CXXC1_BOVIN
ID CXXC1_BOVIN Reviewed; 658 AA.
AC Q5EA28;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=CXXC-type zinc finger protein 1;
DE AltName: Full=CpG-binding protein;
DE AltName: Full=PHD finger and CXXC domain-containing protein 1;
GN Name=CXXC1;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional activator that exhibits a unique DNA binding
CC specificity for CpG unmethylated motifs with a preference for CpGG.
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the SET1 complex, at least composed of the
CC catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2,
CC CXXC1/CFP1, HCFC1 and DPY30. Interacts with SETD1A (By similarity).
CC Interacts with ZNF335 (By similarity). Interacts with PRDM9; this
CC interaction does not link PRDM9-activated recombination hotspot sites
CC with DSB machinery and is not required for the hotspot recognition
CC pathway. Interacts with histone H3K4me3 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9CWW7}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q9P0U4}.
CC Nucleus {ECO:0000250|UniProtKB:Q9CWW7}. Note=Associated with
CC euchromatin. During mitosis, excluded from condensed chromosomes (By
CC similarity). {ECO:0000250|UniProtKB:Q9P0U4}.
CC -!- DOMAIN: The acidic domain carries the potential to activate
CC transcription. {ECO:0000250}.
CC -!- PTM: May be regulated by proteolysis. {ECO:0000250}.
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DR EMBL; BT020741; AAX08758.1; -; mRNA.
DR EMBL; BC102763; AAI02764.1; -; mRNA.
DR RefSeq; NP_001019688.1; NM_001024517.1.
DR AlphaFoldDB; Q5EA28; -.
DR SMR; Q5EA28; -.
DR STRING; 9913.ENSBTAP00000029172; -.
DR PaxDb; Q5EA28; -.
DR PRIDE; Q5EA28; -.
DR Ensembl; ENSBTAT00000029172; ENSBTAP00000029172; ENSBTAG00000021884.
DR GeneID; 511446; -.
DR KEGG; bta:511446; -.
DR CTD; 30827; -.
DR VEuPathDB; HostDB:ENSBTAG00000021884; -.
DR VGNC; VGNC:27859; CXXC1.
DR eggNOG; KOG1632; Eukaryota.
DR GeneTree; ENSGT00730000111044; -.
DR HOGENOM; CLU_025011_2_0_1; -.
DR InParanoid; Q5EA28; -.
DR OMA; VLPQRIQ; -.
DR OrthoDB; 463371at2759; -.
DR TreeFam; TF320326; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000021884; Expressed in retina and 106 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048188; C:Set1C/COMPASS complex; ISS:UniProtKB.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IEA:Ensembl.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0045322; F:unmethylated CpG binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051568; P:histone H3-K4 methylation; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR022056; CpG-bd_C.
DR InterPro; IPR037869; Spp1/CFP1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR002857; Znf_CXXC.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46174; PTHR46174; 1.
DR Pfam; PF12269; CpG_bind_C; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Coiled coil; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..658
FT /note="CXXC-type zinc finger protein 1"
FT /id="PRO_0000283720"
FT ZN_FING 28..76
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 162..211
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 428..470
FT /evidence="ECO:0000255"
FT COMPBIAS 84..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..247
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0U4"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0U4"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0U4"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0U4"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0U4"
FT CROSSLNK 252
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P0U4"
SQ SEQUENCE 658 AA; 75870 MW; 14F8C14E2969645B CRC64;
MEGDASDPEP PDAGEDSKSE NGENAPIYCI CRKPDINCFM IGCDNCNEWF HGDCIRITEK
MAKAIREWYC RECREKDPKL EIRYRHKKSR ERDSSERDGS EPRDEGGGRK RPAPDPDLQR
RAGAGTGVGA MLARGSASPH KSSPQPLVAT PSQHHQQQQQ QQQIKRSARM CGECEACRRT
EDCGHCDFCR DMKKFGGPNK IRQKCRLRQC QLRARESYKY FPSSLSPVTP SESLPRPRRP
LPTQPQPQPS QKLGRLREDE GAVASAAVKE PPEATATPEP LSDEDLPLDS ELYQDFCAGA
FDDHSLPWMS DTEESQFLDP ALRKRAVKVK HVKRREKKSE KKKDERYKRH RQKQKHKDKW
KHPERADAKD PASLPQCLGP GCVRAAQPGS KYCSDDCGMK LAANRIYEIL PQRIQQWQQS
PCIAEEHGKK LLERIRREQQ SARTRLQEME RRFHELEAII LRAKQQAVRE DEESNEGDSD
DTDLQIFCVS CGHPINPRVA LRHMERCYAK YESQTSFGSM YPTRIEGATR LFCDVYNPQS
KTYCKRLQVL CPEHSRDPKV PADEVCGCPL VRDVFELTGD FCRLPKRQCN RHYCWEKLRR
AEVDLERVRV WYKLDELFEQ ERNVRTAMTN RAGLLALMLH QTIQHDPLTT DLRSNAER
