PHF23_BOVIN
ID PHF23_BOVIN Reviewed; 400 AA.
AC A5D962; Q58CU8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; BT021849; AAX46696.1; -; mRNA.
DR EMBL; BT030481; ABQ12921.1; -; mRNA.
DR EMBL; BC142215; AAI42216.1; -; mRNA.
DR RefSeq; NP_001019741.1; NM_001024570.1.
DR AlphaFoldDB; A5D962; -.
DR STRING; 9913.ENSBTAP00000019811; -.
DR PaxDb; A5D962; -.
DR PRIDE; A5D962; -.
DR Ensembl; ENSBTAT00000019811; ENSBTAP00000019811; ENSBTAG00000014881.
DR GeneID; 539774; -.
DR KEGG; bta:539774; -.
DR CTD; 79142; -.
DR VEuPathDB; HostDB:ENSBTAG00000014881; -.
DR VGNC; VGNC:32823; PHF23.
DR eggNOG; KOG1844; Eukaryota.
DR GeneTree; ENSGT00530000063882; -.
DR InParanoid; A5D962; -.
DR OMA; SGHKKDP; -.
DR OrthoDB; 982722at2759; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000014881; Expressed in semen and 108 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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..400
FT /note="PHD finger protein 23"
FT /id="PRO_0000302829"
FT ZN_FING 336..384
FT /note="PHD-type"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..262
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..288
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..313
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 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT MOD_RES 165
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUL5"
FT CONFLICT 248..250
FT /note="Missing (in Ref. 1; AAX46696)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 43440 MW; 024B4DA5E652135C CRC64;
MLEAMAEPSP EDPPPTLKPE TQPPEKRRRT IEDFNKFCSF VLAYAGYIPP SKEESDWPAS
GSSSPLRGES AADSDGWDSA PSDLRTIQTF VKKAKSSKRR AAQAGPTQPG PPRSTFPRLQ
APDSATLLEK MKLKDSLFDI DGPKMASPLS PTSLTHASRP PAALTPVPLS QGDLSQPPRK
KDRKNRKLGP GGATGFGVLR RPRPAPGDGE KRSRIKKSKK RKLKKAERGD RLPPPGPPRA
PPSDTDSEEE EEEEEEEEEM AAMVGGEAPA PVLPTPEAPR PPATVHPEGA PPTDGESKEV
GSTETSQDGD ASSSEGEMRV MDEDIMVESG DDSWDLITCY CRKPFAGRPM IECSLCGTWI
HLSCAKIKKT NVPDFFYCQK CKELRPEARR LGGPPKSGEP
