ID   PF23A_XENLA             Reviewed;         272 AA.
AC   Q5HZN9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=PHD finger protein 23A {ECO:0000305};
GN   Name=phf23-a {ECO:0000305};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2005) 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; BC088943; AAH88943.1; -; mRNA.
DR   RefSeq; NP_001088965.1; NM_001095496.1.
DR   AlphaFoldDB; Q5HZN9; -.
DR   SMR; Q5HZN9; -.
DR   DNASU; 496345; -.
DR   GeneID; 496345; -.
DR   CTD; 496345; -.
DR   Xenbase; XB-GENE-6252084; phf23.L.
DR   OMA; KEERAWT; -.
DR   OrthoDB; 982722at2759; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 496345; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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..272
FT                   /note="PHD finger protein 23A"
FT                   /id="PRO_0000302835"
FT   ZN_FING         212..260
FT                   /note="PHD-type"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          50..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   272 AA;  29375 MW;  B24D1E4DF13EA5E2 CRC64;
     MLETTMGEAS PEDPPLNLKS LSQPPQKRSR TVEDFNRFCS FVLAYAGYIP PPAKEERAWT
     PPSSVSPHRT EESDGWDSPD PPQLPIPSDP RQPPASSDIS TIETFVMKAK SQGGGGGNSE
     NVEGPVGSGE QAQVKKGSRR KRRQRHRGGV TMSDTDTDEE ERGERLAGSL PAPQLPPSAE
     SSRDGGGSSS DADTQVMDED IMVESGDDSW DLVTCYCEKP FAGRPMIECN ICCTWVHLSC
     AKIRKSNVPD VYYCQKCRGG KGSGGTAPKG EP