ID A0A3Q2EIT8_CYPVA Unreviewed; 1023 AA.
AC A0A3Q2EIT8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=PHD finger protein 8 {ECO:0000313|Ensembl:ENSCVAP00000032528.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000032528.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000032528.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. JHDM1D
CC subfamily. {ECO:0000256|ARBA:ARBA00006942}.
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DR RefSeq; XP_015233451.1; XM_015377965.1.
DR AlphaFoldDB; A0A3Q2EIT8; -.
DR STRING; 28743.ENSCVAP00000032528; -.
DR Ensembl; ENSCVAT00000028410.1; ENSCVAP00000032528.1; ENSCVAG00000022608.1.
DR GeneID; 107086788; -.
DR KEGG; cvg:107086788; -.
DR CTD; 23133; -.
DR GeneTree; ENSGT00940000157847; -.
DR OMA; DIFHQNI; -.
DR OrthoDB; 2784357at2759; -.
DR Proteomes; UP000265020; Unplaced.
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 Reference proteome {ECO:0000313|Proteomes:UP000265020};
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 60..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..498
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..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
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..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1023 AA; 112416 MW; 3702537954A1B9BA CRC64;
MASVPVYCLC RLPYDVTRFM IECDICQDWF HGSCVGVEED KAAEIDQYHC PNCQVTHGPS
VMRKRRGGNK QTDGNTGTGR DPSKPVKTGS PQFVRELRSR TFPNADEILL KPSGAQLTVD
FLEEHSFSVP VMVLRRDGLG MTLPPSSFSV TDVEHYIGPD KEIDVIDVAR QCDLKMRLGD
FVEYYNSPNR DKVLNVISLE FSETRLSNLV ETPKIVRKLS WVENLWPEES VFERPNVQKY
CLMGVKDSYT DFHIDFGGTS VWYHVLRGEK IFYLISPTPA NLALFERWSS SSNQNEMFFG
DQVDMCYKCS VKQGNTLFIP TGWIHAVLTP VDCLAFGGNF LHSLNIDMQL RAYEIEKRLS
TAELFKFPNF ETVCWYVGKH LLDIFRGLRE NRRHPASYLV HGAKALNNAF RTWTRKEALA
EHEMEIPETI NTQTLIKDLA KEIRLVEDIF QQNIGRTGPP FPGAPLSKAP LSIAQNSGRP
PGKKKGPKPK EVLGVFGPPG TKKKIQKGLI KAEVGELELI EIHAKHTLKK FQPGKSKHKT
KLELPLDEFE GKINKNKLKL VLTNGKIQGK KDGSSNGAGS AGSYKHLATE GSSVSDLESE
DELQIDETPP PRRKSTGPNK KRKLSGLPRK LPRAKPCSDP NRIREPGEVD FDIEEDYTTD
EEALAAHGVK GGAGGILDLL KASKQVAGLD SAALSEEAPA SPSTRDAIQG MLSMANPPSS
CSSSSSSSPL SISGGLTEGL AAVKEKGGRT VWVTGGIKKS ANLEKKAVIQ RPGKRTIKRP
ARHISDEDSP DEQETLGTCF KDSDYVYPSL ESDEEDHISK TKMKRKKNWD DTPWSPKARV
MPTLPKQDRP AREGARVASV ETGLAAAAAK LAQQEQQKPA KRKYTKKQRP PAPVVSPPPV
QAETSPPSPT PAPESAADDS PDRRMDYFSA SLLDHEYTAG PGPFGPGGPR GSGAMAPGVF
LSSRRPSMSP QNSSSHAGLS PAGLASQGIT GIGQGKRPKK GLATAKQRLG KILKIHRNGK
LLL
//
