ID A0A2Y9DI73_TRIMA Unreviewed; 1214 AA.
AC A0A2Y9DI73;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Zinc finger E-box-binding homeobox 2 isoform X2 {ECO:0000313|RefSeq:XP_004375165.1};
GN Name=LOC101352107 {ECO:0000313|RefSeq:XP_004375165.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004375165.1};
RN [1] {ECO:0000313|RefSeq:XP_004375165.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_004375165.1; XM_004375108.3.
DR AlphaFoldDB; A0A2Y9DI73; -.
DR GeneID; 101352107; -.
DR KEGG; tmu:101352107; -.
DR OrthoDB; 4266655at2759; -.
DR Proteomes; UP000248480; 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 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:SF18; ZINC FINGER PROTEIN 1; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR Pfam; PF05605; zf-Di19; 1.
DR Pfam; PF12874; zf-met; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
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 ECO:0000313|RefSeq:XP_004375165.1};
KW Homeobox {ECO:0000313|RefSeq:XP_004375165.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
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 211..239
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 241..263
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 282..309
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 999..1026
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1027..1054
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1055..1083
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1171
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1214 AA; 136567 MW; 870C567FF8D2E1C7 CRC64;
MKQPIMADGP RCKRRKQANP RRKNVVNYDN VVDTGSETDE EDKLHIAEED GIANPLGQET
SPASMPNHES SPHVSQALLP RDEEEDEIRE GGVEHTWHNS EILQASVDGP EEMKEDYDTM
GPEATIQTTV NNGTVKNANC TSDFEEYFAK RKLEERDGHA VSIEEYLQRS DTAIIYPEAP
EELSRLGTPE ANGQEENDLP PGTPDAFAQL LTCPYCDRGY KRLTSLKEHI KYRHEKNEEN
FSCPLCSYTF AYRTQLERHM LTHKPGTDQH QMLTQGAGNR KFKCTECGKA FKYKHHLKEH
LRIHSGEKPY ECPNCKKRFS HSGSYSSHIS SKKCIGLISV NGRMRNNIKT GSSPNSVSSS
PTNSAITQLR NKLENGKPLS MSEQTGLLKI KTEPLDFNDY KVLMATHGFS GTSPFMNGGL
GATSPLGVHP SAQSPMQHLG VGMEAPLLGF PTMNSNLSEV QKVLQIVDNT VSRQKMDCKA
EEISKLKGYH MKDPCSQPEE QVVTSPNIPP VGLPVVSHNG ATKSIIDYTL EKVNEAKACL
QSLTTDSRRQ ISNIKKEKLR TLIDLVTDDK MIENHNIATP FSCQFCKESF PGPIPLHQHE
RYLCKMNEEI KAVLQPHENI VPNKAGVFVD NKALLLSSVL SEKGMTSPIN PYKDHMSVLK
AYYAMNMEPN SDELLKISIA VGLPQEFVKE WFEQRKVYQY SNSRSPSLER NSKLLAPNNN
PPTKDSLLPR SPVKPMDSIT SPSIAELHNS VTNCDPPLRL TKPSHFTNIK PAEKLDHSRS
NTPSPLNLSS TSSKNSHSSS YTPNSFSSEE LQAEPLDLSL PKQMKEPKSI IAAKNKTKAS
SISLDHNSIS SSSENSDEPL NLTFIKKEFS NSNNLDNKST NPVFGMNPFS AKPLYTALPP
QSAFPPATFM PPVQTSIPGL RPYPGLDQMS FLPHMAYTYP TGAATFAEMQ QRRKYQRKQG
FQGELLDGTQ DYMSGLDDMT DSDSCLSRKK IKKTESGMYA CDLCDKTFQK SSSLLRHKYE
HTGKRPHQCQ ICKKAFKHKH HLIEHSRLHS GEKPYQCDKC GKRFSHSGSY SQHMNHRYSY
CKREAEEREA AEREAREKGH LEPTELLMNR AYLQSITPQG YSDSEERESM PRDGESEKEH
EKEGEDGYEK LGRQDGDEEF EEEEEESENK SMDTDPETIR DEEETGDHSM DDSSEDGKME
TKSDHEEDNM EDGM
//
