ZNF24_PONAB
ID ZNF24_PONAB Reviewed; 368 AA.
AC Q5RAE6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Zinc finger protein 24;
GN Name=ZNF24;
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: Transcription factor required for myelination of
CC differentiated oligodendrocytes. Required for the conversion of
CC oligodendrocytes from the premyelinating to the myelinating state. In
CC the developing central nervous system (CNS), involved in the
CC maintenance in the progenitor stage by promoting the cell cycle.
CC Specifically binds to the 5'-TCAT-3' DNA sequence. Has transcription
CC repressor activity in vitro (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; CR859071; CAH91264.1; -; mRNA.
DR RefSeq; NP_001125749.1; NM_001132277.1.
DR AlphaFoldDB; Q5RAE6; -.
DR SMR; Q5RAE6; -.
DR STRING; 9601.ENSPPYP00000010225; -.
DR Ensembl; ENSPPYT00000010630; ENSPPYP00000010225; ENSPPYG00000009106.
DR GeneID; 100172674; -.
DR KEGG; pon:100172674; -.
DR CTD; 7572; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161396; -.
DR HOGENOM; CLU_002678_49_3_1; -.
DR InParanoid; Q5RAE6; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000001595; Chromosome 18.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..368
FT /note="Zinc finger protein 24"
FT /id="PRO_0000366921"
FT DOMAIN 52..134
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 251..273
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 279..301
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 307..329
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 335..357
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 251..301
FT /note="Necessary and sufficient for nuclear localization"
FT /evidence="ECO:0000250"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT MOD_RES 335
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 236
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 361
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17028"
FT CROSSLNK 367
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17028"
SQ SEQUENCE 368 AA; 42141 MW; 341DA62506F67AF0 CRC64;
MSAQSVEEDS ILIIPTPDEE EKILRVKLEE DPDGEEGSSI PWNHLPDPEI FRQRFRQFGY
QDSPGPREAV SQLRELCRLW LRPETHTKEQ ILELVVLEQF VAILPKELQT WVRDHHPENG
EEAVTVLEDL ESELDDPGQP VSLRRRKREV LVEDMVSQEE AQGLPSSELD AVENQLKWAS
WELHSLRHCD DDGRTENGAL APKQELPSAV ESHEVPGTLN MGVPQIFKYG ETCFPKGRFE
RKRNPSRKKQ HICDECGKHF SQGSALILHQ RIHSGEKPYG CVECGKAFSR SSILVQHQRV
HTGEKPYKCL ECGKAFSQNS GLINHQRIHT GEKPYECVQC GKSYSQSSNL FRHQRRHNAE
KLLNVVKV
