ID A0A3P8YFX0_ESOLU Unreviewed; 1216 AA.
AC A0A3P8YFX0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Zinc finger E-box binding homeobox 2b {ECO:0000313|Ensembl:ENSELUP00000014986.1};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000014986.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000014986.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000014986.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00108}.
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; A0A3P8YFX0; -.
DR Ensembl; ENSELUT00000023943.2; ENSELUP00000014986.1; ENSELUG00000014998.2.
DR GeneTree; ENSGT00950000183208; -.
DR Proteomes; UP000265140; LG22.
DR Bgee; ENSELUG00000014998; Expressed in spleen and 14 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
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; 5.
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; SM00389; HOX; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Homeobox {ECO:0000256|PROSITE-ProRule:PRU00108};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Reference proteome {ECO:0000313|Proteomes:UP000265140};
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 199..227
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 229..256
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 270..297
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 644..693
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DOMAIN 1029..1056
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1057..1085
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DNA_BIND 646..694
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 167..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1216 AA; 136833 MW; 5CB9155A7D693B3D CRC64;
MLCNHQDAAL NYENVMETGS ETEDEDKLLV SEEDGLLNGL CSPASLTNHE AGSPRVGHAL
LTKEDEDDDM RDSGVDHVWH DNDMLHASVD GTDEMKDEYD TMRPEATLQS VGNGTVRNVD
CTSEFEEFFS KRSKLQEDSH SHVVSIAEYL QRGDTAIIYP EAPEGEELSR LGTPEAPEVN
GQEENDLPPG TPDAFAQLLT CPYCDRGYKR LTSLKEHIKY RHEKNEENFA CPLCNYTFAY
RTQLERHMAT HKPGRDQHQL LNQGAGNRKF KCTECGKAFK YKHHLKEHLR IHSGEKPYEC
PNCKKRFSHS GSYSSHISSK KCIGLIAVNG RMRNNMKTGS SPTSASSSPT NTAINQLRHK
LENGNSKPTG HHQDHSNHHL NIKAEPLDFN DYKLMMASHG FGGPGPFMNG GMGGNGSPLG
IHGSAQSPMH HMGMGIEQQL LGYPALSNNL SEVQKVLQIV DNTVCRQKMD CKPEEISKLK
AYMKELGNQI EEQKQGLTSH GGHQIGLPVV SHNGATKSII DYTLEKVNEA KACLQSLTTD
SKRQISNIKR EKSNHMLDLG TEEKMHENHI MFTPFACQYC KETFPGPIPL HQHERYLCKM
NEEIKAVLQP SENLMPTKQG MFTEKHALLL SSMLSEKSPI NPYKDHMSVL KAYFAMNMEP
NSEELLKISI AVGLPQEFVK EWFEQRKVYQ YGNPRTPPLE QQRNNHSDLV LAANNHNHTK
DLMAARSPVS MIKSADRDRD HHITSPSITE LQNNVNNCEN QHRLMKANTF SGHTKHTGDH
SKLDHHSRSN TPSPLNLSST SSKNSHASSY TPNSLTSEDL NLGLNLNTNQ SEQPLDLSLP
KPVREPKHAV TMRSGPKLNS IGHHDRSGVP SPREHFEEPL NLAYLKKEFE ARGGQNHHNG
DLNKSTSPLF GMNPFGAKPM YTSLPPHSAF PPATFMPPMQ ASIPGLRPYP GLDQMGFLPH
MAYTYATGAA TFAEMQQQQR RKYQRKPGFQ GELLDGTAGY MSGLEDMTDS DSCLSRKKIK
KTESGKRPHQ CQICKKAFKH KHHLIEHSRL HSGEKPYQCD KCGKRFSHSG SYSQHMNHRY
SYCKREAEER EAAEREAREK GHLEPTELLM SRAYLQGMTP QGYPGLEDRE GILRDGGMNG
GMRDRQKEVE GTYAKIGRRE EDFEEEEEES ENKSMDTDPD TLRDEEENGE HSMDDSSLDG
KTETKSDHED NMEDGM
//
