SPT2_CHICK
ID SPT2_CHICK Reviewed; 690 AA.
AC E1BUG7;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 3.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Protein SPT2 homolog {ECO:0000305};
GN Name=SPTY2D1;
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 GENOMIC DNA].
RC STRAIN=Red jungle fowl {ECO:0000312|Proteomes:UP000000539};
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-207.
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 [3]
RP FUNCTION, INTERACTION WITH POLR1A, AND SUBCELLULAR LOCATION.
RX PubMed=23378026; DOI=10.1242/jcs.112623;
RA Osakabe A., Tachiwana H., Takaku M., Hori T., Obuse C., Kimura H.,
RA Fukagawa T., Kurumizaka H.;
RT "Vertebrate Spt2 is a novel nucleolar histone chaperone that assists in
RT ribosomal DNA transcription.";
RL J. Cell Sci. 126:1323-1332(2013).
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) (By similarity). Modulates RNA polymerase 1-mediated
CC transcription (PubMed:23378026). Required for optimal growth in the
CC presence of the DNA damaging agents actinomycin D or mitomycin C (in
CC vitro) (PubMed:23378026). Facilitates formation of tetrameric histone
CC complexes containing histone H3 and H4 (By similarity). Modulates RNA
CC polymerase 1-mediated transcription (By similarity). Binds DNA, with a
CC preference for branched DNA species, such as Y-form DNA and Holliday
CC junction DNA (By similarity). {ECO:0000250|UniProtKB:Q68D10,
CC ECO:0000269|PubMed:23378026}.
CC -!- SUBUNIT: Interacts with POLR1A (Probable) (PubMed:23378026). Interacts
CC with histones (PubMed:23378026). Interacts with a heterotetrameric
CC complex formed by histone H3 and H4, especially when the histone
CC tetramer is not bound to DNA (By similarity).
CC {ECO:0000250|UniProtKB:Q68D10, ECO:0000269|PubMed:23378026}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:23378026}.
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}.
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DR EMBL; JH374548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN03004619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ445824; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001186523.1; NM_001199594.1.
DR AlphaFoldDB; E1BUG7; -.
DR SMR; E1BUG7; -.
DR STRING; 9031.ENSGALP00000010258; -.
DR PaxDb; E1BUG7; -.
DR Ensembl; ENSGALT00000010272; ENSGALP00000010258; ENSGALG00000006355.
DR GeneID; 423083; -.
DR KEGG; gga:423083; -.
DR CTD; 144108; -.
DR VEuPathDB; HostDB:geneid_423083; -.
DR eggNOG; ENOG502QWHS; Eukaryota.
DR GeneTree; ENSGT00940000154133; -.
DR HOGENOM; CLU_025934_0_0_1; -.
DR InParanoid; E1BUG7; -.
DR OMA; MMDFDNI; -.
DR OrthoDB; 1092455at2759; -.
DR PhylomeDB; E1BUG7; -.
DR TreeFam; TF350176; -.
DR PRO; PR:E1BUG7; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000006355; Expressed in granulocyte and 13 other tissues.
DR ExpressionAtlas; E1BUG7; baseline and differential.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0140713; F:histone chaperone activity; ISS:UniProtKB.
DR GO; GO:0001042; F:RNA polymerase I core binding; IDA: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 GO; GO:0006360; P:transcription by RNA polymerase I; IMP:UniProtKB.
DR InterPro; IPR013256; Chromatin_SPT2.
DR Pfam; PF08243; SPT2; 1.
DR SMART; SM00784; SPT2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..690
FT /note="Protein SPT2 homolog"
FT /id="PRO_0000434723"
FT REGION 1..579
FT /note="Important for interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q68D10"
FT REGION 105..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..690
FT /note="Important for interaction with histones"
FT /evidence="ECO:0000250|UniProtKB:Q68D10"
FT COILED 40..82
FT /evidence="ECO:0000255"
FT COILED 650..690
FT /evidence="ECO:0000255"
FT COMPBIAS 186..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..614
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 690 AA; 74060 MW; 1B409CA11781E621 CRC64;
MDFHNILVMA SEQQGLNAVP KRYSLAVGPP KKVPKVKGVE SAAVQAFLRR KEEEKRKKEL
EEKRKKERLL AKRIELKHDR KARAMASRTK DNFYGYNGIP VEEKPKKRRR TCENVSQAPE
AEYATENEAE QLEFAQTESE YEQEEYDEKP SKAAVKPKAP PKSAPAPLNF ADLLRLAEKK
QYEPVEIKVV KKIEERPRTA EELREREYLE RKNKRVETQK KKSEKEVKSA GISSSSKKAT
SLKECADAKL SRSAADKHAP PKSSLSSLSG TDKKPKAPAL TEKHSRSFSS SKLSQMEKGK
TSQNSSLKSP AAGSHSKLPA NGMGKTGSSF PVPSSKPMAN GAQRLPSAKE SSLKKPVHTK
PGNAAALQHE TNSSAKRPSS SLGKGGSGHP AGGSSAGPGR SSSNSGTGPG RPGSVSSPGP
GRQGSSSAAG PGRPSSSSSL GPGRLGSGSG VGPGRPGGSS STGLGRPGGS SGTGPGRPGN
STNTAPGRLG SGMGTGPGRP GVGPSAGPGR PGSSSGTGPG RPGVSPSAGP GRPGLTAVKP
RCTVVSETIS SKNLVTRPSN GQINGMRSPP GHRPVFRPQG IGRPPVGYKR QIDDDDDDDE
YDSEMDDFIE DEGEPQEEIS KHIREIFGYD RKRYKDESDY ALRYMESSWR EQQKEEARSL
RLGVQEDLEE LRREEEELKR KRQSKKLRTR
