ID H3AN77_LATCH Unreviewed; 401 AA.
AC H3AN77;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Pygopus family PHD finger 2 {ECO:0000313|Ensembl:ENSLACP00000011098.2};
GN Name=PYGO2 {ECO:0000313|Ensembl:ENSLACP00000011098.2};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000011098.2, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000011098.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Involved in signal transduction through the Wnt pathway.
CC {ECO:0000256|ARBA:ARBA00037400}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AFYH01140235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01140236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006003375.1; XM_006003313.2.
DR AlphaFoldDB; H3AN77; -.
DR STRING; 7897.ENSLACP00000011098; -.
DR Ensembl; ENSLACT00000011181.2; ENSLACP00000011098.2; ENSLACG00000009766.2.
DR GeneID; 102356512; -.
DR KEGG; lcm:102356512; -.
DR CTD; 90780; -.
DR eggNOG; ENOG502QSRS; Eukaryota.
DR GeneTree; ENSGT00530000063948; -.
DR HOGENOM; CLU_686883_0_0_1; -.
DR InParanoid; H3AN77; -.
DR OMA; GGMVFPC; -.
DR OrthoDB; 5403712at2759; -.
DR TreeFam; TF333020; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000009766; Expressed in muscle tissue and 6 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd15636; PHD_PYGO2; 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; PTHR23194; PYGOPUS; 1.
DR PANTHER; PTHR23194:SF7; PYGOPUS HOMOLOG 2; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 322..380
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 42220 MW; 3AAF476C5FB78754 CRC64;
MAAEHDKLEG AATHSRRAKA GLQMKSPEKK RRKSSTQSAP FSHLSEFAPP LTPMVDHLVA
SNPFDDDYPP KGGAPLTPFL NNPGAYGNFR MQGGMPPQLN PGYGGGLQPI RRPAPPPFPP
NQMGPGFNMP HNPNFGQPGN LGFPSQPFNQ GIGQNFSPQT GQMMQPGSGP VSTFGPMMSP
NIGQPPRAEM GAGPGPGMGA PGGLSVGQRF GQPGNPFSQA PMMRPNHSLP NIPTNPGPFP
NPDQSFPPGG DESAKNLNPP SGTAPFSQEH TGSPATINGT QQNFNQNNGG QNSSTPEPSG
SNLPVANKNP GATGHQPPPG LVYPCGACRN EVNDDQDAIL CEASCQKWFH RECTGMTESA
YTLLTREASA VWACDFCLKT KEIQSVYVRE GIGQLVAAND G
//
