ID A0A3Q3GP21_9LABR Unreviewed; 1148 AA.
AC A0A3Q3GP21;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Zinc finger E-box binding homeobox 1 {ECO:0000313|Ensembl:ENSLBEP00000035787.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000035787.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000035787.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Sequence-specific transcription factor which is part of a
CC developmental regulatory system that provides cells with specific
CC positional identities on the anterior-posterior axis.
CC {ECO:0000256|ARBA:ARBA00003263}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the delta-EF1/ZFH-1 C2H2-type zinc-finger
CC family. {ECO:0000256|ARBA:ARBA00009867}.
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DR AlphaFoldDB; A0A3Q3GP21; -.
DR STRING; 56723.ENSLBEP00000035787; -.
DR Ensembl; ENSLBET00000037300.1; ENSLBEP00000035787.1; ENSLBEG00000026840.1.
DR GeneTree; ENSGT00950000183208; -.
DR InParanoid; A0A3Q3GP21; -.
DR OrthoDB; 4266655at2759; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:UniProt.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 6.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR008598; Di19_Zn-bd.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24391; HISTONE H4 TRANSCRIPTION FACTOR-RELATED; 1.
DR PANTHER; PTHR24391:SF11; ZINC FINGER E-BOX-BINDING HOMEOBOX 2; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR Pfam; PF05605; zf-Di19; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 3: Inferred from homology;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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:PRU00042}.
FT DOMAIN 195..223
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 225..252
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 265..292
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 293..327
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 894..921
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 922..949
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 950..978
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 29..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1067
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1099
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1137
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1148 AA; 125595 MW; AA98A3FE562BAE73 CRC64;
MVLATWVGEV REGDVVKLSV VNQVRRRGGE VEAGGGGGGG RGGERGGDSP AAFRHNERIM
ADGPRCKRRK QANPRRNNVT NYNNVVEAGS ESDDEDKLHI VEEEGSLADG ADCDSTLPDE
EHPREHCWDG VKEDCVSDAE DDGSTDALME EMLQQGDTAV IYPEAPEDEP QRQDTPDPSI
HDENAGTPDS FSQLLTCPYC ARGYKRYSSL KEHIKYRHER TEESFNCPEC SYSFAYRAQL
ERHMTVHKSG RDQRHITQSG GNRKFKCTEC GKAFKYKHHL KEHLRIHSGE KPYECSNCKK
RFSHSGSYSS HISSKKCISV ISVNGRPRSG NTKAQNQGPS PVLSTPPSVL RTQIREKLEH
SKPLQEQLPL NQIKTEPVDY EYKPTLITSS SVTAMNGGIF NGGVAAPLQG TVQAVVLPTV
GLMSPISINL ADLQNALKVA VDGNVIRQVL ESNAKGQGQL NSGLTTGTLH PAQQQLISAI
SLPIVGQDGN AKIIINYSLD PNQGQITAKN LKQEPEQISL AQNTTDTFKS QKLPEDLTMR
GSRPNKTKEK EEKTTKTCLL CDSCPGGLES LHALKHCKKD GLRLNGTGLD KSESAVAALL
SEGGLCNQPK NLLSLLKAYF ALNAEPSKDE LAKISDSVSL PINVVKKWFD KMQEGQISLG
APTPPSEEED TCEASSVVSL VQGKDTAMSP SVNTDSPTEA TPAEVNGNHS SPASPSPLNL
TAGGPVPAQP SQSTEGPLDL SLPKPAREEA DRVVAKARVY PSPPSGSTIV DEPLNLTCTK
KEASPFSAMG GSPIALYASQ PSAKPLDIVT TMQCLRALST NNKQTILIPQ LAYSYTTTAS
SPAGTQTQET IHLNGIKEER QDTGSEGVST VEEQNDSDSG PQRKKMKKTE SGMYACDLCD
KIFQKSSSLL RHKYEHTGKR PHECGICSKA FKHKHHLIEH MRLHSGEKPY QCDKCGKRFS
HSGSYSQHMN HRYSYCKKET QGQGGVPGSP EEEAEIQAEM EALRRLQSQL LGPSQLDSDE
RGSSTREDEE SEEEEEMEDG AVDMDDIQVV QIEDEGGEDE EEVERNEEEI ERVLVQEGAE
EEEETEVEMK EEEEEADTRQ EEVLGSIQEE EEDKAEEEEA MDAEEGVTEE EKAEGEVAEE
SGGETNSN
//
