IKZF_MYXGL
ID IKZF_MYXGL Reviewed; 505 AA.
AC Q6XDT6; Q6XDT7;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Ikaros family zinc finger protein;
DE AltName: Full=Ikaros-like transcription factor {ECO:0000312|EMBL:AAP84654.1};
DE Short=HIL {ECO:0000303|PubMed:14634112};
OS Myxine glutinosa (Atlantic hagfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata; Myxini;
OC Myxiniformes; Myxinidae; Myxininae; Myxine.
OX NCBI_TaxID=7769;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAP84654.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 6-198
RP (ISOFORM 1), SUBUNIT, TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=14634112; DOI=10.4049/jimmunol.171.11.6006;
RA Cupit P.M., Hansen J.D., McCarty A.S., White G., Chioda M., Spada F.,
RA Smale S.T., Cunningham C.;
RT "Ikaros family members from the agnathan Myxine glutinosa and the
RT urochordate Oikopleura dioica: emergence of an essential transcription
RT factor for adaptive immunity.";
RL J. Immunol. 171:6006-6013(2003).
CC -!- SUBUNIT: Heterodimer and homodimer with other IKAROS family members.
CC {ECO:0000269|PubMed:14634112}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H2S9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:14634112}; Synonyms=HIL2
CC {ECO:0000269|PubMed:14634112};
CC IsoId=Q6XDT6-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:14634112}; Synonyms=HIL1
CC {ECO:0000269|PubMed:14634112};
CC IsoId=Q6XDT6-2; Sequence=VSP_053189;
CC -!- TISSUE SPECIFICITY: Expression is strongest in the blood, gills and
CC intestine. {ECO:0000269|PubMed:14634112}.
CC -!- DOMAIN: N-terminal zinc-fingers recognize and bind to the consensus
CC Ikaros target site (5'-GGGA-3'), found in the promoter regions of
CC immunologically relevant genes. {ECO:0000269|PubMed:14634112}.
CC -!- DOMAIN: C-terminal zinc fingers mediate homodimerization and
CC heterodimerization. {ECO:0000269|PubMed:14634112}.
CC -!- SIMILARITY: Belongs to the Ikaros C2H2-type zinc-finger protein family.
CC {ECO:0000255}.
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 EMBL; AY237104; AAP84653.1; -; mRNA.
DR EMBL; AY237105; AAP84654.1; -; mRNA.
DR AlphaFoldDB; Q6XDT6; -.
DR SMR; Q6XDT6; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..505
FT /note="Ikaros family zinc finger protein"
FT /id="PRO_0000390936"
FT ZN_FING 18..40
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 46..68
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 74..96
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 102..128
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 448..470
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 476..500
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 262..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 98..155
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14634112"
FT /id="VSP_053189"
FT CONFLICT 187
FT /note="Q -> L (in Ref. 1; AAP84653)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="Q -> L (in Ref. 1; AAP84653)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 55386 MW; 415BAC831E90A17D CRC64;
MIQGSAPGGL SRLPSNKLTC EICGMVCIGP NVLMVHKRSH TGERPFQCNQ CGASFTQKGN
LLRHVKLHTD EKPFKCSLCS YACRRRDALM GHIRTHSVGK PYKCNFCSRS YKQRSSLEEH
QERCPGFHQG LPSSHLAENA FSKYGTTTER ADWEHVIRPG QEPPLLDDSA LLPTDVRLGL
DPAIETQLEP GFDKLSNQDR FSNNFQAKRK SSTPQKVFGQ KRMQLELSDI HYDQATSSLS
ERLHEVPGPV CAQTLEPSAS VFLNTPSPVT RSAGQALEAT RRLESESPGL PSDIGSIVRP
VYSQSVDNRF QHDSPLSTSR SGLSQQPGRH HPSPGILGGS LGGICGRPAE AVGDSRPVNM
PPGRGATSSP SNSCPDSTDT ESSHEERSHH RTGSGSSTSR PNGSTGRPHR PEMHQDNGRL
NRVSGASDSS SLPTYNVSGS DGEALRTYPC HHCGLLFLDH VMYTLHMGCH GFRDPFECNV
CGYRSRDRYE FSSHIIRGEH LPTAE