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