ZN540_PONAB
ID ZN540_PONAB Reviewed; 660 AA.
AC Q5R5S6; Q5REC1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Zinc finger protein 540;
GN Name=ZNF540;
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: May act as a transcriptional repressor. {ECO:0000250}.
CC -!- SUBUNIT: May interact with MVP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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; CR857611; CAH89886.1; -; mRNA.
DR EMBL; CR860780; CAH92890.1; -; mRNA.
DR RefSeq; NP_001127601.1; NM_001134129.1.
DR AlphaFoldDB; Q5R5S6; -.
DR SMR; Q5R5S6; -.
DR STRING; 9601.ENSPPYP00000011104; -.
DR PRIDE; Q5R5S6; -.
DR Ensembl; ENSPPYT00000047615; ENSPPYP00000041824; ENSPPYG00000038995.
DR GeneID; 100174680; -.
DR KEGG; pon:100174680; -.
DR CTD; 163255; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164340; -.
DR InParanoid; Q5R5S6; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000001595; Chromosome 19.
DR GO; GO:0005829; C:cytosol; 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:0000900; F:mRNA regulatory element binding translation repressor activity; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 15.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 17.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 17.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 17.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..660
FT /note="Zinc finger protein 540"
FT /id="PRO_0000047642"
FT DOMAIN 6..77
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 187..209
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 215..237
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 243..265
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 271..293
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 299..321
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 327..349
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 355..377
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 383..405
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 411..433
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 439..461
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 467..489
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 495..517
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 523..545
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 551..573
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 579..601
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 607..629
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 635..657
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2G7"
FT CONFLICT 7
FT /note="T -> S (in Ref. 1; CAH89886)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 77069 MW; 7300E99500DD9CE4 CRC64;
MAHALVTFRD VTIDFSQKEW ECLDTTQRKL YRDVMLENYN NLVSLGYSGS KPDVITLLEQ
GKEPCVAARD VTGRQYPGLL SRHKTKKLSS EKDIHDISLS KGSKIEKSKT LHLKGSIFRN
EWQSKSEFEG QQGLKERSIS QKKIIFKKMS TDRKHPSFTL NQRIHNSEKS CDSNLVQHGK
IDSDVKHDCK ECGSTFNNVY QLTLHQKIHT GEKSCKCEKC GKVFSHSYQL TLHQRFHTGE
KPYECQECGK TFILYPQLNR HQKIHTGKKP YMCKKCDKSF FSRLELTQHK RIHTGKKSYE
CKECGKVFQL VFYFKEHERI HTGKKPYECK ECGKAFSVCG QLTRHQKIHT GVKPYECKEC
GKTFRLSFYL TEHRRTHAGK KPYECKECGK SFNVRGQLNR HKAIHTGIKP FACKVCEKAF
SYSGDLRVHS RIHTGEKPYE CKECGKAFML RSVLTEHQRL HTGVKPYECK ECGKTFRVRS
QISLHKKIHT DVKPYKCVRC GKTFRFGFYL TEHQRIHTGE KPYKCKECGK AFIRRGNLKE
HLKIHSGLKP YDCKECGKSF SRRGQFTEHQ KIHTGVKPYK CKECGKAFSR SVDLRIHQRI
HTGEKPYECK QCGKAFRLNS HLTEHQRIHT GEKPYECKVC RKAFRQYSHL YQHQKTHNVI
