SP16H_XENLA
ID SP16H_XENLA Reviewed; 1035 AA.
AC Q9W603; Q6GQJ6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=FACT complex subunit SPT16;
DE AltName: Full=DNA unwinding factor 140 kDa subunit;
DE Short=DUF140;
DE AltName: Full=Facilitates chromatin transcription complex subunit spt16;
GN Name=supt16h;
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 536-549 AND 894-902,
RP FUNCTION, AND INTERACTION WITH SSRP1.
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 1-640.
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-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.
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. {ECO:0000250,
CC ECO:0000269|PubMed:10209116, ECO:0000269|PubMed:12646158}.
CC -!- SUBUNIT: Component of the FACT complex (also called the DUF complex), a
CC stable heterodimer of ssrp1 and supt16h. May also be a component of a
CC ck2-spt16-ssrp1 complex composed of ssrp1, supt16h, csnk2a1, csnk2a2
CC and csnk2b. The FACT complex may also interact with vcp. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- DOMAIN: The Glu-rich acidic region in C-terminus is essential for FACT
CC activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Although related to the peptidase M24 family, this protein
CC lacks conserved active site residues suggesting that it may lack
CC peptidase activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH72746.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA76334.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB004794; BAA76334.1; ALT_FRAME; mRNA.
DR EMBL; BC072746; AAH72746.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001084166.1; NM_001090697.1.
DR AlphaFoldDB; Q9W603; -.
DR SMR; Q9W603; -.
DR BioGRID; 100670; 1.
DR MEROPS; M24.974; -.
DR GeneID; 399345; -.
DR KEGG; xla:399345; -.
DR CTD; 399345; -.
DR Xenbase; XB-GENE-979310; supt16h.S.
DR OMA; NREVLWA; -.
DR OrthoDB; 145488at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 399345; Expressed in gastrula and 19 other tissues.
DR GO; GO:0035101; C:FACT complex; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd01091; CDC68-like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR013719; DUF1747.
DR InterPro; IPR029148; FACT-Spt16_Nlobe.
DR InterPro; IPR013953; FACT_Spt16.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR040258; Spt16.
DR InterPro; IPR033825; Spt16_M24.
DR PANTHER; PTHR13980; PTHR13980; 1.
DR Pfam; PF14826; FACT-Spt16_Nlob; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF08512; Rtt106; 1.
DR Pfam; PF08644; SPT16; 1.
DR SMART; SM01285; FACT-Spt16_Nlob; 1.
DR SMART; SM01287; Rtt106; 1.
DR SMART; SM01286; SPT16; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; Direct protein sequencing; DNA damage; DNA repair;
KW DNA replication; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1035
FT /note="FACT complex subunit SPT16"
FT /id="PRO_0000245171"
FT REGION 491..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 432..500
FT /evidence="ECO:0000255"
FT COMPBIAS 500..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..992
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1035
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1035 AA; 118440 MW; C8129B7FE0082F3B CRC64;
MAVTLDKEAY YRRIKRFFGS WKKGDDEFAN VDAIVVSVGV DEEIVYAKST ALQTWLFGYE
LTDTIMVFCE EKILFMASKK KVEFLKQIAN TKGNENANGT PAITLLVREK QNESNKGNFD
KMIEAIKVSK KGKRIGVFIK DKFPGDFMKS WYDILNKESF EKVDISASVA YTIAVKEEGE
LNLMKKAASI TSDVFSKFFK DRVMEIVDAD EKVRHGKLAE SVEKAIEDKK YLGGTDPSTI
EMCYPPIIQS GGNYNLKFSV VSDKNHMHFG AITCALGIRY KSYCSNLVRT LMVDPTQEMQ
ENYNFLLQLQ EELLKELKHG AKICDAYQVI MDQVKKQKPD LMSKITKTLG FAMGIEFREG
SLVINNKNQY KLKKGMVFSV HLGLAELNNK MGKKPEEKTY ALFVGDTVLV NEEGAATVLT
NVKKKVKNVG IFLKKEDEEE EEEEKDEAED LLGRGSRAAA LLTERTRNEM TAEEKRRTHQ
KELATQLNDE AKRRLTEQKG GQQTMKARKS NVSYKNASQV PKEPELREMK LYIDKKYETV
IMPVFGISTP FHIATIKNIS MSVEGDYTYL RINFFCPGSA LGRNEGNIFP NPEATFVKEI
TYRASNVKTP GDPSVPSLNL QNAFRIIKEV QKRYKTREAE EKEKEGIVKQ DSLVINLNRS
NPKLKDLYIR PNIAQKRMQG SLEAHVNGFR FTSVRGDKVD ILYNNIKHAL FQPCDGEMII
VLHFHLKNAI MFGKKRHTDV QFYTEVGEIT TDLGKHQHMH DRDDLYAEQL EREMRHKLKT
AFKNFIEKVE SLTKEDLEFE IPFRDLGFNG APYRSTCLLQ PTSSSLVNTT EWPPFVVTLD
EVELVHFERV QFHLKNFDMV IVYKEYGKKV TMINAIPMAS LDPIKEWLNS CDIKYTEGVQ
SLNWTKIMKT IVDDPEGFFE QGGWSFLEPD GEGSDAAEGD SESELDDETF NPSEDEEEEE
EDSDEDYSDE TEDSVDSEES ADSEEESGKD WDELEEEARK ADRESLYEEV EEQKSGNRKR
KGHAPLPNPS KKRKK
