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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}.
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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
 
 
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