GZF1_RAT
ID GZF1_RAT Reviewed; 707 AA.
AC D3ZUU2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=GDNF-inducible zinc finger protein 1;
DE AltName: Full=Zinc finger protein 336;
GN Name=Gzf1; Synonyms=Zfp336;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcriptional repressor that binds the GZF1 responsive
CC element (GRE) (consensus: 5'-TGCGCN[TG][CA]TATA-3'). May be regulating
CC VSX2/HOX10 expression. {ECO:0000250|UniProtKB:Q9H116}.
CC -!- SUBUNIT: Interacts with NCL. {ECO:0000250|UniProtKB:Q9H116}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H116}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9H116}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9H116}. Note=Nuclear localization depends upon
CC NCL. {ECO:0000250|UniProtKB:Q9H116}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; CH474026; EDL95094.1; -; Genomic_DNA.
DR EMBL; CH474026; EDL95095.1; -; Genomic_DNA.
DR RefSeq; NP_001101258.1; NM_001107788.1.
DR RefSeq; XP_006235215.1; XM_006235153.3.
DR RefSeq; XP_006235216.1; XM_006235154.2.
DR RefSeq; XP_008760496.1; XM_008762274.2.
DR RefSeq; XP_017447260.1; XM_017591771.1.
DR AlphaFoldDB; D3ZUU2; -.
DR SMR; D3ZUU2; -.
DR STRING; 10116.ENSRNOP00000006287; -.
DR iPTMnet; D3ZUU2; -.
DR PhosphoSitePlus; D3ZUU2; -.
DR PaxDb; D3ZUU2; -.
DR PeptideAtlas; D3ZUU2; -.
DR Ensembl; ENSRNOT00000006287; ENSRNOP00000006287; ENSRNOG00000004735.
DR GeneID; 311508; -.
DR KEGG; rno:311508; -.
DR UCSC; RGD:1562321; rat.
DR CTD; 64412; -.
DR RGD; 1562321; Gzf1.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00870000136554; -.
DR HOGENOM; CLU_018348_1_0_1; -.
DR InParanoid; D3ZUU2; -.
DR OMA; VVYRCET; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; D3ZUU2; -.
DR TreeFam; TF350965; -.
DR PRO; PR:D3ZUU2; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000004735; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; D3ZUU2; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..707
FT /note="GDNF-inducible zinc finger protein 1"
FT /id="PRO_0000409661"
FT DOMAIN 31..103
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 316..338
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 347..370
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 376..399
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 406..428
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 434..456
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 462..484
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 490..512
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 518..540
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 546..568
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 574..596
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 149..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 707 AA; 79887 MW; 2DB5E7ADA8C5E926 CRC64;
MESGTVLLES KSSPLNLLHE MHELRLLGHL CDVTVIVDYQ GVREDFMAHK AVLAATSKFF
KEVFLNEKRA DGTRTNVYLS EVQVVDFASF LEFVYTARVR VKEDRVQQML EVAEKLKCLD
LSETCLQLKK QMLESVLLEL QNFSESQEVE ASSGPQVSVT PSSKASVPAG EDAHSNGLVD
SSDYPIERLG NGLSPETPSK KCKEKLDKKK DVAKPPFPKI RRASGRLAGK KVFVEIPKKK
YTRRLREQQK SAEEAAKNDK CPQDQSPDNE RVEAEPASKS EACPASVERE ESLQKVEGEK
EEEEGKDGEE KKKSNFQCTV CDKAFLYEKS FLKHIKYHHG VATEVVYRCD TCGQTFANRC
NLKSHQRHVH SSERHFPCEM CAKKFKRKKD VKRHVLQVHE GGGERHRCGQ CGKGLSSKTA
LRLHERTHTG DKPYGCTKCD AKFSQPSALK THLRVHTGER PFVCDECGAR FTQNHMLIYH
KRCHTGERPF MCETCGKSFA SKEYLKHHNR IHTGSKPFKC EVCLRTFAQR NSLYQHIKVH
TGERPYCCDQ CGKQFTQVNA LQRHHRIHTG EKPYMCNACG RTFTDKSTLR RHTSIHDKNT
PWKSFLVIVD GSPKNDEGQK TEQPDEEYAS PKLSDRLLSF GENSHFNNLL EVQGNVPAVQ
ENSSTDTACK AVVSQDALLT TSISALGELT PQTVSMPAHL PSLTNME
