ID A0A2K5XAM4_MANLE Unreviewed; 752 AA.
AC A0A2K5XAM4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Zinc finger protein 425 {ECO:0000313|Ensembl:ENSMLEP00000000349.1};
GN Name=ZNF425 {ECO:0000313|Ensembl:ENSMLEP00000000349.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000000349.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000000349.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000256|ARBA:ARBA00006991}.
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DR AlphaFoldDB; A0A2K5XAM4; -.
DR STRING; 9568.ENSMLEP00000000349; -.
DR Ensembl; ENSMLET00000000960.1; ENSMLEP00000000349.1; ENSMLEG00000000829.1.
DR GeneTree; ENSGT00940000163692; -.
DR OMA; THMAVHA; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR CDD; cd07765; KRAB_A-box; 1.
DR Gene3D; 6.10.140.140; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 18.
DR InterPro; IPR003655; aKRAB.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR47772:SF5; ZGC:162958 PROTEIN-RELATED; 1.
DR PANTHER; PTHR47772; ZINC FINGER PROTEIN 200; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 14.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 19.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 11.
DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS50806; KRAB_RELATED; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 19.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 19.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 6..70
FT /note="KRAB-related"
FT /evidence="ECO:0000259|PROSITE:PS50806"
FT DOMAIN 9..80
FT /note="KRAB"
FT /evidence="ECO:0000259|PROSITE:PS50805"
FT DOMAIN 190..217
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 246..273
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 274..301
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 302..329
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 330..357
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 358..385
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 386..413
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 414..441
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 442..469
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 470..497
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 498..525
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 526..553
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 554..581
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 582..609
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 610..637
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 638..665
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 666..693
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 694..721
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 722..749
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 78..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 87650 MW; 79679A279765B188 CRC64;
NNSPASVTVT FDDVALYFSE QEWEILEKWQ KQMYKQEMKT NYQTLDSLGY AFSKPDLITW
MEQGRMLFIS EQGCLDKTRR TTSPPTDEQL DMKDTGKLPC FDHEGTLRTK EEDCRLNGPQ
KQDLGAALPG KERKILSARR DTFQSPSLQE TEIPNKKVSI TASDPDKKDL RHKPRETPGR
LEIPTGPRCY SCYVCRKVFQ VRRDLLKHKR SHSKSQLRRY PKYRNTSRGK SELRRTQRLL
CQKKRFQCSE CEKSYFLKGS LVTHQVVHTG QRPYPCPECD KTFRYRANLK KHLCLHRGER
PFCCGECGRA FVQQCELTEH LRLHSGEKPF QCPQCDRCFR LKRGMKVHLS QHSGKRPFHC
PECGRSFSRK AALKTHQRTH SEEKPFSCAE CGRKFIYKIK LDEHIRVHTG EKPFSCPECN
KSFRLKRSLK AHGLQHSGKR PFQCPECSRG FFWRNAMRAH QRLHSEQKPF PCAECGKRFT
RPSKLACHTR VHDRQKEFPC GECKKTFSQQ SRLTQHLKVH TTEKPFSCAE CGRSFRRRAH
LTEHTRLHSG EEPFQCPECD KSFSWKASMK FHQRMHRDEK PFACSECGKT YTHQSQLTEH
LRLHSGEKPY QCPECQKTFR LKGNLKSHLL QHSGQKPFSC VMCGKSFTQQ YRLTEHIRVH
SGEKPFQCPE CDKSYCIRGS LKVHLYTHSG ERPFQCPECG KGFLQKRSLK AHLCLHSGER
PFSCDECGRS FTYVGALKTH IAVHAKEKPS SL
//
