ID   A0A2Y9IHE0_ENHLU        Unreviewed;       923 AA.
AC   A0A2Y9IHE0;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Histone lysine demethylase PHF8 isoform X2 {ECO:0000313|RefSeq:XP_022348048.1};
GN   Name=LOC111139928 {ECO:0000313|RefSeq:XP_022348048.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022348048.1};
RN   [1] {ECO:0000313|RefSeq:XP_022348048.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022348048.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_022348048.1; XM_022492340.1.
DR   AlphaFoldDB; A0A2Y9IHE0; -.
DR   Proteomes; UP000248482; 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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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   4: Predicted;
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:UP000248482};
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          195..351
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   REGION          631..703
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          715..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          780..905
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..673
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        721..741
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..895
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   923 AA;  102847 MW;  E0EF75CAA2510B20 CRC64;
     MASVPVYCLC RLPYDVTRFM IECDMCQDWF HGSCVGVEEE KAADIDLYHC PNCEVLHGPS
     IMKKRRVSSK GHDTHKGKPV KTGSPTFIRE LRSRTFDSSD EVILKPTGSQ LTVEFLEENS
     FSVPILVLKK DGLGMTLPSP SFTVRDVEHY VGSDKEIDVI DVTRQADCKM KLGDFVKYYY
     SGKREKVLNV ISLEFSDTRL SNLVETPKIV RKLSWVENLW PEECIFERPN VQKYCLMSVR
     DSYTDFHIDF GGTSVWYHVL KGEKIFYLIR PTNANLTLFE CWSSSSNQNE MFFGDQVDKC
     YKCSVKQGQT LFIPTGWIHA VLTPVDCLAF GGNFLHSLNI EMQLKAYEIE KRLSTADLFK
     FPNFETICWY VGKHILDIFR GLRENRRHPA SYLVHGGKAL NLAFRAWTRK EALPDHEDEI
     PETVRTVQLI KDLAREIRLV EFNITGTCLN DSDDDSPDLD LDGNEGPLAL LMSNGSTKRV
     KTLSKSRRAK LTKKADKARL VAEQVMEDEF DLDSDDELQI DERLGKEKAT LIIRPKFPRK
     LPRAKPCSDP NRVREPGEVE FDIEEDYTTD EDMVEGVEGK LGNGSGAGGI LDLLKASRQV
     GGPDYAALTE APASPSTQEA IQGMLCMANL QSSSSSPATS SLQAWWTGGQ DRSSGSSSSG
     LGTVSSSPAS QRTPGKRPIK RPAYWRTESE EEEENASLDE QDSLGACFKD AEYIYPSLES
     DDDDPALKSR PKKKKNSDDA PWSPKARVTP TLPKQDRPVR EGTRVASIET GLAAAAAKLA
     QQELQKAQKK KYIKKKPLLK EVEQPRPQES ILSVAAPAPA LATTPQLLTS SSPPPPPEPK
     QEALSGSLAD HEYTARPNAF GMAQANRSTT PMAPGVFLTQ RRPSVGSQSN QAGQGKRPKK
     GLATAKQRLG RILKIHRNGK LLL
//