ID A0A3Q2ZP30_KRYMA Unreviewed; 1195 AA.
AC A0A3Q2ZP30;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Zinc finger E-box binding homeobox 2 {ECO:0000313|Ensembl:ENSKMAP00000005431.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000005431.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000005431.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 RefSeq; XP_017287262.1; XM_017431773.1.
DR AlphaFoldDB; A0A3Q2ZP30; -.
DR Ensembl; ENSKMAT00000005528.1; ENSKMAP00000005431.1; ENSKMAG00000004104.1.
DR GeneID; 108245114; -.
DR CTD; 564934; -.
DR GeneTree; ENSGT00950000183208; -.
DR OMA; QENMFTP; -.
DR OrthoDB; 4266655at2759; -.
DR Proteomes; UP000264800; Unplaced.
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 Developmental protein {ECO:0000256|ARBA:ARBA00022473};
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:UP000264800};
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 208..236
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 238..265
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 279..306
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 651..700
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DOMAIN 1010..1037
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1038..1066
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DNA_BIND 653..701
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1195 AA; 133733 MW; F003E78CBE13BACA CRC64;
MKQEIMADGP RCKRRKQANP RRKNALNYEN LVETGSETEE EDKLPVSEED PLINGTGSPG
SLTNPEVSPR TESHGLLTKD EDDDEMRDSG VEHIWPDNDI LSASVDGTDE IKDDFDALGP
DATLQAVGNG TVKSVDCTSE LEDFFAKRKL DDGDSHVVSI AEYLQRGDTA IIYPEAPEEL
SRLGTPEATG PEENDLPPGT PDAFAQLLTC PYCDRGYKRL TSLKEHIKYR HEKNEENFAC
PLCNYTFAYR TQLERHMATH KPARDQHQLL NQAAGNRKFK CTECGKAFKY KHHLKEHLRI
HSGEKPYECP NCKKRFSHSG SYSSHISSKK CIGLIAVNGR MRSSLKPGSS PTSASASPTN
TAITQLRQKL ENGKPLGLTD HNNHLSIKTE PLDFNDYKLM MASHGFGAPV PFMNGGMGGN
SPLGVNHNST AQSPLQHLSM AALESQFTGY PGPLGNNLSE VQKVLQIVDN TVCRQKMDCK
PEELSKLKAY MKELGTQMEE QKQSLMSPGG PQVGLPLVNH NGATKSIIDY TLEKVNEAKA
CLQSLTTDSK RQISNIKREK PNHMLEGGVD EKVQENMFTP YACQYCKETF PGPIPLHQHE
RYLCKMNEEI KAVLQPSENL MPNKPGIFME KNSHSSILSE KGLTGPLNPY RDHMSVLMAY
FAMNMDPNSE ELLKISIAVG LPQEFVKEWF EQRKMQEYST TRTPPLEHRN NADIVVGTNN
HQTQPKDSLA ARSPVTLIKP TDRITSPSIA ELHNNVNNCD SSLRHLKNHQ FSGSTKPVGE
KLDHSRSNTP SPLNLSSTSS KNSHSSSYTP NSLTSEDLQA EPLDLSLPRL MKEPKHALTV
KSRPKVNSIT IDHNSIPSPR EHFEEPLNLA YLKKEFSGST NNGNLEKSTS PIFGINPFAA
KPLYTSLPPQ TAFPPATFMP PMQASIPGLR PYPGMDQMGF LPHMAYTYAA GAATFAEMQQ
RRKYQRKPGF QGDLLDGTPD YLSGLDDMTD PDSCLSRKKI KKTESGKRPH QCQICKKAFK
HKHHLIEHSR LHSGEKPYQC DKCGKRFSHS GSYSQHMNHR YSYCKREAEE REAAEREARE
KGHLEPTELL MSRAYLQGMT PQGYPELAER EAILRHDAVN GGIREGRKEV DGTYAKIGRR
DEFEEEEEEE SKSMDTDPDT LRDEEENGEH SMDDSSLDGK METKSDHEDA MEDGM
//
