SPT2_DANRE
ID SPT2_DANRE Reviewed; 629 AA.
AC Q6DGN6; Q502T7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Protein SPT2 homolog;
DE AltName: Full=SPT2 domain-containing protein 1;
GN Name=spty2d1; ORFNames=zgc:111826;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Histone chaperone that stabilizes pre-existing histone
CC tetramers and regulates replication-independent histone exchange on
CC chromatin. Required for normal chromatin refolding in the coding region
CC of transcribed genes, and for the suppression of spurious
CC transcription. Binds DNA and histones and promotes nucleosome assembly
CC (in vitro). Facilitates formation of tetrameric histone complexes
CC containing histone H3 and H4 (By similarity). Modulates RNA polymerase
CC 1-mediated transcription (By similarity). Binds DNA, with a preference
CC for branched DNA species, such as Y-form DNA and Holliday junction DNA
CC (By similarity). {ECO:0000250|UniProtKB:E1BUG7,
CC ECO:0000250|UniProtKB:Q68D10}.
CC -!- SUBUNIT: Interacts with histones. Interacts with a heterotetrameric
CC complex formed by histone H3 and H4, especially when the histone
CC tetramer is not bound to DNA. {ECO:0000250|UniProtKB:Q68D10}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:E1BUG7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6DGN6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6DGN6-2; Sequence=VSP_030691;
CC -!- DOMAIN: The acidic C-terminal domain mediates interaction with histone
CC H3/H4 complexes. {ECO:0000250|UniProtKB:Q68D10}.
CC -!- SIMILARITY: Belongs to the SPT2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH76305.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; BC076305; AAH76305.1; ALT_SEQ; mRNA.
DR EMBL; BC095563; AAH95563.1; -; mRNA.
DR AlphaFoldDB; Q6DGN6; -.
DR SMR; Q6DGN6; -.
DR STRING; 7955.ENSDARP00000068017; -.
DR PaxDb; Q6DGN6; -.
DR ZFIN; ZDB-GENE-050522-212; spty2d1.
DR eggNOG; ENOG502QWHS; Eukaryota.
DR InParanoid; Q6DGN6; -.
DR PhylomeDB; Q6DGN6; -.
DR PRO; PR:Q6DGN6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0140713; F:histone chaperone activity; ISS:UniProtKB.
DR GO; GO:0001042; F:RNA polymerase I core binding; ISS:UniProtKB.
DR GO; GO:0031507; P:heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR GO; GO:0010847; P:regulation of chromatin assembly; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR013256; Chromatin_SPT2.
DR Pfam; PF08243; SPT2; 1.
DR SMART; SM00784; SPT2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..629
FT /note="Protein SPT2 homolog"
FT /id="PRO_0000315738"
FT REGION 1..522
FT /note="Important for interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q68D10"
FT REGION 53..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..629
FT /note="Important for interaction with histones"
FT /evidence="ECO:0000250|UniProtKB:Q68D10"
FT REGION 608..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 45..72
FT /evidence="ECO:0000255"
FT COILED 203..228
FT /evidence="ECO:0000255"
FT COILED 591..629
FT /evidence="ECO:0000255"
FT COMPBIAS 53..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 63..204
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_030691"
FT CONFLICT 41
FT /note="S -> A (in Ref. 1; AAH95563)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 629 AA; 69438 MW; C8FA8A670DEE960A CRC64;
MDFDSVLSIA SQNQGLSSLP KRYSLKTGPP KKDLKVGGVN SAAVQAFLKK KAVEQKNKEQ
QDKKAKEDLL AKRVELKSDR KARAMASRTK DNFRGYNGIP VIDQPKKRQS KGSSTEEQQS
STKYEGGDYD DEDNFDYEGT DSESEPSRPV KPQAISRPEY SNRVENKPKK LSAPARPASS
SMNFADLLKL AEKKQFEPVE LKVVKKTEER LRTAEEIREL EMERRVKKLD KGKDVRSDKN
SGQKDSRSQT SSNPQKKHVD RDGKNGRFPR PSEEKHQSSS TSKKPKLQAS SERTPTSAKL
HGDRSNSGSS GALNSKSAMK NGASFQAKQA PPRPSQGQRP ATPSDLTPRK GNVSLTQAKS
SISGSCPPGA ARPGQGPHKN SAHGRPSNFS TSGPSQKPAN PGKLSRPGSN APPRPGGSGV
VRPFTGDPSK QPRPGGNLQS QQFPGSSRAS LNGPKRMERG VSGSQINRMS SGPGRSQCTV
VSETISTKNI TPRPGMVQRP PGPQGPRTVI GPSGHRILVK PSGPALPPIT SSYKRKFEDE
EEYDSEMDDF IDDEGEDQDE ISKHIREIFG YDKNKYKDES DYALKFMESS WKEQQKEEAR
SLRMAVLEDE EEERRELEEM QRKNAKKRK
