SSRP1_CHICK
ID SSRP1_CHICK Reviewed; 706 AA.
AC Q04678; Q08780; Q5ZLU3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=FACT complex subunit SSRP1;
DE AltName: Full=Facilitates chromatin transcription complex subunit SSRP1;
DE AltName: Full=Recombination signal sequence recognition protein 1;
DE AltName: Full=Structure-specific recognition protein 1;
DE AltName: Full=T160;
GN Name=SSRP1; Synonyms=CIIDBP; ORFNames=RCJMB04_4n20;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 39-706.
RX PubMed=8464746; DOI=10.1093/nar/21.6.1493;
RA Wang L., Precht P., Balakir R., Horton W.E. Jr.;
RT "Rat and chick cDNA clones encoding HMG-like proteins.";
RL Nucleic Acids Res. 21:1493-1493(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 412-706.
RC TISSUE=Lens;
RX PubMed=7904558; DOI=10.1242/dev.119.2.433;
RA Funahashi J., Sekido R., Murai K., Kamachi Y., Kondoh H.;
RT "Delta-crystallin enhancer binding protein delta EF1 is a zinc finger-
RT homeodomain protein implicated in postgastrulation embryogenesis.";
RL Development 119:433-446(1993).
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). {ECO:0000250}.
CC -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of SSRP1
CC and SUPT16H. Also a component of a CK2-SPT16-SSRP1 complex which forms
CC following UV irradiation, composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2
CC and CSNK2B (By similarity). {ECO:0000250}.
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}.
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DR EMBL; AJ719641; CAG31300.1; -; mRNA.
DR EMBL; L08815; AAA48685.1; -; mRNA.
DR EMBL; D14315; BAA03261.1; -; mRNA.
DR PIR; S78050; S78050.
DR RefSeq; NP_001005796.1; NM_001005796.2.
DR AlphaFoldDB; Q04678; -.
DR SMR; Q04678; -.
DR BioGRID; 676756; 1.
DR STRING; 9031.ENSGALP00000012145; -.
DR PaxDb; Q04678; -.
DR GeneID; 396509; -.
DR KEGG; gga:396509; -.
DR CTD; 6749; -.
DR VEuPathDB; HostDB:geneid_396509; -.
DR eggNOG; KOG0526; Eukaryota.
DR InParanoid; Q04678; -.
DR OrthoDB; 915055at2759; -.
DR PhylomeDB; Q04678; -.
DR PRO; PR:Q04678; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0035101; C:FACT complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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:1902275; P:regulation of chromatin organization; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Chromosome; DNA damage; DNA repair; DNA replication; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..706
FT /note="FACT complex subunit SSRP1"
FT /id="PRO_0000048605"
FT DNA_BIND 545..613
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 458..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..495
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 39..40
FT /note="KV -> IP (in Ref. 2; AAA48685)"
FT /evidence="ECO:0000305"
FT CONFLICT 412..415
FT /note="GKLF -> TATV (in Ref. 3; BAA03261)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="A -> S (in Ref. 2; AAA48685)"
FT /evidence="ECO:0000305"
FT CONFLICT 517..521
FT /note="PAKKA -> SSQEGP (in Ref. 2; AAA48685)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="A -> V (in Ref. 2; AAA48685)"
FT /evidence="ECO:0000305"
FT CONFLICT 646..647
FT /note="AA -> SP (in Ref. 2; AAA48685)"
FT /evidence="ECO:0000305"
FT CONFLICT 682
FT /note="K -> N (in Ref. 3; BAA03261)"
FT /evidence="ECO:0000305"
FT CONFLICT 685..702
FT /note="DSEDESGASPAQSSEDSA -> QEEEHRGANRPKPHKSPQQAP (in Ref.
FT 3; BAA03261)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="S -> R (in Ref. 2; AAA48685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 706 AA; 80026 MW; D260F78BC43C3344 CRC64;
MADTLEFNEI YQEVKGSMND GRLRLSRQGV IFKNSKTGKV DNIQASELAE GVWRRVALGH
GLKLLTKNGH VYKYDGFRES EFDKLSDFFK AHYRLELAEK DLCVKGWNWG TVRFGGQLLS
FDIGEQPVFE IPLSNVSQCT TGKNEVTLEF HQNDDAEVSL MEVRFYVPPT QEDGVDPVEA
FAQNVLSKAD VIQATGDAIC IFRELQCLTP RGRYDIRIYP TFLHLHGKTF DYKIPYTTVL
RLFLLPHKDQ RQMFFVISLD PPIKQGQTRY HFLILLFSKD EDISLTLNMN EEEVEKRFEG
RLTKNMSGSL YEMVSRVMKA LVNRKITVPG NFQGHSGAQC ITCSYKASSG LLYPLERGFI
YVHKPPVHIR FDEISFVNFA RGTTTTRSFD FEIETKQGTQ YTFSSIEREE YGKLFDFVNA
KKLNIKNRGL KEGMKQSYDE YADSDEDQHD AYLERMKEEG KIREENANDS SDGSGEETDE
SFNPGEEDDD VAEEFDSNAS ASSSSGDGDS DRGEKKPAKK AKIVKDRKPR KKQVESKKGK
DPNAPKRPMS AYMLWLNANR EKIKSDHPGI SITDLSKKAG ELWKAMSKEK KEEWDRKAED
AKRDYEKAMK EYSVGNKSES SKMERSKKKK KKQEKQMKGK GEKKGAASKS SSSTKSSAKT
MSESFKSKEF VSSDESSSAE SKKEDSEDES GASPAQSSED SASGSD
