CXXC5_BOVIN
ID CXXC5_BOVIN Reviewed; 317 AA.
AC Q32LB3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=CXXC-type zinc finger protein 5;
GN Name=CXXC5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May indirectly participate in activation of the NF-kappa-B
CC and MAPK pathways. Acts as a mediator of BMP4-mediated modulation of
CC canonical Wnt signaling activity in neural stem cells. Required for DNA
CC damage-induced ATM phosphorylation, p53 activation and cell cycle
CC arrest. Involved in myelopoiesis (By similarity). Binds to the oxygen
CC responsive element of COX4I2 and represses its transcription under
CC hypoxia conditions (4% oxygen), as well as normoxia conditions (20%
CC oxygen). May repress COX4I2 transactivation induced by CHCHD2 and RBPJ
CC (By similarity). Binds preferentially to DNA containing cytidine-
CC phosphate-guanosine (CpG) dinucleotides over CpH (H=A, T, and C),
CC hemimethylated-CpG and hemimethylated-hydroxymethyl-CpG (By
CC similarity). {ECO:0000250|UniProtKB:Q5XIQ3,
CC ECO:0000250|UniProtKB:Q7LFL8}.
CC -!- SUBUNIT: Interacts with DVL1 (By similarity). Interacts with RBPJ (By
CC similarity). {ECO:0000250|UniProtKB:Q5XIQ3,
CC ECO:0000250|UniProtKB:Q7LFL8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5XIQ3}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q5XIQ3}. Note=Colocalizes with DVL1 in large
CC bodies localized just outside the nuclear membrane.
CC {ECO:0000250|UniProtKB:Q5XIQ3}.
CC -!- DOMAIN: The CXXC zinc finger mediates binding to CpG-DNA.
CC {ECO:0000250|UniProtKB:Q7LFL8}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI09663.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC109662; AAI09663.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001033265.2; NM_001038176.2.
DR RefSeq; XP_005209522.1; XM_005209465.1.
DR RefSeq; XP_005209523.1; XM_005209466.3.
DR RefSeq; XP_005209524.1; XM_005209467.3.
DR RefSeq; XP_005209525.1; XM_005209468.2.
DR AlphaFoldDB; Q32LB3; -.
DR SMR; Q32LB3; -.
DR STRING; 9913.ENSBTAP00000005204; -.
DR PaxDb; Q32LB3; -.
DR PRIDE; Q32LB3; -.
DR Ensembl; ENSBTAT00000005204; ENSBTAP00000005204; ENSBTAG00000003986.
DR GeneID; 538485; -.
DR KEGG; bta:538485; -.
DR CTD; 51523; -.
DR VEuPathDB; HostDB:ENSBTAG00000003986; -.
DR VGNC; VGNC:27860; CXXC5.
DR eggNOG; ENOG502QT2M; Eukaryota.
DR GeneTree; ENSGT00940000154108; -.
DR HOGENOM; CLU_074593_0_0_1; -.
DR InParanoid; Q32LB3; -.
DR OMA; ANGHDPP; -.
DR OrthoDB; 946583at2759; -.
DR TreeFam; TF326617; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000003986; Expressed in cerebellum and 106 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0008327; F:methyl-CpG binding; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR InterPro; IPR040388; CXXC4/CXXC5.
DR InterPro; IPR002857; Znf_CXXC.
DR PANTHER; PTHR13419; PTHR13419; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..317
FT /note="CXXC-type zinc finger protein 5"
FT /id="PRO_0000317547"
FT ZN_FING 251..292
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 252..257
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
SQ SEQUENCE 317 AA; 32650 MW; CA7C75580439E76F CRC64;
MSSLSSGPQD TGGSSSSSSN GSSGSGPKAG VADKSAAVAA AAPASVADDA PPPERRNKSG
IISEPLNKSL RRSRPLSHYS SFGGSGGSGG GSMMGGESAE KAAAAAASLL ANGHDLAAAM
AVDKSNSTSK HKSSAVASLL SKAERATELG AEGQLTLQQF AQSTEMLKRV VQEHLPLMSE
AGAGLPDMEA VAGAEALNGQ SDFPYLGAFP INPGLFIMTP AGVFLAESAL HMAGLAEYPM
QGELASAISS GKKKRKRCGM CAPCRRRINC EQCSSCRNRK TGHQICKFRK CEELKKKPSA
ALEKVMLPTG AAFRWFQ
