MTG16_CHICK
ID MTG16_CHICK Reviewed; 591 AA.
AC Q5F3B1; Q5IJ74; Q5IJ75;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Protein CBFA2T3;
GN Name=CBFA2T3; ORFNames=RCJMB04_23o9;
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] (ISOFORM 1).
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 19-591 (ISOFORMS 1 AND 2), AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15649458; DOI=10.1016/j.ydbio.2004.10.010;
RA Koyano-Nakagawa N., Kintner C.;
RT "The expression and function of MTG/ETO family proteins during
RT neurogenesis.";
RL Dev. Biol. 278:22-34(2005).
CC -!- FUNCTION: Functions as a transcriptional repressor. Regulates the
CC proliferation and the differentiation of erythroid progenitors. Plays a
CC role in granulocyte differentiation. May also function as an A-kinase-
CC anchoring protein (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm
CC {ECO:0000250}. Golgi apparatus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5F3B1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5F3B1-2; Sequence=VSP_028628;
CC -!- DEVELOPMENTAL STAGE: Expressed in the spinal cord of stage 22 embryos.
CC Expressed during neurogenesis in the mantle zone of the spinal cord in
CC domains corresponding to interneurons. {ECO:0000269|PubMed:15649458}.
CC -!- SIMILARITY: Belongs to the CBFA2T family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW49212.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAW49213.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ851739; CAH65373.1; -; mRNA.
DR EMBL; AY714074; AAW49212.1; ALT_INIT; mRNA.
DR EMBL; AY714075; AAW49213.1; ALT_INIT; mRNA.
DR RefSeq; NP_001025751.1; NM_001030580.1. [Q5F3B1-1]
DR AlphaFoldDB; Q5F3B1; -.
DR BMRB; Q5F3B1; -.
DR SMR; Q5F3B1; -.
DR STRING; 9031.ENSGALP00000038113; -.
DR GeneID; 415846; -.
DR KEGG; gga:415846; -.
DR CTD; 863; -.
DR VEuPathDB; HostDB:geneid_415846; -.
DR eggNOG; ENOG502QTD6; Eukaryota.
DR InParanoid; Q5F3B1; -.
DR OrthoDB; 334242at2759; -.
DR PhylomeDB; Q5F3B1; -.
DR PRO; PR:Q5F3B1; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.20.120.1110; -; 1.
DR InterPro; IPR013289; CBFA2T1/2/3.
DR InterPro; IPR013292; CBFA2T3.
DR InterPro; IPR014896; NHR2.
DR InterPro; IPR037249; TAFH/NHR1_dom_sf.
DR InterPro; IPR003894; TAFH_NHR1.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR10379; PTHR10379; 1.
DR Pfam; PF08788; NHR2; 1.
DR Pfam; PF07531; TAFH; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR PRINTS; PR01875; ETOFAMILY.
DR PRINTS; PR01878; MTG16PROTEIN.
DR SMART; SM00549; TAFH; 1.
DR SUPFAM; SSF158553; SSF158553; 1.
DR PROSITE; PS51119; TAFH; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Differentiation; Golgi apparatus;
KW Metal-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..591
FT /note="Protein CBFA2T3"
FT /id="PRO_0000307175"
FT DOMAIN 112..207
FT /note="TAFH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00440"
FT ZN_FING 501..537
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 1..381
FT /note="Mediates localization to the nucleus"
FT /evidence="ECO:0000250"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 433..488
FT /evidence="ECO:0000255"
FT COMPBIAS 41..55
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 501
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 504
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 512
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 515
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 521
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 533
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 537
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT VAR_SEQ 68
FT /note="M -> NRDAVPPTFLPRGRFHGCLKWSMVCLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15649458"
FT /id="VSP_028628"
SQ SEQUENCE 591 AA; 64874 MW; 6190232E1346735E CRC64;
MPGGTPRLEG HPFSKTGPDP ATPGAATMPD SPADVKTQPR STPPNMPPPP PAVTQGATRH
PSFTPSTMMN GSSHSPTAIN GAPSTPNGFS NGPATSSSAS LSTHQLPPAC GARQLSKLKR
FLTTLQQFGN DISPEIGERV RTLVLGLVNS TLTIEEFHAK LQEATNFPLR PFVIPFLKAN
LPLLQRELLH CARMAKQSPA QYLAQHEQLL LDANASSPID SSELLLEVSE SGKRRTPDRT
KENGLDRDPL HPEHLSKRPC TMSPAQRYSP SNGLSHPPNG LPHPPGPPPQ HYRLEDMAMA
HHYRDAYRHA DPRERPRPAV HGARQEEVID HRLTDREWAE EWKHLNNLLN CIMDMVEKTR
RSLTVLRRCQ EADREELNHW IRRYSDAEDM KKGSPPSARP HNSSSSSEAP QLDVHRDFAP
RPLSGYMPEE IWRKAEEAVN EVKRQAMSEL QKAVSDAERK AHELITTERA KMERALAEAK
RQASEDALTV INQQEDSSES CWNCGRKASE TCSGCNTARY CGSFCQHKDW EKHHHVCGQT
LQGLPAPSVP TAVGQPEAVP PMASSPSDAG SAGASRAGTP GTPAPLESAS R
