SSRP1_XENLA
ID SSRP1_XENLA Reviewed; 693 AA.
AC Q9W602; Q640L1;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=FACT complex subunit SSRP1;
DE AltName: Full=DNA unwinding factor 87 kDa subunit;
DE Short=DUF87;
DE AltName: Full=Facilitates chromatin transcription complex subunit ssrp1;
DE AltName: Full=Structure-specific recognition protein 1;
GN Name=ssrp1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 228-234; 450-462 AND
RP 476-484, FUNCTION, AND INTERACTION WITH SUPT16H.
RC TISSUE=Egg;
RX PubMed=10209116; DOI=10.1016/s0960-9822(99)80160-2;
RA Okuhara K., Ohta K., Seo H., Shioda M., Yamada T., Tanaka Y., Dohmae N.,
RA Seyama Y., Shibata T., Murofushi H.;
RT "DNA unwinding factor involved in DNA replication in cell-free extracts of
RT Xenopus eggs.";
RL Curr. Biol. 9:341-350(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-454.
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH VCP.
RX PubMed=10682845; DOI=10.1016/s0014-5793(99)01673-7;
RA Yamada T., Okuhara K., Iwamatsu A., Seo H., Ohta K., Shibata T.,
RA Murofushi H.;
RT "p97 ATPase, an ATPase involved in membrane fusion, interacts with DNA
RT unwinding factor (DUF) that functions in DNA replication.";
RL FEBS Lett. 466:287-291(2000).
RN [4]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=12646158; DOI=10.1016/s0006-291x(03)00307-3;
RA Seo H., Okuhara K., Kurumizaka H., Yamada T., Shibata T., Ohta K.,
RA Akiyama T., Murofushi H.;
RT "Incorporation of DUF/FACT into chromatin enhances the accessibility of
RT nucleosomal DNA.";
RL Biochem. Biophys. Res. Commun. 303:8-13(2003).
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. {ECO:0000269|PubMed:10209116, ECO:0000269|PubMed:12646158}.
CC -!- SUBUNIT: Component of the FACT complex (also known as the DUF complex),
CC a stable heterodimer of ssrp1 and supt16h. May also be a component of a
CC ck2-spt16-ssrp1 complex which forms following UV irradiation, composed
CC of ssrp1, supt16h, csnk2a1, csnk2a2 and csnk2b. The FACT complex may
CC also interact with vcp.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q05344}.
CC Chromosome {ECO:0000250|UniProtKB:Q05344}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q05344}. Note=Colocalizes with RNA polymerase II
CC on chromatin. Recruited to actively transcribed loci.
CC {ECO:0000250|UniProtKB:Q05344}.
CC -!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH82613.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={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; AB004793; BAA76333.1; -; mRNA.
DR EMBL; BC082613; AAH82613.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001084164.1; NM_001090695.1.
DR AlphaFoldDB; Q9W602; -.
DR SMR; Q9W602; -.
DR BioGRID; 100669; 1.
DR MaxQB; Q9W602; -.
DR GeneID; 399344; -.
DR KEGG; xla:399344; -.
DR CTD; 399344; -.
DR Xenbase; XB-GENE-994299; ssrp1.S.
DR OrthoDB; 915055at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 399344; Expressed in spleen and 19 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; Direct protein sequencing; DNA damage; DNA repair;
KW DNA replication; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..693
FT /note="FACT complex subunit SSRP1"
FT /id="PRO_0000245191"
FT DNA_BIND 541..609
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 460..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..492
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..531
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 78668 MW; 26E84B1D657E516B CRC64;
MADTLEFNDI YQEVKGSMND GRLRLSRAGL MYKNNKTGKV ENISAADIAE VVWRRVALGH
GIKLLTNGGH VYKYDGFRET EYDKLFDYFK SHFSVELVEK DLCVKGWNWG SVRFGGQLLS
FDIGDQPAFE LPLSNVSQCT TGKNEVTLEF HQNDDSEVSL MEIRFYVPPT QDDGGDSVEA
FAQNVLSKAD VIQATGDAVC IFRELQCLTP RGRYDIRIYP TFLHLHGKTF DYKIPYTTVL
RLFLLPHKDQ RQMFFVISLD PPIKQGQTRY HFLILLFSKD EDMTLTLNMS EEEVERRFEG
KLKKSMSGCL YEMVSRVMKA LVNRKITVPG NFLGHSGSQC ITCSYKASSG LLYPLERGFI
YVHKPPVHIR FDEITCVNFA RGTTTTRSFD FEIETKQGSQ YTFSSIEREE YGKLFDFVNA
KKLSIKNRGL KEGMKPAYDD YADSDEDQHD AYLERMKEEG KIRENADSDE SGDETDESFN
PGEEEEEVAE EFDSNPSASS SSADSDDDTD KKKDAKRAKI VKQKKPRKKP EAKKTKDPGA
PKRPMSAYML WLNASREKIK SENPGISITD LSKKAGEIWK NMSRDKKEEW DRRAEEAKRD
YEKAMKEYNT SAPTEASKKE KKTKGEKKKA ETSEKKKQKP SSPARAAPKL NSESFKSKEF
VSSDDSSSDD SAQKKDSEEI ASTPASSAES GSD
