ZN516_MOUSE
ID ZN516_MOUSE Reviewed; 1157 AA.
AC Q7TSH3;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Zinc finger protein 516 {ECO:0000312|MGI:MGI:2443957};
GN Name=Znf516 {ECO:0000250|UniProtKB:Q92618};
GN Synonyms=Kiaa0222 {ECO:0000312|EMBL:BAC97902.1},
GN Zfp516 {ECO:0000312|MGI:MGI:2443957};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 735-1157.
RC TISSUE=Fetal brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH PRDM16, SUBCELLULAR
RP LOCATION, REGION, INDUCTION BY COLD, AND TISSUE SPECIFICITY.
RX PubMed=25578880; DOI=10.1016/j.molcel.2014.12.005;
RA Dempersmier J., Sambeat A., Gulyaeva O., Paul S.M., Hudak C.S.,
RA Raposo H.F., Kwan H.Y., Kang C., Wong R.H., Sul H.S.;
RT "Cold-inducible Zfp516 activates UCP1 transcription to promote browning of
RT white fat and development of brown fat.";
RL Mol. Cell 57:235-246(2015).
RN [4]
RP INTERACTION WITH PWWP2B AND HDAC1.
RX PubMed=34180153; DOI=10.1002/advs.202102060;
RA Yan L., Jin W., Zhao Q., Cui X., Shi T., Xu Y., Li F., Jin W., Zhang Z.,
RA Zhang Z., Tang Q.Q., Pan D.;
RT "PWWP2B Fine-Tunes Adipose Thermogenesis by Stabilizing HDACs in a NuRD
RT Subcomplex.";
RL Adv. Sci. 8:e2102060-e2102060(2021).
CC -!- FUNCTION: Transcriptional regulator that binds to the promoter and
CC activates the transcription of genes promoting brown adipose tissue
CC (BAT) differentiation. Among brown adipose tissue-specific genes, binds
CC the proximal region of the promoter of the UCP1 gene to activate its
CC transcription and thereby regulate thermogenesis. May also play a role
CC in the cellular response to replication stress (By similarity).
CC {ECO:0000250|UniProtKB:Q92618, ECO:0000269|PubMed:25578880}.
CC -!- SUBUNIT: Interacts with PRDM16; the interaction is direct and may play
CC a role in the transcription of brown adipose tissue-specific genes
CC (PubMed:25578880). Interacts with PWWP2B (PubMed:34180153). Interacts
CC with HDAC1; this interaction is enhanced in the presence of PWWP2B
CC (PubMed:34180153). {ECO:0000269|PubMed:25578880,
CC ECO:0000269|PubMed:34180153}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25578880}.
CC -!- TISSUE SPECIFICITY: Expressed by adipocytes more specifically in brown
CC adipose tissue compared to white adipose tissue (WAT).
CC {ECO:0000269|PubMed:25578880}.
CC -!- INDUCTION: Up-regulated in response to cold in brown and subcutaneous
CC white adipose tissue where it may regulate non-shivering thermogenesis
CC (at protein level). {ECO:0000269|PubMed:25578880}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice die immediately after birth. 20.5
CC dpc embryos display an impaired development of brown adipose tissue.
CC {ECO:0000269|PubMed:25578880}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; BC053104; AAH53104.1; -; mRNA.
DR EMBL; AK129092; BAC97902.1; -; mRNA.
DR CCDS; CCDS29380.1; -.
DR RefSeq; NP_001170935.1; NM_001177464.1.
DR RefSeq; NP_898854.1; NM_183033.2.
DR RefSeq; XP_006526561.1; XM_006526498.1.
DR RefSeq; XP_006526562.1; XM_006526499.3.
DR RefSeq; XP_006526563.1; XM_006526500.2.
DR RefSeq; XP_006526564.1; XM_006526501.3.
DR RefSeq; XP_006526565.1; XM_006526502.3.
DR RefSeq; XP_006526566.1; XM_006526503.3.
DR RefSeq; XP_011245387.1; XM_011247085.2.
DR AlphaFoldDB; Q7TSH3; -.
DR BioGRID; 236692; 4.
DR IntAct; Q7TSH3; 3.
DR MINT; Q7TSH3; -.
DR STRING; 10090.ENSMUSP00000126629; -.
DR iPTMnet; Q7TSH3; -.
DR PhosphoSitePlus; Q7TSH3; -.
DR MaxQB; Q7TSH3; -.
DR PaxDb; Q7TSH3; -.
DR PeptideAtlas; Q7TSH3; -.
DR PRIDE; Q7TSH3; -.
DR ProteomicsDB; 299584; -.
DR Antibodypedia; 5767; 70 antibodies from 16 providers.
DR Ensembl; ENSMUST00000071233; ENSMUSP00000071216; ENSMUSG00000058881.
DR Ensembl; ENSMUST00000171238; ENSMUSP00000126629; ENSMUSG00000058881.
DR GeneID; 329003; -.
DR KEGG; mmu:329003; -.
DR UCSC; uc008fuf.2; mouse.
DR CTD; 329003; -.
DR MGI; MGI:2443957; Zfp516.
DR VEuPathDB; HostDB:ENSMUSG00000058881; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160839; -.
DR HOGENOM; CLU_009481_0_0_1; -.
DR InParanoid; Q7TSH3; -.
DR OMA; KLNHTHE; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q7TSH3; -.
DR TreeFam; TF332241; -.
DR BioGRID-ORCS; 329003; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Zfp516; mouse.
DR PRO; PR:Q7TSH3; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q7TSH3; protein.
DR Bgee; ENSMUSG00000058881; Expressed in manus and 222 other tissues.
DR ExpressionAtlas; Q7TSH3; baseline and differential.
DR Genevisible; Q7TSH3; MM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0060612; P:adipose tissue development; IMP:UniProtKB.
DR GO; GO:0050873; P:brown fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IDA:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1157
FT /note="Zinc finger protein 516"
FT /id="PRO_0000047635"
FT ZN_FING 34..56
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 62..84
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 162..185
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 188..211
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 236..258
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 264..286
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 323..345
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 504..526
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 753..776
FT /note="C2H2-type 9; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1092..1114
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..420
FT /note="Mediates promoter DNA-binding and activation of
FT transcription"
FT /evidence="ECO:0000269|PubMed:25578880"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 630
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92618"
FT CROSSLNK 669
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92618"
FT CROSSLNK 1032
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92618"
FT CROSSLNK 1051
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92618"
SQ SEQUENCE 1157 AA; 124788 MW; E14AEDEBF70E5100 CRC64;
MDRSREAEME LRRGPSPPRA GRSHEVDGDK AACHSCCICG KSFPFQSSLS QHMRKHTGEK
PYKCPYCDHR ASQKGNLKIH IRSHRTGTLI QGHEPEAGEA QLGEMRVSEG LDGCASPTKS
TSACNRVLNG AVPMDGSKIL LRSSRKEVEG AASAQEDTEA TVPCSFCKSR FERKKDLELH
VHQAHKPFKC RLCSYVTLRE ESLLSHIERD HITAQVPNGS EACVENGKPE LSPGEFPCEV
CGQAFSQTWF LKAHMKKHRG SFDHGCHICG RRFKEPWFLK NHMKAHGPKA GSKNRPKSEL
DPIATINNVV QEEVIVAGLS LYEVCTKCGN LFTNLDSLNA HNAIHRKVEA SRIRAPAEEG
DSEDPLDTKQ FFLQCLNLTP YVAGDVSPGG QAGRRVAELD PVNSYQAWQL ATRGKVAEPA
EYLKYGTWDE ALAGDVAFDK DKREYILVSQ EKRKREQDAP ATQAPPRKRA SVPGDPMLSG
HLDPRPTSRP NRRASATTGQ GKSSECFECG KIFRTYHQMV LHSRVHRRAR RDRDPEGDRA
ARARCGSLSE GDSASQPSSP GSACAIADSP GLAEEVVDDS GEEAVPEPAS GGQPRHCCSS
GEVTPTALSN GDQNHKLGNN LPEKDISEPK VGSAMPSVSI LENSSRETTK GPEQHRYSLD
LKMPAFHPKQ EVPSTTDRVD FPASMEITSL QHTLDSQAGH SKEKLSDLHK EHCGVGKRAS
APDLVPLDLS MRSSRDEPSG KEACSLQAAL VIHPCPYCTH KTYYPEVLWM HKRIWHRVSC
SSVAPPWTQP SGHKSIRSNL VFLTRSGRTG PPPALGGKEC QPLLLSRFAR TQVPGGAPGS
KGSSSPLGVT TKAASMPKNK ESHSGGPCAL WASGPDGYRQ TRAGHGQEPP SAAVQGPLAK
PKQEGSSRLA PSPGSGSLSR STTPTPSVIT RVGAQPSANS KPVEKLGGPA VGTGFTPPNK
HSAPDSLKAK FSPQPQGQPP LKGEGGSPLP PREPSVKAAQ ELRTLATCAA GSRGEAALQA
PPGAPPTLNS AKQEPAAEGQ EKRLDILSIF KTYIPKDFAT LYQGWGVSSP GPEHRGTSLT
GTPRTQAHQG DFVCVECGKS FHQPSQLRAH LRAHTVVFEC DGPRDSEVHT ASTDAPKQGR
DHTTPGTVPA GPLRKGI
