SMYD4_PONAB
ID SMYD4_PONAB Reviewed; 804 AA.
AC Q5R5X9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=SET and MYND domain-containing protein 4;
DE EC=2.1.1.-;
GN Name=SMYD4;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a critical role in cardiac development (By similarity).
CC Acts as a key epigenetic regulator of gene expression during cardiac
CC development via its dual activities as a methyltransferase and negative
CC regulator of HDAC1 (By similarity). {ECO:0000250|UniProtKB:Q08C84,
CC ECO:0000250|UniProtKB:Q8IYR2}.
CC -!- SUBUNIT: Interacts (via MYND-type zinc finger) with HDAC1.
CC {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; CR860722; CAH92837.1; -; mRNA.
DR RefSeq; NP_001127594.1; NM_001134122.1.
DR AlphaFoldDB; Q5R5X9; -.
DR SMR; Q5R5X9; -.
DR STRING; 9601.ENSPPYP00000008770; -.
DR GeneID; 100174673; -.
DR KEGG; pon:100174673; -.
DR CTD; 114826; -.
DR eggNOG; KOG2084; Eukaryota.
DR InParanoid; Q5R5X9; -.
DR OrthoDB; 1278034at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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 Gene3D; 2.170.270.10; -; 1.
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; 1.
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..804
FT /note="SET and MYND domain-containing protein 4"
FT /id="PRO_0000227786"
FT DOMAIN 233..574
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 296..335
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 112..114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 427
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 539..540
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H7B4"
FT BINDING 573
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 595
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
SQ SEQUENCE 804 AA; 89276 MW; DDC4C455AF3D9F51 CRC64;
MDLPVDEWKS YLLQKWASLP TSVQVTISTA ETLRDIFLHS SSLLQPEDEL FLKRLSKGYL
VGKDLDAPLF YREEGNKKFQ EKDYTGAAVL YSKGVSHSRP NTEDMSLCYA NRSAALFHLG
EYETCLKDIN RAQTHGYPER LQPKIMLRKA ECLVALGRLQ EASQTISDLE RNFTATPTLA
NVRPQTLQRN LHHLKMKVQE KDKLTETFPA ALAKTLEDAA LREENEQLSS ASSSVGLCID
PLKGRYLVAT KDILPGELLV KEDAFVSVLN PGELPPPHHG LDSKWDTRVT NGDLYCHRCL
KHTLATVPCD GCSYAKYCSQ ECLQQAWELY HRTECPLGGL LLTLGVFCHI ALRLTLLVGF
EDVRKIITKV CDKISNKDIC LPESNNQVKT LNYGLGESEK SGNIIETPIP GCDINGKYEN
NYNAVFNLLP HTENHSPEHK FLCALCVSAL CRQLEAASFQ AIPTERSVNS SQLQAAVTPE
LCPDVTIWGV AMLRHMLQLQ CNAQAMTTIQ HTGSKGSIVT DSRQVRLATG IFPVVSLLNH
SCSPNTSMSF ISTVATIQAS QRIRKGQEIL HCYGPHKSRM GVAERQQELR SQYFFDCACP
ACQTEAHRMA AEPRWEAFCC NSCGAPMQGD DVLHCGSRSC AESAVSRDHL VSRLQDLQQQ
VGVAQKLLRD GELERAVQQL LGCQRDAESF LWAEHALVGE IADGLARACA ALGDWQKAAT
HLQRSLRVVE VRHGPSSVEM GHELFKLAQI FFNGFAVPEA LSTIQKAEEA LLLHCGPWDD
EIQELQKMKS CLLDLPPTPV GPAV
