ID A0A3P8PBU4_ASTCA Unreviewed; 1089 AA.
AC A0A3P8PBU4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Zinc finger E-box binding homeobox 1 {ECO:0000313|Ensembl:ENSACLP00000014496.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000014496.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000014496.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000014496.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; A0A3P8PBU4; -.
DR Ensembl; ENSACLT00000014843.1; ENSACLP00000014496.1; ENSACLG00000009867.1.
DR GeneTree; ENSGT00950000183208; -.
DR Proteomes; UP000265100; Chromosome 9.
DR Bgee; ENSACLG00000009867; Expressed in spleen and 7 other cell types or tissues.
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 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; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24391; HISTONE H4 TRANSCRIPTION FACTOR-RELATED; 1.
DR PANTHER; PTHR24391:SF18; ZINC FINGER PROTEIN 1; 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; 6.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
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 123..151
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 153..180
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 193..220
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 820..847
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 848..875
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 876..904
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..969
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..991
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1021
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1089
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1089 AA; 118913 MW; AABF70FAEE7AD60F CRC64;
LSDTPQCVTN YNNVVEAGSD SDDEDKLHIV EEEGSLADGA DCESTLPEDE HPREHCWDRV
KEDCVSDGED DVSTDALVEE MLQQGDTAVI YPEAPDDEPQ RQGTPDTGIH DENGTPDSFS
QLLTCPYCAR GYKRYSSLKE HIKYRHEKTE ESFSCPECNY SFAYRAQLER HMTVHKSARD
QRHITQSGGN RKFKCTECGK AFKYKHHLKE HLRIHSGEKP YECSNCKKRF SHSGSYSSHI
SSKKCISVIS VNGRSRLGNA KTQSQGQSPG LSTPPSVLRT QIREKLEHSK PLQEQLPLNQ
IKTEPVDYEY KPTVISSPTV TAMNGGVFGG GAAAPLQGTV QAVVLPTVGL VSPISINLAD
LQNALKVAVD GNVIRQVLEN NAKGQVNSGL TTGTLHTPQQ QLISAISLPI VGQDGNAKII
INYNLDPNQG QLTAHNLKKE PEPMSPAQTT TNTFKSQKLP EDLTIRGNRA NETKEKEEKT
TKTCLLCDNC PGGLDALHAL KHCKKDCLKL NGAGLDRSDS TIAALLSDGG LCSQPKNLLS
LLKAYFALNA EPTKDELAKI SDSVSLPVSV VKKWFEKMQE GQISLGAPTP PSEEEDTCES
NSVVSLVPGK DKATIIPPVT QDSPTEATPA EINGTHSSPA SPSPLNLTAG GPGPAKKTQS
TEGPLDLSLP KPARDEAERA ANKTCLYPSP SSGSANMDEP LNLTCTKKEA LPLSAMGTCP
TALYASQPSA KSLDIVTTMQ CLRALATNNK QTILIPQLAY TYTTTANSPA GTETHETIHL
NGVKDRQDTG SEGVSTVEEQ NDSDSGPPRK KMKKTDSGMY ACDLCDKIFQ KSSSLLRHKY
EHTGKRPHEC GICSKAFKHK HHLIEHMRLH SGEKPYQCDK CGKRFSHSGS YSQHMNHRYS
YCKKETQSQA GGRESPEEDG ETQIDMEVLS GAQRQLLAPS QLDSDERGSS TREDEESEEE
EEEEGVVDMD DIQVVQIGDE GGEEEDEPEE RNEEEMKRVA VEEGGEEEKS ETGEEEADTG
QEDGLGSVQE ETNVEEEKAM ETEGSSPEAE TEGGLSEREG GEVAEESQSE TNRNEVCEDE
KQTPREKGD
//
