CXXC5_RAT
ID CXXC5_RAT Reviewed; 316 AA.
AC Q5XIQ3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=CXXC-type zinc finger protein 5;
GN Name=Cxxc5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, INTERACTION WITH DVL1, SUBCELLULAR LOCATION, INDUCTION, AND
RP TISSUE SPECIFICITY.
RX PubMed=19001364; DOI=10.1074/jbc.m808119200;
RA Andersson T., Soedersten E., Duckworth J.K., Cascante A., Fritz N.,
RA Sacchetti P., Cervenka I., Bryja V., Hermanson O.;
RT "CXXC5 is a novel BMP4-regulated modulator of Wnt signaling in neural stem
RT cells.";
RL J. Biol. Chem. 284:3672-3681(2009).
CC -!- FUNCTION: May indirectly participate in activation of the NF-kappa-B
CC and MAPK pathways (By similarity). Required for DNA damage-induced ATM
CC phosphorylation, p53 activation and cell cycle arrest. Involved in
CC myelopoiesis (By similarity). Acts as a mediator of BMP4-mediated
CC modulation of canonical Wnt signaling activity in neural stem cells
CC (PubMed:19001364). Binds to the oxygen responsive element of COX4I2 and
CC represses its transcription under hypoxia conditions (4% oxygen), as
CC well as normoxia conditions (20% oxygen) (By similarity). May repress
CC COX4I2 transactivation induced by CHCHD2 and RBPJ (By similarity).
CC Binds preferentially to DNA containing cytidine-phosphate-guanosine
CC (CpG) dinucleotides over CpH (H=A, T, and C), hemimethylated-CpG and
CC hemimethylated-hydroxymethyl-CpG (By similarity).
CC {ECO:0000250|UniProtKB:Q7LFL8, ECO:0000269|PubMed:19001364}.
CC -!- SUBUNIT: Interacts with DVL1 (PubMed:19001364). Interacts with RBPJ (By
CC similarity). {ECO:0000250|UniProtKB:Q7LFL8,
CC ECO:0000269|PubMed:19001364}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19001364}. Cytoplasm
CC {ECO:0000269|PubMed:19001364}. Note=Colocalizes with DVL1 in large
CC bodies localized just outside the nuclear membrane.
CC -!- TISSUE SPECIFICITY: Expressed in neural stem cells (at protein level).
CC Expressed in the dorsal telencephalon. {ECO:0000269|PubMed:19001364}.
CC -!- INDUCTION: Up-regulated by BMP4. {ECO:0000269|PubMed:19001364}.
CC -!- DOMAIN: The CXXC zinc finger mediates binding to CpG-DNA.
CC {ECO:0000250|UniProtKB:Q7LFL8}.
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DR EMBL; BC083622; AAH83622.1; -; mRNA.
DR RefSeq; NP_001007629.1; NM_001007628.2.
DR RefSeq; XP_017456389.1; XM_017600900.1.
DR RefSeq; XP_017456390.1; XM_017600901.1.
DR RefSeq; XP_017456391.1; XM_017600902.1.
DR RefSeq; XP_017456392.1; XM_017600903.1.
DR RefSeq; XP_017456393.1; XM_017600904.1.
DR AlphaFoldDB; Q5XIQ3; -.
DR SMR; Q5XIQ3; -.
DR STRING; 10116.ENSRNOP00000042976; -.
DR PhosphoSitePlus; Q5XIQ3; -.
DR PaxDb; Q5XIQ3; -.
DR Ensembl; ENSRNOT00000045795; ENSRNOP00000042976; ENSRNOG00000032878.
DR GeneID; 291670; -.
DR KEGG; rno:291670; -.
DR UCSC; RGD:1359466; rat.
DR CTD; 51523; -.
DR RGD; 1359466; Cxxc5.
DR eggNOG; ENOG502QT2M; Eukaryota.
DR GeneTree; ENSGT00940000154108; -.
DR InParanoid; Q5XIQ3; -.
DR OMA; ANGHDPP; -.
DR OrthoDB; 946583at2759; -.
DR PhylomeDB; Q5XIQ3; -.
DR TreeFam; TF326617; -.
DR PRO; PR:Q5XIQ3; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000032878; Expressed in pancreas and 19 other tissues.
DR Genevisible; Q5XIQ3; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..316
FT /note="CXXC-type zinc finger protein 5"
FT /id="PRO_0000317551"
FT ZN_FING 250..291
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 251..256
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
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 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
SQ SEQUENCE 316 AA; 32626 MW; E8E772D04A4BE97B CRC64;
MSSLGGGSQD AGGSSSSSNT SSSSGSGQKA GGTDKSATVA ATAPASVADD APPPERRNKS
GIISEPLNKS LRRSRPLSHY SSFGSSGGAG SMMGGESADK AAAAAASLLA NGHDLAAAMA
VDKSNPTSKH KSGAVASLLS KAERATELAA EGQLTLQQFA QSTEMLKRVV QEHLPLMSEA
GAGLPDMEAV AGAEALNGQS DFPYLGAFPI NPGLFIMTPA GVFLAESALH MAGLAEYPMQ
GELASAISSG KKKRKRCGMC APCRRRINCE QCSSCRNRKT GHQICKFRKC EELKKKPSAA
LEKVMLPSGA AFRWFQ
