SSP1B_CAEEL
ID SSP1B_CAEEL Reviewed; 689 AA.
AC O01683;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=FACT complex subunit ssrp1-B;
DE AltName: Full=Facilitates chromatin transcription complex subunit ssrp1-B;
DE AltName: Full=HMG box-containing protein 3;
DE AltName: Full=Structure-specific recognition protein 1-B;
GN Name=hmg-3 {ECO:0000303|PubMed:30336114, ECO:0000312|WormBase:C32F10.5};
GN ORFNames=C32F10.5 {ECO:0000312|WormBase:C32F10.5};
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-4 to
CC promote cell cycle progression and development of the anterior pharynx
CC (PubMed:30336114). In the germline, acts non-redundantly with hmg-4 to
CC play a role in oocyte development (PubMed:30336114).
CC {ECO:0000250|UniProtKB:Q08945, ECO:0000269|PubMed:30336114}.
CC -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of hmg-3
CC and spt-16 (Probable). The FACT complex may also include hmg-4 instead
CC of hmg-3 (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.
CC {ECO:0000269|PubMed:30336114}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development
CC (PubMed:30336114). First expressed in embryos at the 1-cell stage, but,
CC in contrast to hmg-4, expression begins to decrease in somatic cells
CC from the 8E stage until the 2-fold stage (PubMed:30336114). However,
CC expression in the germline persists throughout the larval and adult
CC stages (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 and surviving
CC adults are sterile (PubMed:30336114). Double RNAi-mediated knockdown
CC with hmg-4 at the L4 larval stage results in 60% embryonic lethality in
CC offspring (PubMed:30336114). Double RNAi-mediated knockdown with hmg-4
CC in embryos results in defective cell cycle initiation, duration and
CC completion and in failed development of the anterior pharynx
CC (PubMed:30336114). {ECO:0000269|PubMed:30336114}.
CC -!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}.
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DR EMBL; BX284601; CCD61910.1; -; Genomic_DNA.
DR PIR; T34025; T34025.
DR RefSeq; NP_491688.1; NM_059287.3.
DR AlphaFoldDB; O01683; -.
DR SMR; O01683; -.
DR BioGRID; 37705; 104.
DR ComplexPortal; CPX-3890; FACT complex hmg-3 variant.
DR IntAct; O01683; 1.
DR STRING; 6239.C32F10.5; -.
DR iPTMnet; O01683; -.
DR EPD; O01683; -.
DR PaxDb; O01683; -.
DR PeptideAtlas; O01683; -.
DR EnsemblMetazoa; C32F10.5.1; C32F10.5.1; WBGene00001973.
DR GeneID; 172250; -.
DR KEGG; cel:CELE_C32F10.5; -.
DR UCSC; C32F10.5; c. elegans.
DR CTD; 172250; -.
DR WormBase; C32F10.5; CE08542; WBGene00001973; hmg-3.
DR eggNOG; KOG0526; Eukaryota.
DR GeneTree; ENSGT00940000172942; -.
DR HOGENOM; CLU_017374_2_1_1; -.
DR InParanoid; O01683; -.
DR OMA; YIVELHM; -.
DR OrthoDB; 915055at2759; -.
DR PhylomeDB; O01683; -.
DR PRO; PR:O01683; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001973; Expressed in germ line (C elegans) and 3 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..689
FT /note="FACT complex subunit ssrp1-B"
FT /id="PRO_0000245193"
FT DNA_BIND 561..627
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 434..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 689 AA; 77752 MW; D1F3057CF09880FB CRC64;
MTELKFKGVY VEDIGHLTCG TLTLTENSIN FIGDKGGKSV YITGTDVDKL KWQKLGNKPG
LRVGLSDGGA HRFGGFLDDD LQKIQSFTSS NWSKSINQSN LFINGWNYGQ ADVKGKNIEF
SWENEPIFEI PCTNVSNVIA NKNEAILEFH QNEQSKVQLM EMRFHMPVDL ENEEDTDKVE
EFKKAVLAYA GLEAETEQPI CLLTDILCTT PRGRYDIKVY PTSIALHGKT YDYKIPVKTI
NRLFLVPHKD GRQVYFVLSL NPPIRQGQTH YSYLIFEFGK DEEEDLELSL TDEQLDYFNG
NLQREMTGPI YETISILFKS ICNLKVTVPG RFLGSSGTPA IQCTHRQNLG LLYPMEKGFL
FIQKPVMYIR FEEISSCHFA RSDSGTVTRT FDFEIDLKTG SSLTFSAMDK EENNKLFDYL
NKKEIKIRNS HRIDNKSAGY GSSDEDDIDP YKSTVKAEGR EQDDDSDDES TDEDYDLDKD
MKKQKNDKDS SEGSGSEPDD EYDSGSEKDA SGTGESDPDE ENIEPKKKES KEKKNKREKK
EKPVKEKAVK KGKKTKDPNE PKRATTAYII WFNANRNSMK EDGDTLGDVA KKAGAKWKSM
SADDKKEWND KAAQDKARYE AEMKEYKKNG GGVEKASGPS TKKSSDQSPG KQFKSKEHIS
DTDDSDDDEP LKAKKDESDA ASESSGESD
