PHF23_XENTR
ID PHF23_XENTR Reviewed; 278 AA.
AC Q5U5E5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=PHD finger protein 23A {ECO:0000305};
GN Name=phf23 {ECO:0000305}; ORFNames=TEgg129n08.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a negative regulator of autophagy.
CC {ECO:0000250|UniProtKB:Q9BUL5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BUL5}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9BUL5}.
CC -!- DOMAIN: The PHD-type zinc-finger domain is required for negative
CC regulation of autophagy. {ECO:0000250|UniProtKB:Q9BUL5}.
CC -!- SIMILARITY: Belongs to the PHF23 family. {ECO:0000305}.
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DR EMBL; CR942437; CAJ83696.1; -; mRNA.
DR EMBL; BC084739; AAH84739.1; -; mRNA.
DR RefSeq; NP_001011148.1; NM_001011148.1.
DR AlphaFoldDB; Q5U5E5; -.
DR SMR; Q5U5E5; -.
DR DNASU; 496566; -.
DR GeneID; 496566; -.
DR KEGG; xtr:496566; -.
DR CTD; 79142; -.
DR Xenbase; XB-GENE-6455436; phf23.
DR InParanoid; Q5U5E5; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; ISS:GO_Central.
DR GO; GO:1901097; P:negative regulation of autophagosome maturation; ISS:GO_Central.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Cytoplasm; Metal-binding; Nucleus; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..278
FT /note="PHD finger protein 23A"
FT /id="PRO_0000302837"
FT ZN_FING 216..264
FT /note="PHD-type"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..95
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 278 AA; 30183 MW; 6EB1687A7A93C011 CRC64;
MLETTMGEAS PEDPPLNLKS LSQPPQKRSR TVEDFNRFCS FVLAYAGYIP TPAKEERAWT
PPSSVSPHRT EESDGWDSPD PPQLPAPPEP PQPPATSDIS TIETFVMKAK SQGAGGGSSK
MPGGQEDGAE EEEVQAKKGS RRKRRQRHRG GVRMSDTDTD EEEREERPAA PGSLPAPQLP
PSAESSRDGG GSSSDADTQV MDEDIMVESG DDSWDLVTCY CEKPFAGRPM IECNVCCTWV
HLSCAKIRKS NVPDVYYCQK CRAGRLPGAT TPKADSAP