CXXC5_PONAB
ID CXXC5_PONAB Reviewed; 322 AA.
AC Q5R7N4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=CXXC-type zinc finger protein 5;
GN Name=CXXC5;
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 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}.
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DR EMBL; CR860080; CAH92226.1; -; mRNA.
DR RefSeq; NP_001126301.1; NM_001132829.1.
DR AlphaFoldDB; Q5R7N4; -.
DR SMR; Q5R7N4; -.
DR STRING; 9601.ENSPPYP00000017717; -.
DR Ensembl; ENSPPYT00000018430; ENSPPYP00000017717; ENSPPYG00000015845.
DR GeneID; 100173280; -.
DR KEGG; pon:100173280; -.
DR CTD; 51523; -.
DR eggNOG; ENOG502QT2M; Eukaryota.
DR GeneTree; ENSGT00940000154108; -.
DR HOGENOM; CLU_074593_0_0_1; -.
DR InParanoid; Q5R7N4; -.
DR OMA; ANGHDPP; -.
DR OrthoDB; 946583at2759; -.
DR TreeFam; TF326617; -.
DR Proteomes; UP000001595; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..322
FT /note="CXXC-type zinc finger protein 5"
FT /id="PRO_0000317550"
FT ZN_FING 256..297
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 257..262
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 281
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="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7LFL8"
SQ SEQUENCE 322 AA; 33007 MW; ADC87CD399819CAE CRC64;
MSSLGGGSQD AGGSSSSSTN GSGGSGSSGP KAGAADKSAV VAAATPASVA DDTPPPERRN
KSGIISEPLN KSLRRSRPLS HYSSFGSSGG SGGGSMMGGE SADKATAAAA AASLLANGHD
LAAAMAVDKS NPTSKHKSGA VASLLSKAER ATELAAEGQL TLQQFAQSTE MLKRVVQEHL
PLMSEAGAGL PDMEAVAGAE ALNGQSDFPY LGAFPINPGL FIMTPAGVFL AESALHMAGL
AEYPMQGELA SAISSGKKKR KRCGMCAPCR RRINCEQCSS CRNRKTGHQI CKFRKCEELK
KKPSAALEKV MLPTGAAFRW FQ
