ID   ZBED3_HUMAN             Reviewed;         234 AA.
AC   Q96IU2;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Zinc finger BED domain-containing protein 3;
DE   AltName: Full=Axin-interacting protein;
GN   Name=ZBED3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [4]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY HYPERGLYCEMIA
RP   AND HYPERINSULINEMIA.
RX   PubMed=24283382; DOI=10.1111/joim.12170;
RA   Jia Y., Yuan L., Hu W., Luo Y., Suo L., Yang M., Chen S., Wang Y., Liu H.,
RA   Yang G., Li L.;
RT   "Zinc-finger BED domain-containing 3 (Zbed3) is a novel secreted protein
RT   associated with insulin resistance in humans.";
RL   J. Intern. Med. 275:522-533(2014).
CC   -!- FUNCTION: Acts as a positive regulator in the activation of the
CC       canonical Wnt/beta-catenin signaling pathway by stabilizing cytoplasmic
CC       beta-catenin (By similarity). Involved in transcription activation of
CC       Wnt target gene expression (By similarity). Plays a role in symmetric
CC       division of blastomeres in the early stages of embryogenesis via
CC       regulation of mitotic spindle central positioning and organization of
CC       the F-actin filament network (By similarity). Plays a role in
CC       regulating the distribution of cellular organelles, via modulation of
CC       cytoskeletal dynamics and cytoplasmic lattice formation (By
CC       similarity). {ECO:0000250|UniProtKB:Q9D0L1}.
CC   -!- SUBUNIT: Associates with the subcortical maternal complex (SCMC)
CC       composed of at least NLRP5, KHDC3L, OOEP, and TLE6 via interaction with
CC       NLRP5 and TLE6 (By similarity). Interacts with AXIN1; the interaction
CC       is direct, enhanced by protein kinase GSK3B and casein kinase CSNK1E
CC       activities and decreases GSK3B-induced beta-catenin serine and
CC       threonine phosphorylations (By similarity).
CC       {ECO:0000250|UniProtKB:Q9D0L1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9D0L1}.
CC       Membrane {ECO:0000250|UniProtKB:Q9D0L1}. Secreted
CC       {ECO:0000269|PubMed:24283382}.
CC   -!- TISSUE SPECIFICITY: Secreted in blood plasma, and expressed in skeletal
CC       muscle and adipose tissue (at protein level).
CC       {ECO:0000269|PubMed:24283382}.
CC   -!- INDUCTION: Induced in blood plasma by hyperglycemia (PubMed:24283382).
CC       Decreased in blood plasma by hyperinsulinemia (PubMed:24283382).
CC       {ECO:0000269|PubMed:24283382}.
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DR   EMBL; AC008581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC007239; AAH07239.1; -; mRNA.
DR   CCDS; CCDS4036.1; -.
DR   RefSeq; NP_001316493.1; NM_001329564.1.
DR   RefSeq; NP_115743.1; NM_032367.3.
DR   AlphaFoldDB; Q96IU2; -.
DR   SMR; Q96IU2; -.
DR   BioGRID; 124051; 10.
DR   IntAct; Q96IU2; 3.
DR   STRING; 9606.ENSP00000255198; -.
DR   iPTMnet; Q96IU2; -.
DR   PhosphoSitePlus; Q96IU2; -.
DR   BioMuta; ZBED3; -.
DR   DMDM; 34925646; -.
DR   jPOST; Q96IU2; -.
DR   MassIVE; Q96IU2; -.
DR   MaxQB; Q96IU2; -.
DR   PaxDb; 9606-ENSP00000255198; -.
DR   PeptideAtlas; Q96IU2; -.
DR   ProteomicsDB; 76853; -.
DR   Pumba; Q96IU2; -.
DR   Antibodypedia; 24479; 103 antibodies from 24 providers.
DR   DNASU; 84327; -.
DR   Ensembl; ENST00000255198.3; ENSP00000255198.2; ENSG00000132846.6.
DR   GeneID; 84327; -.
DR   KEGG; hsa:84327; -.
DR   MANE-Select; ENST00000255198.3; ENSP00000255198.2; NM_032367.4; NP_115743.1.
DR   UCSC; uc003kev.2; human.
DR   AGR; HGNC:20711; -.
DR   CTD; 84327; -.
DR   DisGeNET; 84327; -.
DR   GeneCards; ZBED3; -.
DR   HGNC; HGNC:20711; ZBED3.
DR   HPA; ENSG00000132846; Low tissue specificity.
DR   MIM; 615250; gene.
DR   neXtProt; NX_Q96IU2; -.
DR   OpenTargets; ENSG00000132846; -.
DR   PharmGKB; PA134974972; -.
DR   VEuPathDB; HostDB:ENSG00000132846; -.
DR   eggNOG; ENOG502SQ4N; Eukaryota.
DR   GeneTree; ENSGT00940000164103; -.
DR   HOGENOM; CLU_112726_0_0_1; -.
DR   InParanoid; Q96IU2; -.
DR   OMA; RDSCVIT; -.
DR   OrthoDB; 4613048at2759; -.
DR   PhylomeDB; Q96IU2; -.
DR   TreeFam; TF338048; -.
DR   PathwayCommons; Q96IU2; -.
DR   SignaLink; Q96IU2; -.
DR   BioGRID-ORCS; 84327; 15 hits in 1163 CRISPR screens.
DR   ChiTaRS; ZBED3; human.
DR   GenomeRNAi; 84327; -.
DR   Pharos; Q96IU2; Tbio.
DR   PRO; PR:Q96IU2; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q96IU2; Protein.
DR   Bgee; ENSG00000132846; Expressed in kidney epithelium and 159 other cell types or tissues.
DR   ExpressionAtlas; Q96IU2; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR   GO; GO:0051643; P:endoplasmic reticulum localization; ISS:UniProtKB.
DR   GO; GO:0051293; P:establishment of spindle localization; ISS:UniProtKB.
DR   GO; GO:0051646; P:mitochondrion localization; ISS:UniProtKB.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0040019; P:positive regulation of embryonic development; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0009749; P:response to glucose; IDA:UniProtKB.
DR   GO; GO:0032868; P:response to insulin; IDA:UniProtKB.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR043471; ZBED2/3.
DR   InterPro; IPR003656; Znf_BED.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   PANTHER; PTHR35827; ZINC FINGER BED DOMAIN-CONTAINING PROTEIN 3; 1.
DR   PANTHER; PTHR35827:SF2; ZINC FINGER BED DOMAIN-CONTAINING PROTEIN 3; 1.
DR   Pfam; PF02892; zf-BED; 1.
DR   SMART; SM00614; ZnF_BED; 1.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR   PROSITE; PS50808; ZF_BED; 1.
DR   Genevisible; Q96IU2; HS.
PE   1: Evidence at protein level;
KW   Cytoplasm; Membrane; Metal-binding; Reference proteome; Secreted;
KW   Wnt signaling pathway; Zinc; Zinc-finger.
FT   CHAIN           1..234
FT                   /note="Zinc finger BED domain-containing protein 3"
FT                   /id="PRO_0000066562"
FT   ZN_FING         43..104
FT                   /note="BED-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT   REGION          19..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..124
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
SQ   SEQUENCE   234 AA;  25132 MW;  3E615F16B68EE3B2 CRC64;
     MRSGEPACTM DQARGLDDAA ARGGQCPGLG PAPTPTPPGR LGAPYSEAWG YFHLAPGRPG
     HPSGHWATCR LCGEQVGRGP GFHAGTSALW RHLRSAHRRE LESSGAGSSP PAAPCPPPPG
     PAAAPEGDWA RLLEQMGALA VRGSRREREL ERRELAVEQG ERALERRRRA LQEEERAAAQ
     ARRELQAERE ALQARLRDVS RREGALGWAP AAPPPLKDDP EGDRDGCVIT KVLL
//