PRDM4_PONAB
ID PRDM4_PONAB Reviewed; 801 AA.
AC Q5R5M1;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=PR domain zinc finger protein 4;
DE EC=2.1.1.-;
DE AltName: Full=PR domain-containing protein 4;
GN Name=PRDM4;
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=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May function as a transcription factor involved in cell
CC differentiation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR860836; CAH92945.1; -; mRNA.
DR RefSeq; NP_001126735.1; NM_001133263.1.
DR RefSeq; XP_009246470.1; XM_009248195.1.
DR AlphaFoldDB; Q5R5M1; -.
DR BMRB; Q5R5M1; -.
DR SMR; Q5R5M1; -.
DR STRING; 9601.ENSPPYP00000005606; -.
DR GeneID; 100173737; -.
DR KEGG; pon:100173737; -.
DR CTD; 11108; -.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; KOG2461; Eukaryota.
DR HOGENOM; CLU_019772_0_0_1; -.
DR InParanoid; Q5R5M1; -.
DR OMA; RDYAQQM; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF332513; -.
DR Proteomes; UP000001595; Chromosome 12.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0035097; C:histone methyltransferase complex; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:1990226; F:histone methyltransferase binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd19189; PR-SET_PRDM4; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR017124; PRDM4.
DR InterPro; IPR044404; PRDM4_PR/SET.
DR InterPro; IPR041493; PRDM4_Znf_knuckle.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR Pfam; PF18445; zf_PR_Knuckle; 1.
DR PIRSF; PIRSF037161; PRDM4; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Methyltransferase; Nucleus; Reference proteome;
KW Repeat; S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..801
FT /note="PR domain zinc finger protein 4"
FT /id="PRO_0000341944"
FT DOMAIN 412..529
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 545..566
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 618..640
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 646..668
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 674..696
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 702..724
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 730..752
FT /note="C2H2-type 6; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 751..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..778
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 87874 MW; DB52DEC6531A6955 CRC64;
MHHRMNEMNL SPVGMEQLTS SSVSNALPVS GSHLGLAASP THSAIPAPGL PVAIPNLGPS
LSSLPSALSL MLPMGIGDRG VMCGLPERNY TLPPPPYPHL ESSYFRTILP GILSYLADRP
PPQYIHPNSI NVDGNTALSI TNNASALDPY QSNGNVGLEP GIVSIDSRSV NTHGAQSLHP
SDGHEVALDT AITMENVSRV TSPISTDGMA EELTMDGVAG EHSQIPNGSR SHEPLSVDSV
SNNLAADAVG HGGVIPMHGN GLELPVVMET DHIASRVNGM SDSALSDSIH TVAMSTNSVS
VALSTSHNLA SLESVSLHEV GLSLEPVAVS SITQEVAMGT GHVDVSSDSL SFVPPSLQME
DSNSNKENMA TLFTIWCTLC DRAYPSDCPE HGPVTFVPDT PIESRARLSL PKQLVLRQSI
VGAEVGVWTG ETIPVRTCFG PLIGQQSHSM EVAEWTDKAV NHIWKIYHNG VLEFCIITAD
ENECNWMMFV RKARNREEQN LVAYPHDGKI FFCTSQDIPP ENELLFYYSR DYAQQIGVPE
HPDVHLCNCG KECNSYTEFK AHLTSHIHNH LPTQGHSGSH GPSHSKERKW KCSMCPQAFI
SPSKLHVHFM GHMGMKPHKC DFCSKAFSDP SNLRTHLKIH TGQKNYRCTL CDKSFTQKAH
LESHMVIHTG EKNLKCDYCD KLFMRRQDLK QHVLIHTQER QIKCPKCDKL FLRTNHLKKH
LNSHEGKRDY VCEKCTKAYL TKYHLTRHLK TCKGPTSSSS APEEEEEDDS EEEDLADSVG
TEDCRINSAV YSADESLSAH K
