ID C3ZL59_BRAFL Unreviewed; 1073 AA.
AC C3ZL59;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=PHD finger protein 12 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_89536 {ECO:0000313|EMBL:EEN46741.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN46741.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN46741.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN46741.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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DR EMBL; GG666640; EEN46741.1; -; Genomic_DNA.
DR RefSeq; XP_002590730.1; XM_002590684.1.
DR AlphaFoldDB; C3ZL59; -.
DR STRING; 7739.C3ZL59; -.
DR eggNOG; KOG4299; Eukaryota.
DR InParanoid; C3ZL59; -.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd22703; FHA_PHF12; 1.
DR CDD; cd15533; PHD1_PHF12; 1.
DR CDD; cd15534; PHD2_PHF12_Rco1; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.20.60; PHD finger protein 12; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR031966; PHF12_MRG-bd.
DR InterPro; IPR038098; PHF12_MRG-bd_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
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; PTHR46309; PHD FINGER PROTEIN 12; 1.
DR PANTHER; PTHR46309:SF1; PHD FINGER PROTEIN 12; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF16737; PHF12_MRG_bd; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 50..99
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 319..369
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 900..954
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT REGION 24..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..460
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1073 AA; 115028 MW; 5207033EA167E406 CRC64;
MTTVTYDLDT SGGLMEKIQA LIAPPQSEEP PKRSRREARE PRRTGKSFNH DCCDSCKEGG
DLLCCDRCPA AFHLQCCDPP LCEEDLPEGE WLCHRCMVLE QFPELDDRDE TASNASVASS
TASYKQRNLR DKKIVRAECW TIFQASSSAS SSGTNGSKQA PNAAGSSSST GGNKQALGPA
AKQPAPSRKL SGASGVRGQS FERGDRALEN APVSATTRSK VLENGERGAG DAAVAMETGL
PGTGDGDEPK SGLETPFQLL LRAARLQNPK QFALPNEFMY HAALPGTSKT QWTYRQRHTS
RRETKKPYEI DNGMVPLPAK LCFTCNRSCR VSPLIQCDYC PLLFHQDCLD PPLTSMPAGR
WMCPNHAEHA ILNQKNLTLT ERCEIFNKFN GRISQHAVKI DFLYKIHRKY PPFRRERPAK
RKTINVPNAI KQQYVLPPPL MPPPPKRLCQ AAPPKEPRPT SPSTTAGEQE DWLKSVIAMQ
VKVAQHLTQQ QLRGETPGIK TNVPTSAPVT VETTRVPSPP VTASSGSVTT ATTASGTLDQ
SQHTNSVAVS TSRNSPVPNG PVKQEAALQR DSSPGLNAGP HGHQAGPHGH QAGPHGTAKP
QEVVANGPTC QRTEGKANGP VSSVGKSTSI SSSTPETLLD LLKPDPERSR DAAWTPNHSV
LRPKVGGEPE VKPGESRVIV TVPNSMTANL QQRFVTTVAG RQGTVAGRQG TVVTTRVMAP
NARSGQVPKV SVGQGVSTVA VNQSPVGGRS SPTVTGSAAG LMGSLGRMVN SQTAGSAKPV
NSPSPSVGVA GGNKTTPITM LSSSPTIQNL NNQLQAMIDG VGEVELSKLD QQLINILAFQ
RLQQLLPPKT SASQPSNKKT LFNGLNGPLL SGSSQQLQAR AVMCPLTGKG QPVQMCYRTL
HIGTGGDMDV CLNHYGNCSF VSAKHACIFY DETTQHYELL NYSEHGTTVD NVLYSCDFSD
KQAAVAPGNT IVSQVRSIIC RRQQEKEEEK ERKRMSASGS NQSKPCNCKA SSSSLIGGSG
AGWEGTALLH HGSYIKVGCL QFVFSIVDHA TRFAPSERKT PGKSTLLRST SVP
//
