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PHF23_RAT
ID   PHF23_RAT               Reviewed;         334 AA.
AC   Q6AY75;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=PHD finger protein 23 {ECO:0000250|UniProtKB:Q9BUL5};
DE   AltName: Full=PDH-containing protein JUNE-1 {ECO:0000250|UniProtKB:Q8BSN5};
GN   Name=Phf23 {ECO:0000250|UniProtKB:Q9BUL5};
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=Kidney;
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).
CC   -!- FUNCTION: Acts as a negative regulator of autophagy, through promoting
CC       ubiquitination and degradation of LRSAM1, an E3 ubiquitin ligase that
CC       promotes autophagy in response to starvation or infecting bacteria.
CC       {ECO:0000250|UniProtKB:Q9BUL5}.
CC   -!- SUBUNIT: Interacts with LRSAM1. {ECO:0000250|UniProtKB:Q9BUL5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BUL5}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9BUL5}. Note=Mainly present in the nucleus and
CC       part in the cytoplasm. {ECO:0000250|UniProtKB:Q9BUL5}.
CC   -!- DOMAIN: The PHD-type zinc-finger domain is required for interaction
CC       with LRSAM1 and negative regulation of autophagy.
CC       {ECO:0000250|UniProtKB:Q9BUL5}.
CC   -!- SIMILARITY: Belongs to the PHF23 family. {ECO:0000305}.
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DR   EMBL; BC079162; AAH79162.1; -; mRNA.
DR   RefSeq; NP_001004272.1; NM_001004272.1.
DR   AlphaFoldDB; Q6AY75; -.
DR   SMR; Q6AY75; -.
DR   STRING; 10116.ENSRNOP00000024079; -.
DR   PaxDb; Q6AY75; -.
DR   PRIDE; Q6AY75; -.
DR   GeneID; 360550; -.
DR   KEGG; rno:360550; -.
DR   UCSC; RGD:1302969; rat.
DR   CTD; 79142; -.
DR   RGD; 1302969; Phf23.
DR   VEuPathDB; HostDB:ENSRNOG00000017657; -.
DR   eggNOG; KOG1844; Eukaryota.
DR   HOGENOM; CLU_047981_1_1_1; -.
DR   InParanoid; Q6AY75; -.
DR   OMA; SGHKKDP; -.
DR   OrthoDB; 982722at2759; -.
DR   PRO; PR:Q6AY75; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000017657; Expressed in thymus and 20 other tissues.
DR   Genevisible; Q6AY75; RN.
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; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Autophagy; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..334
FT                   /note="PHD finger protein 23"
FT                   /id="PRO_0000302832"
FT   ZN_FING         270..318
FT                   /note="PHD-type"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..194
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..222
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT   MOD_RES         57
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT   MOD_RES         96
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT   MOD_RES         246
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT   MOD_RES         247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT   MOD_RES         248
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT   MOD_RES         331
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUL5"
SQ   SEQUENCE   334 AA;  36232 MW;  A7200FCDE1B2571D CRC64;
     MLEAMAEPSP EDPPPTLKPE TQPPEKRRRT IEDFNKFCSF VLAYAGYIPP SKGAPDSATL
     LEKMKLKDSL FDLDGPKVAS PLSPTSLTSR PPAALTPVPL SQGDLSQPRK KDRKNRKLGP
     GGGAGFGVLR RPRPAPGDGE KRSRIKKSKK RKLKKADRGD RLPPPGPPRA PPSDTDSEEE
     EEEEEEEDDE EETTVVGGGG VPAPVLPTPP EAPRPPVTVH PEGAPPTDSE GKDAGSTETS
     QDGDGSSSEG EMRVMDEDIM VESGDDSWDL ITCYCRKPFA GRPMIECSLC GTWIHLSCAK
     IKKTNVPDFF YCQKCKELRP EARRLGGLPK SGEP
 
 
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