Entry euk:ZN431_MOUSE

ID   ZN431_MOUSE             Reviewed;         526 AA.
AC   E9QAG8;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   10-MAY-2017, entry version 51.
DE   RecName: Full=Zinc finger protein 431;
DE   AltName: Full=Zinc finger protein 932;
GN   Name=Znf431; Synonyms=Zfp431, Zfp932;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, INTERACTION WITH HDAC1 AND HDAC2, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=21177534; DOI=10.1074/jbc.M110.178780;
RA   He Z., Cai J., Lim J.W., Kroll K., Ma L.;
RT   "A novel KRAB domain-containing zinc finger transcription factor
RT   ZNF431 directly represses Patched1 transcription.";
RL   J. Biol. Chem. 286:7279-7289(2011).
RN   [4]
RP   FUNCTION, INTERACTION WITH HDAC2, AND DEVELOPMENTAL STAGE.
RX   PubMed=22391310; DOI=10.1016/B978-0-12-394622-5.00014-6;
RA   Huang G.J., He Z., Ma L.;
RT   "ZFP932 suppresses cellular Hedgehog response and Patched1
RT   transcription.";
RL   Vitam. Horm. 88:309-332(2012).
CC   -!- FUNCTION: Sequence-specific DNA binding transcriptional repressor.
CC       Represses target gene transcription by recruiting HDAC1 and HDAC2
CC       histone deacetylases. Acts as a specific transcriptional repressor
CC       for PTCH1 during embryonic development. Required for osteoblast
CC       differentiation and sonic hedgehog/SHH signaling response. Binds
CC       to the consensus site 5'-GCGCCC-3' in the promoter of PTCH1.
CC       {ECO:0000269|PubMed:21177534, ECO:0000269|PubMed:22391310}.
CC   -!- SUBUNIT: Interacts (via KRAB domain) with HDAC2; the interaction
CC       is direct. Interacts (via KRAB domain) with HDAC1.
CC       {ECO:0000269|PubMed:21177534, ECO:0000269|PubMed:22391310}.
CC   -!- INTERACTION:
CC       O09106:Hdac1; NbExp=3; IntAct=EBI-9549639, EBI-301912;
CC       P70288:Hdac2; NbExp=3; IntAct=EBI-9549639, EBI-302251;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21177534}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, heart, lung, thymus,
CC       spleen, lymph node, liver, kidney, muscle, testis, ovary, skin and
CC       uterus. {ECO:0000269|PubMed:21177534}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in limb mesenchyme at 10.5 dpc.
CC       Expressed in tooth, submandibular glands, thymus, thyroid,
CC       vibrissa follicles at 14.5 dpc. {ECO:0000269|PubMed:21177534,
CC       ECO:0000269|PubMed:22391310}.
CC   -!- DOMAIN: The KRAB domain is necessary for its repressive activity.
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DR   EMBL; AC123679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC012405; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS59681.1; -.
DR   RefSeq; NP_663538.2; NM_145563.2.
DR   UniGene; Mm.441438; -.
DR   ProteinModelPortal; E9QAG8; -.
DR   SMR; E9QAG8; -.
DR   BioGrid; 213490; 2.
DR   IntAct; E9QAG8; 2.
DR   STRING; 10090.ENSMUSP00000108159; -.
DR   iPTMnet; E9QAG8; -.
DR   PhosphoSitePlus; E9QAG8; -.
DR   PaxDb; E9QAG8; -.
DR   PRIDE; E9QAG8; -.
DR   Ensembl; ENSMUST00000112540; ENSMUSP00000108159; ENSMUSG00000066613.
DR   GeneID; 69504; -.
DR   KEGG; mmu:69504; -.
DR   UCSC; uc008ypn.1; mouse.
DR   CTD; 69504; -.
DR   MGI; MGI:1916754; Zfp932.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00760000119089; -.
DR   InParanoid; E9QAG8; -.
DR   OMA; KACNQAS; -.
DR   TreeFam; TF338854; -.
DR   PRO; PR:E9QAG8; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000066613; -.
DR   ExpressionAtlas; E9QAG8; baseline and differential.
DR   Genevisible; E9QAG8; MM.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; TAS:UniProtKB.
DR   GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF01352; KRAB; 1.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 15.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 9.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 15.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
PE   1: Evidence at protein level;
KW   Complete proteome; Differentiation; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    526       Zinc finger protein 431.
FT                                /FTId=PRO_0000425265.
FT   DOMAIN        5     76       KRAB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00119}.
FT   ZN_FING     104    126       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     132    154       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     160    182       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     188    210       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     216    238       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     244    266       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     272    294       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     300    322       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     328    350       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     356    378       C2H2-type 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     384    406       C2H2-type 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     412    434       C2H2-type 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     440    462       C2H2-type 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     468    490       C2H2-type 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     496    518       C2H2-type 15. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   CONFLICT    323    323       I -> T (in Ref. 2; BC012405).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       190    210       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       132    154       ismart:ZnF_C2H2 [T]
FT   MYHIT       328    355       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       440    467       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       218    238       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       442    462       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       440    462       ismart:ZnF_C2H2 [T]
FT   MYHIT       412    439       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       302    322       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       160    187       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       358    378       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       356    383       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       384    411       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       188    215       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       468    490       ismart:ZnF_C2H2 [T]
FT   MYHIT       272    294       ismart:ZnF_C2H2 [T]
FT   MYHIT       300    327       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       162    182       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       414    434       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       274    294       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       496    523       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       272    299       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       496    518       ismart:ZnF_C2H2 [T]
FT   MYHIT       160    182       ismart:ZnF_C2H2 [T]
FT   MYHIT       412    434       ismart:ZnF_C2H2 [T]
FT   MYHIT       104    126       ismart:ZnF_C2H2 [T]
FT   MYHIT       216    238       ismart:ZnF_C2H2 [T]
FT   MYHIT       468    495       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       104    131       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       356    378       ismart:ZnF_C2H2 [T]
FT   MYHIT       328    350       ismart:ZnF_C2H2 [T]
FT   MYHIT       330    350       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       498    518       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       470    490       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       188    210       ismart:ZnF_C2H2 [T]
FT   MYHIT         5     76       iprf:KRAB [T]
FT   MYHIT         5     45       ipfam:KRAB [T]
FT   MYHIT       246    266       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       134    154       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       300    322       ismart:ZnF_C2H2 [T]
FT   MYHIT       386    406       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       106    126       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       244    266       ismart:ZnF_C2H2 [T]
FT   MYHIT       244    271       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       132    159       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT         5     61       ismart:KRAB [T]
FT   MYHIT       384    406       ismart:ZnF_C2H2 [T]
FT   MYHIT       216    243       iprf:ZINC_FINGER_C2H2_2 [T]
SQ   SEQUENCE   526 AA;  61280 MW;  1F7F44631FEB1BA2 CRC64;
     MVDALTYDDV YVNFTQEEWA LLNPSQKSLY KDVMLETYRN LNAVGYNWED SNIEEHCESS
     RRHGRHERNH TGEKPYEGIQ YGEAFVHHSS LQMRKIIHTG EKRYKCNQCD KAYSRHSILQ
     IHKRTHSGEK PYECNQCGKA FTQHSHLKIH MVTHTGEKPY KCDQCGKAFA FHSTLQVHKR
     THTGEKPYEC NQCSKAFAHH CHLRVHKRIH TGEKPYKCDQ CGKAFVGQND LKRHERVHTG
     EKPYKCNECG KAFVCNASLR THKTTHTGVK PYECKQCTKS FASHGQLQKH ERIHTGEKPY
     KCDQCGKAFA SHDKFQKHER IHIGEKPYKC KQCTKSFASH DKLQKHERIH TGEKPYECKQ
     CTKSFASHNK LQKHERIHTG EKPYKCDQCN KAFVYESYLQ VHKKTHTGEK PYKCNECGKA
     FARHSHLKVH KITHTGEKPY KCNQCGKALA YHSTLQVHQR THTGEKPYEC EQCGKAFANQ
     SYFQVHKRIH TGEKPYKCDQ CGKAFVGSSD LKRHERVHTG RETLQM
//