ID A0A3P8NNM7_ASTCA Unreviewed; 1023 AA.
AC A0A3P8NNM7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=PHD finger protein 8 {ECO:0000313|Ensembl:ENSACLP00000006390.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000006390.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000006390.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000006390.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. JHDM1D
CC subfamily. {ECO:0000256|ARBA:ARBA00006942}.
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DR AlphaFoldDB; A0A3P8NNM7; -.
DR STRING; 8154.ENSACLP00000006390; -.
DR Ensembl; ENSACLT00000006536.1; ENSACLP00000006390.1; ENSACLG00000004276.1.
DR GeneTree; ENSGT00940000157847; -.
DR OMA; DIFHQNI; -.
DR OrthoDB; 2784357at2759; -.
DR Proteomes; UP000265100; Chromosome 20.
DR Bgee; ENSACLG00000004276; Expressed in camera-type eye and 8 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0048922; P:posterior lateral line neuromast deposition; IEA:Ensembl.
DR GO; GO:0060319; P:primitive erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; IEA:Ensembl.
DR CDD; cd15642; PHD_PHF8; 1.
DR Gene3D; 1.20.58.1360; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR PANTHER; PTHR23123:SF11; HISTONE LYSINE DEMETHYLASE PHF8; 1.
DR PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 5..56
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 201..357
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 61..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..629
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..914
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1023 AA; 112109 MW; 3218E80C3FAE36B8 CRC64;
MASVPVYCLC RLPYDVTRFM IECDICQDWF HGSCVGVEED KAAEIDLYHC PNCQVTHGPS
VMRKRRGGNK QVDGGATGGR DPSKPVKTGS AQFVRELRSR TFPNADEILL KPSGAQLTVE
FLEEHSFSVP VMVLRRDGLG MTLPPSSFGV SDVEHYIGSD KQIDVIDVSR QCDLKMRLGD
FVEHYNSPNR DRVLNVISLE FSETRLSNLV ETPKIVRKLS WVENLWPEES VFERPNVQKY
CLMGVKDSYT DFHIDFGGTS VWYHVLRGEK IFYLISPTPA NLALFERWSS SSNQNEMFFG
DQVDMCYKCS VKQGNTLFIP TGWIHAVLTP VDCLAFGGNF LHSLNIDMQL RAYEIEKRLS
TADLFKFPNF ETVCWYVGKH LLDTFRGLRE NRRHPATYLV HGAKALNNAF RSWTRKEALA
DHEVEIPETI NTQALVKDLA KEIRLVEDIF QQNIGRTGPQ FPGSPLSKAP LTTSQNSGRP
PGKKKGPKPK EMTGGVGPPG TKKKSQKGLL KAEAGELDLI EIHTKHTLKK FQPGKSKHKN
KLELPLEEFE GKINKSKLKL VLTNGKIQGK KDGSSNGAGS ARNYKHLATE GSSLSDLESE
DELQIDETPP PRRKTAGLSK KKKLSGLPRK LPRAKPCSDP NRIREPGEVD FDIEEDYTTD
EEALAAHGVK GGAGGILDLL KASKQVAGLD STAIGEEAPA SPSTRDAIQG MLSMANPPSS
SSSSSSSSPL SISGGLTEGL GVVKEKGGKA VWVTGGVKKT ANSEKKPVIQ RPGKRPIKRP
ARHLSDEESP DEQETLGTCF KDSDYVYPSL ESDEEDHTNK TKMKRKKNWD DTPWSPKARV
MPTLPKQDRP AREGARVASV ETGLAAAAAK LAQQEQQKPA KRKYTKKQRP PAPVITPPPV
QTEPAPPSPT PAPESAADVS PDRRVDYYSA SLLDHEYTAG PGPFGSGGPR GSGAMAPGVF
LTSRRPSLSP QNSSSHSGAS PAGLSSQGTT GVGQGKRPKK GLATAKQRLG KILKIHRNGK
LLL
//
