SSP1A_CAEEL
ID SSP1A_CAEEL Reviewed; 697 AA.
AC P41848;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=FACT complex subunit SSRP1-A;
DE AltName: Full=Facilitates chromatin transcription complex subunit ssrp1-A;
DE AltName: Full=HMG box-containing protein 4;
DE AltName: Full=Structure-specific recognition protein 1-A;
GN Name=hmg-4 {ECO:0000303|PubMed:30336114, ECO:0000312|WormBase:T20B12.8};
GN ORFNames=T20B12.8 {ECO:0000312|WormBase:T20B12.8};
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, 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. Binds specifically to double-stranded
CC DNA (By similarity). In embryos, may function redundantly with hmg-3 in
CC embryos to promote cell cycle progression and development of the
CC anterior pharynx (PubMed:30336114). In the germline, acts non-
CC redundantly with hmg-3 to play a role in oocyte development
CC (PubMed:30336114). {ECO:0000250|UniProtKB:Q08945,
CC ECO:0000269|PubMed:30336114}.
CC -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of hmg-4
CC and spt-16 (Probable). The FACT complex may also include hmg-3 instead
CC of hmg-4 (Probable). {ECO:0000305|PubMed:30336114}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:30336114}. Chromosome
CC {ECO:0000250|UniProtKB:Q08945}.
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 at the L4 larval stage
CC results in less than 10% embryonic lethality in offspring or death at
CC the larval stage (PubMed:30336114). RNAi-mediated knockdown at the L1
CC larval stage results in sterile animals, which do not seem to produce
CC mature oocytes, but that survive to adulthood (PubMed:30336114). Double
CC RNAi-mediated knockdown at the L4 larval stage with hmg-3 results in
CC 60% embryonic lethality in offsping (PubMed:30336114). Double RNAi-
CC mediated knockdown with hmg-3 in embryos results in defective cell
CC cycle initiation, duration and completion and in failed development of
CC the anterior pharynx (PubMed:30336114). {ECO:0000269|PubMed:30336114}.
CC -!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284603; CCD69078.1; -; Genomic_DNA.
DR PIR; T16908; T16908.
DR RefSeq; NP_498633.1; NM_066232.5.
DR AlphaFoldDB; P41848; -.
DR SMR; P41848; -.
DR BioGRID; 41261; 59.
DR ComplexPortal; CPX-3891; FACT complex hmg-4 variant.
DR DIP; DIP-26608N; -.
DR STRING; 6239.T20B12.8; -.
DR iPTMnet; P41848; -.
DR EPD; P41848; -.
DR PaxDb; P41848; -.
DR PeptideAtlas; P41848; -.
DR EnsemblMetazoa; T20B12.8.1; T20B12.8.1; WBGene00001974.
DR GeneID; 176052; -.
DR KEGG; cel:CELE_T20B12.8; -.
DR UCSC; T20B12.8; c. elegans.
DR CTD; 176052; -.
DR WormBase; T20B12.8; CE01414; WBGene00001974; hmg-4.
DR eggNOG; KOG0526; Eukaryota.
DR GeneTree; ENSGT00940000172942; -.
DR HOGENOM; CLU_017374_2_1_1; -.
DR InParanoid; P41848; -.
DR OMA; SKQPGKC; -.
DR OrthoDB; 915055at2759; -.
DR PhylomeDB; P41848; -.
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 SignaLink; P41848; -.
DR PRO; PR:P41848; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001974; Expressed in germ line (C elegans) 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
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:0006334; P:nucleosome assembly; IC:ComplexPortal.
DR GO; GO:0006337; P:nucleosome disassembly; IC:ComplexPortal.
DR GO; GO:0060465; P:pharynx development; IMP:ComplexPortal.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:1902275; P:regulation of chromatin organization; IBA:GO_Central.
DR GO; GO:0045995; P:regulation of embryonic development; IGI:UniProtKB.
DR Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 2.30.29.220; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR013719; DUF1747.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR035417; POB3_N.
DR InterPro; IPR000969; SSrcognition.
DR InterPro; IPR024954; SSRP1_dom.
DR InterPro; IPR038167; SSRP1_sf.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF17292; POB3_N; 1.
DR Pfam; PF08512; Rtt106; 1.
DR Pfam; PF03531; SSrecog; 1.
DR PRINTS; PR00887; SSRCOGNITION.
DR SMART; SM00398; HMG; 1.
DR SMART; SM01287; Rtt106; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA damage; DNA repair; DNA replication; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..697
FT /note="FACT complex subunit SSRP1-A"
FT /id="PRO_0000048609"
FT DNA_BIND 556..622
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 434..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 697 AA; 78635 MW; 90A47AD4F5B30B6F CRC64;
MAELQFPGVY VEDVGHLAFG TLKLTEKSLN FKGDKGGKSV NVTGSDIDKL KWQKLGNKPG
LRVGLNDGGA HRFGGFKDTD LEKIQSFTSS NWSQSIDQSN LFIKGWNYGQ AEVKGKTVEF
SWEDKPIFEI PCTNVSNVIA NKNEAVLEFH QNDDSKVQLM EMRFHMPIDL ENEEDADKVE
EFKKAVLAYA GLEAETEQPI CLLTDILCTT PRGRYDIKVY PTSIALHGKT YDYKIPIKSI
NRLFLVPHKD GRHVYFVLSL NPPIRQGQTR YSYLIFEFGK DEEQDLELAL TDEQLESSNG
NLRRDMTGPI YETISILFKS ICNLKITVPG RFLGSSGTPA IQCTHRQNPG LLYPMEKGFL
FIHKPAMYIR FEEISSCHFA RSDSGTVTRT FDFEIDLKYG GPLTFNAMEK EENNKLFDYL
NKKNIKIRNS QRVENTVADS SDDEIDPYKA AVTAEGRQRD DSDDDSTDED YDLDKDIKKK
KEDKESSEGT GSEPDDEYDS GSEQDSSGTG ESEPDSEQDV PSKRRKGEPK EKREKKEKRE
KKEGKKGKKD KDPNAPKRAT SAYMQWFLAS RNELKEDGDS VADVAKKGGA KWKTMSSDDK
KKWEEKAEED KSRYEKEMKE YRKNGPPSSS SKPSSSKTSK KSSGPSSSKA ISKEYISDSD
DSDDEEPKKK EKKAAPKEES EESNNGSDGS DESDDSD
