HIC1_CHICK
ID HIC1_CHICK Reviewed; 676 AA.
AC Q90850; Q90851; Q90852;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Hypermethylated in cancer 1 protein;
DE Short=Hic-1;
DE AltName: Full=GammaFBP;
DE Flags: Fragment;
GN Name=HIC1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Embryonic lens;
RX PubMed=8088434; DOI=10.1006/dbio.1994.1243;
RA Liu Q., Shalaby F., Puri M.C., Tang S., Breitman M.L.;
RT "Novel zinc finger proteins that interact with the mouse gamma F-crystallin
RT promoter and are expressed in the sclerotome during early somitogenesis.";
RL Dev. Biol. 165:165-177(1994).
CC -!- FUNCTION: Binds specifically to the gamma F-1-binding motif of the
CC gamma F-crystallin promoter. May have a regulatory role in sclerotome
CC specification and/or differentiation. Isoform 2 functions as a
CC transcriptional repressor in lens cells.
CC -!- SUBUNIT: Interacts with CtBP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=3; Synonyms=GammaFBP-C;
CC IsoId=Q90850-1; Sequence=Displayed;
CC Name=1; Synonyms=GammaFBP-A;
CC IsoId=Q90850-2; Sequence=VSP_006827;
CC Name=2; Synonyms=GammaFBP-B;
CC IsoId=Q90850-3; Sequence=VSP_006828;
CC -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in kidney and lung.
CC Expression of isoform 2 is higher in the lens, retina and stomach, and
CC extremely low in heart, muscle, kidney and lung. Isoform 3 is weakly
CC expressed in heart, kidney and lens.
CC -!- DEVELOPMENTAL STAGE: In the embryo of stage 11, expressed predominantly
CC in the head mesenchyme surrounding the brain and in the paraxial
CC mesoderm. Highly expressed in presomitic mesoderm and then over the
CC entire epithelial somite. During somitic differentiation, expression
CC becomes restricted to the sclerotome. In the developing lens,
CC expression is most active at the beginning of lens fiber cell
CC differentiation.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. Hic subfamily. {ECO:0000305}.
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DR EMBL; X79011; CAA55644.1; -; mRNA.
DR EMBL; X79050; CAA55652.1; -; mRNA.
DR EMBL; X79051; CAA55653.1; -; mRNA.
DR PIR; I50643; I50643.
DR RefSeq; NP_990567.1; NM_205236.1. [Q90850-2]
DR RefSeq; XP_015151166.1; XM_015295680.1. [Q90850-3]
DR AlphaFoldDB; Q90850; -.
DR SMR; Q90850; -.
DR STRING; 9031.ENSGALP00000040837; -.
DR Ensembl; ENSGALT00000079270; ENSGALP00000053534; ENSGALG00000042077. [Q90850-2]
DR GeneID; 396164; -.
DR KEGG; gga:396164; -.
DR CTD; 3090; -.
DR VEuPathDB; HostDB:geneid_396164; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161725; -.
DR HOGENOM; CLU_015352_1_0_1; -.
DR InParanoid; Q90850; -.
DR OMA; GHDTRHE; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q90850; -.
DR Reactome; R-GGA-3232118; SUMOylation of transcription factors.
DR Proteomes; UP000000539; Chromosome 19.
DR Bgee; ENSGALG00000042077; Expressed in heart and 12 other tissues.
DR ExpressionAtlas; Q90850; baseline and differential.
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:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR028424; HIC1.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24394:SF16; PTHR24394:SF16; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 2: Evidence at transcript level;
KW Alternative splicing; Developmental protein; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN <1..676
FT /note="Hypermethylated in cancer 1 protein"
FT /id="PRO_0000046944"
FT DOMAIN 63..126
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 420..447
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 474..501
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 502..529
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 530..557
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 558..585
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..245
FT /note="Binding to CtBP"
FT REGION 264..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..35
FT /note="APGARPAASRERGHKSREERCGERGAAAGRRARGA -> MRVHRELGWLAEG
FT SGRAGRRARGA (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:8088434"
FT /id="VSP_006827"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8088434"
FT /id="VSP_006828"
FT NON_TER 1
SQ SEQUENCE 676 AA; 73759 MW; 3D3C7FD3302F32EC CRC64;
APGARPAASR ERGHKSREER CGERGAAAGR RARGAMLEAM EVPSHSRQLL LQLNTQRTKG
FLCDVIIVVQ NALFRAHKNI LAASSAYLKS LVVHDNLLNL DHEMVSPGIF RLILDFIYTG
RLGECEPGGE QSLGAVLAAA SYLQIPGLVA LCKKKLKRSG KYCHLRGGYA PYKLGRGLRA
TTPVIQACYS GTPRPVDLQP VEPAAPLNTQ CGELYASASQ GTPLHPHGLC PPERHCSPPC
GLDLSKKSPT GPSAQLLPTD RLLPAEPREP SLPPRHDSPP VSGGLLAGHP AAYKDSPPGG
EPGGHPHATD PFRSTPPCAE PPLPRGDGRE LMYRWMKHEP LGPYLDEGEA EKELEREEKA
ESPPAAPQPR YPSVESNDLE PDNSTSEETG SSEGPSPGDA LDRYCNHLGY EPESLGDNLY
VCIPCGKGFP SSEQLNAHVE AHNEEELYHK AAAEQAVPFL DKGGAGLGDI LRPYRCSSCD
KSYKDPATLR QHEKTHWLTR PYPCTICGKK FTQRGTMTRH MRSHLGLKPF ACDACGMRFT
RQYRLTEHMR IHSGEKPYEC QVCGGKFAQQ RNLISHMKMH AAGPDGKAKL DFPDSVYAMA
RLTADQLGLK QEKAAELLSH TSHFLSDPKA MESLYPLAKF TAEHLGLSQD KAAEVLAQAP
HLHADAARTI ERYSPP
