ID F1S8K5_PIG Unreviewed; 1083 AA.
AC F1S8K5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN Name=SUPT16H {ECO:0000313|Ensembl:ENSSSCP00000022646.2,
GN ECO:0000313|VGNC:VGNC:93622};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000022646.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000022646.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000022646.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDA51427.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000022646.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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:0000256|RuleBase:RU367052}.
CC -!- SUBUNIT: Component of the FACT complex.
CC {ECO:0000256|RuleBase:RU367052}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367052}.
CC Chromosome {ECO:0000256|RuleBase:RU367052}.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
CC {ECO:0000256|ARBA:ARBA00010779, ECO:0000256|RuleBase:RU367052}.
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DR EMBL; DQIR01095951; HDA51427.1; -; Transcribed_RNA.
DR EMBL; DQIR01167597; HDB23074.1; -; Transcribed_RNA.
DR RefSeq; XP_001929215.3; XM_001929180.5.
DR STRING; 9823.ENSSSCP00000022646; -.
DR PaxDb; 9823-ENSSSCP00000022646; -.
DR Ensembl; ENSSSCT00000031400.3; ENSSSCP00000022646.2; ENSSSCG00000022900.3.
DR GeneID; 100155525; -.
DR KEGG; ssc:100155525; -.
DR CTD; 11198; -.
DR VGNC; VGNC:93622; SUPT16H.
DR eggNOG; KOG1189; Eukaryota.
DR GeneTree; ENSGT00390000014495; -.
DR HOGENOM; CLU_004627_0_0_1; -.
DR OMA; GKNNLQW; -.
DR OrthoDB; 169847at2759; -.
DR TreeFam; TF300341; -.
DR Reactome; R-SSC-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-SSC-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SSC-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SSC-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-SSC-75955; RNA Polymerase II Transcription Elongation.
DR Proteomes; UP000008227; Chromosome 7.
DR Bgee; ENSSSCG00000022900; Expressed in hindlimb bud and 45 other cell types or tissues.
DR GO; GO:0035101; C:FACT complex; IBA:GO_Central.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006337; P:nucleosome disassembly; IEA:Ensembl.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IBA:GO_Central.
DR CDD; cd01091; CDC68-like; 1.
DR Gene3D; 2.30.29.150; -; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR Gene3D; 2.30.29.210; FACT complex subunit Spt16p/Cdc68p; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
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; IPR013719; RTT106/SPT16-like_middle_dom.
DR InterPro; IPR040258; Spt16.
DR InterPro; IPR048969; SPT16_C.
DR InterPro; IPR033825; Spt16_M24.
DR PANTHER; PTHR13980; CDC68 RELATED; 1.
DR PANTHER; PTHR13980:SF15; FACT COMPLEX SUBUNIT SPT16; 1.
DR Pfam; PF14826; FACT-Spt16_Nlob; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF08512; Rttp106-like_middle; 1.
DR Pfam; PF08644; SPT16; 1.
DR Pfam; PF21091; SPT16_C; 1.
DR SMART; SM01285; FACT-Spt16_Nlob; 1.
DR SMART; SM01287; Rtt106; 1.
DR SMART; SM01286; SPT16; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
PE 1: Evidence at protein level;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU367052};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367052};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367052};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU367052};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367052};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1S8K5};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU367052};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU367052}.
FT DOMAIN 41..204
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 565..725
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 842..932
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 528..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..1007
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1054
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 123660 MW; AF2D2F11218768B9 CRC64;
MLPGHWESAG FRGRERVAEP GPRVILGTRG GAASVAMAVT LDKDAYYRRV KRLYSNWRKG
EDEYANVDAI VVSVGVDEEI VYAKSTALQT WLFGYELTDT IMVFCDDKII FMASKKKVEF
LKQIANTKGN ENANGAPAIT LLIREKNESN KSSFDKMIEA IKESKNGKKI GVFSKDKFPG
EFMKSWNDCL NKEGFDKIDI SAVVAYTIAV KEDGELNLMK KAASITSEVF NKFFKERVME
IVDADEKVRH SKLAESVEKA IEEKKYLAGA DPSTVEMCYP PIIQSGGNYN LKFSVVSDKN
HMHFGAITCA MGIRFKSYCS NLVRTLMVDP SQEVQENYNF LLQLQEELLK ELRHGVKICD
VYNAVMDVVK KQKPELLNKI TKNLGFGMGI EFREGSLVIN SKNQYKLKKG MVFSINLGFS
DLTNKEGKKP EEKTYALFIG DTVLVDEDGP ATVLTSVKKK VKNVGIFLKN EDEEEEEEEK
DEAEDLLGRG SRAALLTERT RNEMTAEEKR RAHQKELAAQ LNEEAKRRLT EQKGEQQIQK
ARKSNVSYKN PSLMPKEPHI REMKIYIDKK YETVIMPVFG IATPFHIATI KNISMSVEGD
YTYLRINFYC PGSALGRNEG NIFPNPEATF VKEITYRASN MKAPGEQTVP ALNLQNAFRI
IKEVQKRYKT REAEEKEKEG IVKQDSLVIN LNRSNPKLKD LYIRPNIAQK RMQGSLEAHV
NGFRFTSVRG DKVDILYNNI KHALFQPCDG EMIIVLHFHL KNAIMFGKKR HTDVQFYTEV
GEITTDLGKH QHMHDRDDLY AEQMEREMRH KLKTAFKNFI EKVEALTKEE LEFEVPFRDL
GFNGAPYRST CLLQPTSSAL VNATEWPPFV VTLDEVELIH FERVQFHLKN FDMVIVYKDY
SKKVTMINAI PVASLDPIKE WLNSCDLKYT EGVQSLNWTK IMKTIVDDPE GFFEQGGWSF
LEPEGEGSDA EEGDSESEIE DETFNPSEDD YEEEEEDSDE DYSSEAEESD YSKESLGSEE
ESGKDWDELE EEARKADRES RYEEEEEQSR SMSRKRKASV HSSGRGSNRG SRHSSAPPKK
KRK
//