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Database: UniProt
Entry: SSP1A_CAEEL
LinkDB: SSP1A_CAEEL
Original site: 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   27-MAR-2024, entry version 163.
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}.
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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; 61.
DR   ComplexPortal; CPX-3891; FACT complex hmg-4 variant.
DR   DIP; DIP-26608N; -.
DR   STRING; 6239.T20B12.8.1; -.
DR   iPTMnet; P41848; -.
DR   EPD; P41848; -.
DR   PaxDb; 6239-T20B12-8; -.
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   AGR; WB:WBGene00001974; -.
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; KQPGKCK; -.
DR   OrthoDB; 5488575at2759; -.
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 cell types or 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:0160094; P:nematode pharynx development; IGI:UniProtKB.
DR   GO; GO:0006334; P:nucleosome assembly; NAS:ComplexPortal.
DR   GO; GO:0006337; P:nucleosome disassembly; NAS: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   CDD; cd13230; PH1_SSRP1-like; 1.
DR   CDD; cd13231; PH2_SSRP1-like; 1.
DR   Gene3D; 2.30.29.150; -; 1.
DR   Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   Gene3D; 2.30.29.220; Structure-specific recognition protein (SSRP1); 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR   InterPro; IPR048993; SSRP1-like_PH1.
DR   InterPro; IPR000969; SSRP1/POB3.
DR   InterPro; IPR035417; SSRP1/POB3_N.
DR   InterPro; IPR024954; SSRP1_DD.
DR   InterPro; IPR038167; SSRP1_sf.
DR   PANTHER; PTHR45849; FACT COMPLEX SUBUNIT SSRP1; 1.
DR   PANTHER; PTHR45849:SF1; FACT COMPLEX SUBUNIT SSRP1; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   Pfam; PF21103; PH1_SSRP1-like; 1.
DR   Pfam; PF17292; POB3_N; 1.
DR   Pfam; PF08512; Rttp106-like_middle; 1.
DR   Pfam; PF03531; SSrecog; 1.
DR   PRINTS; PR00887; SSRCOGNITION.
DR   SMART; SM00398; HMG; 1.
DR   SMART; SM01287; Rtt106; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   SUPFAM; SSF50729; PH domain-like; 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
//
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