SMYD4_CHICK
ID SMYD4_CHICK Reviewed; 742 AA.
AC Q5F3V0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=SET and MYND domain-containing protein 4;
DE EC=2.1.1.-;
GN Name=SMYD4; ORFNames=RCJMB04_6f24;
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].
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).
CC -!- FUNCTION: Plays a critical role in cardiac development. Acts as a key
CC epigenetic regulator of gene expression during cardiac development via
CC its dual activities as a methyltransferase and negative regulator of
CC HDAC1. {ECO:0000250|UniProtKB:Q08C84, ECO:0000250|UniProtKB:Q8IYR2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8BTK5}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8BTK5}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AJ851550; CAH65184.1; -; mRNA.
DR RefSeq; NP_001025886.1; NM_001030715.1.
DR AlphaFoldDB; Q5F3V0; -.
DR SMR; Q5F3V0; -.
DR STRING; 9031.ENSGALP00000004786; -.
DR GeneID; 417562; -.
DR KEGG; gga:417562; -.
DR CTD; 114826; -.
DR VEuPathDB; HostDB:geneid_417562; -.
DR eggNOG; KOG2084; Eukaryota.
DR InParanoid; Q5F3V0; -.
DR PhylomeDB; Q5F3V0; -.
DR PRO; PR:Q5F3V0; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd10536; SET_SMYD4; 1.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044421; SMYD4_SET.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SUPFAM; SSF48452; SSF48452; 2.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..742
FT /note="SET and MYND domain-containing protein 4"
FT /id="PRO_0000227787"
FT DOMAIN 230..569
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 295..334
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 110..112
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 418
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 534..535
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H7B4"
FT BINDING 568
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
SQ SEQUENCE 742 AA; 82027 MW; 3B464F4E8A994B78 CRC64;
MALPVEEWRR SAARCWAALE PALRERLAAA PLGEALRMGC GLFGPEEAAL QRLCRRARTG
KEPAAARFYR EEGNRQFGRC CYRDAVRLYS QAAAHEPPRS PEVALCFANR SAALFHLGHF
EVCLEDIARA ESHGYPDRLL PKVLLRKAEC LLRLGRLQDA TDTLTAVENK MAVDGIMTSP
IHRMLLKKLS QLKTEIHEGS CPEPAREADG DVQRESEIWE ENGSISGASS SLSLNFSTER
GRHLVASQDI LPGQNLLKEK AFVSVLCPGE GDSLLLQDSS ETVWDTRVTN ADLYCHHCLK
QLLASIPCCG CSYAKYCSQN CADVAWEQYH RTECPLGALL LTLGVFFHVA LRTVLLAGFS
EVSRLVEWSR DDSNKDLCNA EAGGEHPSEA LDTRAGRKVI PGCNDNGQYQ SSYQAVFNLL
PHVEKHSPEH KFLCMLSIVA ICKKLQETGL EAAVLNGESS TTGSEQKTCG KTSDELSPEL
MIMAEAMLRH VLQLQCNAQA ITVMQELESG DGAVVNKKPV RLATAFFPVL SLLNHSCSPN
ISVSFSGTAA TVRASQPIPS GQEIFHCYGE EMLCCSSEAC AFSVSRERLS QRLLDLQQQM
EKALELLRDS KADEAIKMLL KCQIDARNFL SPEHLLMGEL EDHLAQVYAT LGKWQEAARH
LGRSIQLVEM HHGPSSVEMG HELFKLAQIL FNGFAVSEAL STIQRAEEIL SVHCGPQSTQ
IQELQEMKTC LLELPRSILQ RT
