE YCTNLTRTML IFPSSELETA
YEAILAAELA VIAALKPGAK LSDVYKIGID TLTEKSPKLA ETLNKKELGF ATGIEFRESR
LAISAKCDEV VKAGMVFIVY IGVDSIPNKN KGEKGKPAAI AISDTILVKE EGDNEILTEK
AKSRLKSNVI KFKEEQENRE AEKDNDQKKM LGRGQRSVVL TDQTRNKTTN EELRKERQKE
LGVQLNELAK ARLSKQGGGT DEKKSKKSNV SYKTEERFPQ DADVQKMLIF VDRKYDSVVV
PIFGIPVPFH ISMIKNCSQS VEGDFTYLRI NFATPGSQVG KDSGQFPHPL AHYMKELTFR
ASNIKDHHSD STAPSHNLST AFRLIKEMQK RFKTEEAEER EKEGAVKQDK LILSQNKLNP
KLKDLLIRPN IIQKRITGSL EAHTNGFRYT SLRGDRIDVL YNNIKHAFFQ PCDNEMIILL
HFHLKNPVLW GKKKYKDVQF YTEVGEITTD LGKYHHMQDR DDMQSEQQER EMRRRLNAAF
NSFCEKVSRL TNDQFEFDSP FAGLGFFGVP YRSATTLKPT ASCLVNLTEW PTFIVTLSEV
ELVHFERVSL QLKNFDMVFI FKDYKIKPQM VAQIPMSSID KIKEWLHTCD IWYSEGIQSL
NWAKVMKTIT DDLEAFFEEG GWSFLNVESD NEEAMDDSDD SDAYDPEEED ASAGSGSESD
EDESEGEETE SDDDDEGSLD SDESEGKDWS DLEEEAANAD KRREVEEPSR DRDRKRPHSS
KSGPSHKRRK
