ID W5MEH2_LEPOC Unreviewed; 695 AA.
AC W5MEH2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=PHD finger protein 21A {ECO:0000313|Ensembl:ENSLOCP00000006781.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000006781.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000006781.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01036566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01036567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01036568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015194093.1; XM_015338607.1.
DR AlphaFoldDB; W5MEH2; -.
DR STRING; 7918.ENSLOCP00000006781; -.
DR Ensembl; ENSLOCT00000006789.1; ENSLOCP00000006781.1; ENSLOCG00000005618.1.
DR GeneID; 102694453; -.
DR KEGG; loc:102694453; -.
DR CTD; 51317; -.
DR eggNOG; KOG0383; Eukaryota.
DR GeneTree; ENSGT00940000156124; -.
DR HOGENOM; CLU_020260_1_0_1; -.
DR InParanoid; W5MEH2; -.
DR OMA; SHQTGGD; -.
DR OrthoDB; 4547516at2759; -.
DR Proteomes; UP000018468; Linkage group LG27.
DR Bgee; ENSLOCG00000005618; Expressed in camera-type eye and 13 other cell types or tissues.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd15523; PHD_PHF21A; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR24102; PHD FINGER PROTEIN; 1.
DR PANTHER; PTHR24102:SF6; PHD FINGER PROTEIN 21A; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 499..546
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 66..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 30..57
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 573..604
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 75..91
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..367
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 75007 MW; 62C5DEB34D9BBE56 CRC64;
MELQTLQEAL KVEIQVHQKL VAQMKQDPQN ADLKKQLHEL QAKITALSEK QKKVVEQLRK
DLLVSKEQPE VKLQAQPALP PPPPGDGKHA PPAPAPTEAK ALVQPAPAQL PLSLLAQNAP
AQQKTVTVTP VIATKTLPLV LKAAAQTMPA SVVTQRPTVA MVTAISNTQK TSANTDMQNA
PINLQTSSKL ASPGTEAVRI VSKNAVTLVQ ATTTAHTIKV PQFIPPPRLT PRPNFLPQVR
PKPITPNNVP IAPAPPPMLA APQLIQRPVM LTKVTATSLP TATGSIHQVR IMNGQPCATI
AKTISPAQLT SIVITAPGTR IAGSQTLQIS SANTDAKTVK VQGGTEDKSP VTVSPSPPPP
APAPPKPKRE DNPQKLAFMV SLGLVTHDHL EEIQSRRQER KRRTTANPVY SGAVFEPERK
KSAVTYLNSP IHQGTRKRGR PPKFNSVPEL GSLTPTSPPS SLPSSPAHEK TEIGGFHFPV
LSQNLPLPSP NSGDGDIHED FCTVCRRSGQ LLMCDTCSRV YHLDCLDPPL KAIPKGMWIC
PKCQDQILKK EEAIPWPGTL AIVHSYIAYK AAKEEEKQKL VKWSTELKQE RDLLEQKVKQ
LSNSITKCME TKNTMLARQK EMQASLEKVK RLFRLVQGTQ GPTKPAEGAQ DAEGVANGTD
GGGGGSREED DTRSNGKTSE PSQQPAVTLS SSDTK
//
