Z385A_MOUSE
ID Z385A_MOUSE Reviewed; 386 AA.
AC Q8VD12; G3UWA5; Q9QY68;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Zinc finger protein 385A;
DE AltName: Full=Hematopoietic zinc finger protein;
GN Name=Znf385a; Synonyms=Hzf, Zfp385a;
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 [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=10585558; DOI=10.1016/s0925-4773(99)00234-8;
RA Hidaka M., Caruana G., Stanford W.L., Sam M., Correll P.H., Bernstein A.;
RT "Gene trapping of two novel genes, Hzf and Hhl, expressed in hematopoietic
RT cells.";
RL Mech. Dev. 90:3-15(2000).
RN [2]
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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP FUNCTION IN MEGAKARYOCYTE DEVELOPMENT, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=11927637; DOI=10.1084/jem.20011522;
RA Kimura Y., Hart A., Hirashima M., Wang C., Holmyard D., Pittman J.,
RA Pang X.L., Jackson C.W., Bernstein A.;
RT "Zinc finger protein, Hzf, is required for megakaryocyte development and
RT hemostasis.";
RL J. Exp. Med. 195:941-952(2002).
RN [6]
RP FUNCTION IN MRNA LOCALIZATION, RNA-BINDING, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=16286649; DOI=10.1073/pnas.0504684102;
RA Iijima T., Imai T., Kimura Y., Bernstein A., Okano H.J., Yuzaki M.,
RA Okano H.;
RT "Hzf protein regulates dendritic localization and BDNF-induced translation
RT of type 1 inositol 1,4,5-trisphosphate receptor mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17190-17195(2005).
RN [7]
RP FUNCTION IN TP53-DEPENDENT CELL CYCLE ARREST, AND INDUCTION BY DNA DAMAGE.
RX PubMed=16382142; DOI=10.1128/mcb.26.2.502-512.2006;
RA Sugimoto M., Gromley A., Sherr C.J.;
RT "Hzf, a p53-responsive gene, regulates maintenance of the G2 phase
RT checkpoint induced by DNA damage.";
RL Mol. Cell. Biol. 26:502-512(2006).
RN [8]
RP FUNCTION IN TP53-DEPENDENT CELL CYCLE ARREST, INTERACTION WITH TP53, AND
RP INDUCTION BY DNA DAMAGE.
RX PubMed=17719541; DOI=10.1016/j.cell.2007.06.013;
RA Das S., Raj L., Zhao B., Kimura Y., Bernstein A., Aaronson S.A., Lee S.W.;
RT "Hzf Determines cell survival upon genotoxic stress by modulating p53
RT transactivation.";
RL Cell 130:624-637(2007).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=17383763; DOI=10.1016/j.neures.2007.02.013;
RA Iijima T., Ogura H., Takatsuki K., Kawahara S., Wakabayashi K.,
RA Nakayama D., Fujioka M., Kimura Y., Bernstein A., Okano H.J., Kirino Y.,
RA Okano H.;
RT "Impaired motor functions in mice lacking the RNA-binding protein Hzf.";
RL Neurosci. Res. 58:183-189(2007).
RN [10]
RP FUNCTION IN ADIPOGENESIS, RNA-BINDING, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18418387; DOI=10.1038/emboj.2008.76;
RA Kawagishi H., Wakoh T., Uno H., Maruyama M., Moriya A., Morikawa S.,
RA Okano H., Sherr C.J., Takagi M., Sugimoto M.;
RT "Hzf regulates adipogenesis through translational control of C/EBPalpha.";
RL EMBO J. 27:1481-1490(2008).
RN [11]
RP FUNCTION IN MRNA LOCALIZATION, RNA-BINDING, AND INTERACTION WITH ELAVL1.
RX PubMed=21402775; DOI=10.1128/mcb.01424-10;
RA Nakamura H., Kawagishi H., Watanabe A., Sugimoto K., Maruyama M.,
RA Sugimoto M.;
RT "Cooperative role of the RNA-binding proteins Hzf and HuR in p53
RT activation.";
RL Mol. Cell. Biol. 31:1997-2009(2011).
CC -!- FUNCTION: RNA-binding protein that affects the localization and the
CC translation of a subset of mRNA. May play a role in adipogenesis
CC through binding to the 3'-UTR of CEBPA mRNA and regulation of its
CC translation. Targets ITPR1 mRNA to dendrites in Purkinje cells, and may
CC regulate its activity-dependent translation. With ELAVL1, binds the 3'-
CC UTR of p53/TP53 mRNAs to control their nuclear export induced by
CC CDKN2A. Hence, may regulate p53/TP53 expression and mediate in part the
CC CDKN2A anti-proliferative activity. May also bind CCNB1 mRNA.
CC Alternatively, may also regulate p53/TP53 activity through direct
CC protein-protein interaction. Interacts with p53/TP53 and promotes cell-
CC cycle arrest over apoptosis enhancing preferentially the DNA binding
CC and transactivation of p53/TP53 on cell-cycle arrest target genes over
CC proapoptotic target genes. May also regulate the ubiquitination and
CC stability of CDKN1A promoting DNA damage-induced cell cycle arrest.
CC Also plays a role in megakaryocytes differentiation.
CC {ECO:0000269|PubMed:11927637, ECO:0000269|PubMed:16286649,
CC ECO:0000269|PubMed:16382142, ECO:0000269|PubMed:17719541,
CC ECO:0000269|PubMed:18418387, ECO:0000269|PubMed:21402775}.
CC -!- SUBUNIT: Interacts with p53/TP53; the interaction is direct and
CC enhances p53/TP53 transactivation functions on cell-cycle arrest target
CC genes, resulting in growth arrest. Interacts with ELAVL1; the
CC interaction is indirect, mRNA-dependent and may regulate p53/TP53
CC expression. {ECO:0000269|PubMed:17719541, ECO:0000269|PubMed:21402775}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16286649}. Nucleus,
CC nucleolus {ECO:0000250}. Cell projection, dendrite
CC {ECO:0000269|PubMed:16286649}. Note=Detected in dendrites of Purkinje
CC cells and hippocampal neurons.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VD12-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VD12-2; Sequence=VSP_047450;
CC -!- TISSUE SPECIFICITY: Expressed in brain and testis (at protein level).
CC In brain, the expression is located to olfactory bulb, cerebral cortex,
CC hippocampus, satellite cells and Purkinje cells of the cerebellum
CC molecular layer. Detected in bone marrow, white and brown adipose
CC tissue, lung and at lower levels in the thymus.
CC {ECO:0000269|PubMed:10585558, ECO:0000269|PubMed:11927637,
CC ECO:0000269|PubMed:16286649, ECO:0000269|PubMed:18418387}.
CC -!- DEVELOPMENTAL STAGE: At 14.5 dpc, expressed in large polynucleated
CC cells within the liver. Induced during adipogenesis.
CC {ECO:0000269|PubMed:10585558, ECO:0000269|PubMed:18418387}.
CC -!- INDUCTION: By p53/TP53 in response to DNA damage.
CC {ECO:0000269|PubMed:16382142, ECO:0000269|PubMed:17719541}.
CC -!- PTM: Ubiquitinated upon prolonged exposure to genotoxic stress, which
CC leads to proteasomal degradation of ZNF385A and releases p53/TP53 from
CC cell-cycle arrest target gene promoters. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype at birth. Between 2-3 weeks
CC after birth, some lethality is observed, may be due to internal
CC hemorrhaging mainly in brain and gastrointestinal tracts. Surviving
CC mutants are fertile and smaller than their wild-type littermates.
CC Deficiency alters hemostasis which is associated with a block in the
CC formation of alpha-granules in megakaryocytes and abnormal platelet
CC morphology. Mice also exhibit tremor, ataxic gate, tilted head, severe
CC impairments in motor coordination and motor learning related to
CC cerebellar functions. Mice show functional deregulation of adipose
CC tissues, although the total fat mass is not affected. They express
CC lower levels of C/EBP alpha in adipose tissue, have impaired glucose
CC tolerance with high plasma insulin levels and plasma adiponectin levels
CC are significantly lower. Upon genotoxic stress, skin and prostate show
CC increased apoptosis. {ECO:0000269|PubMed:11927637,
CC ECO:0000269|PubMed:17383763, ECO:0000269|PubMed:18418387}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24093.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF118566; AAF24093.1; ALT_FRAME; mRNA.
DR EMBL; AC164069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466550; EDL03923.1; -; Genomic_DNA.
DR EMBL; BC017644; AAH17644.1; -; mRNA.
DR CCDS; CCDS49743.1; -. [Q8VD12-1]
DR CCDS; CCDS88860.1; -. [Q8VD12-2]
DR RefSeq; NP_038894.2; NM_013866.2. [Q8VD12-1]
DR RefSeq; XP_006521116.1; XM_006521053.3. [Q8VD12-2]
DR RefSeq; XP_006521120.1; XM_006521057.3.
DR RefSeq; XP_011243958.1; XM_011245656.2. [Q8VD12-2]
DR AlphaFoldDB; Q8VD12; -.
DR BioGRID; 205894; 1.
DR STRING; 10090.ENSMUSP00000130176; -.
DR iPTMnet; Q8VD12; -.
DR PhosphoSitePlus; Q8VD12; -.
DR EPD; Q8VD12; -.
DR MaxQB; Q8VD12; -.
DR PaxDb; Q8VD12; -.
DR PeptideAtlas; Q8VD12; -.
DR PRIDE; Q8VD12; -.
DR ProteomicsDB; 275333; -. [Q8VD12-1]
DR ProteomicsDB; 275334; -. [Q8VD12-2]
DR Antibodypedia; 15350; 110 antibodies from 20 providers.
DR Ensembl; ENSMUST00000168828; ENSMUSP00000130176; ENSMUSG00000000552. [Q8VD12-1]
DR Ensembl; ENSMUST00000229373; ENSMUSP00000155498; ENSMUSG00000000552. [Q8VD12-2]
DR GeneID; 29813; -.
DR KEGG; mmu:29813; -.
DR UCSC; uc007xxz.1; mouse. [Q8VD12-1]
DR CTD; 29813; -.
DR MGI; MGI:1352495; Zfp385a.
DR VEuPathDB; HostDB:ENSMUSG00000000552; -.
DR eggNOG; ENOG502QWH6; Eukaryota.
DR GeneTree; ENSGT00940000160876; -.
DR HOGENOM; CLU_027876_1_0_1; -.
DR OMA; SEARCIP; -.
DR OrthoDB; 899600at2759; -.
DR PhylomeDB; Q8VD12; -.
DR TreeFam; TF326622; -.
DR Reactome; R-MMU-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR Reactome; R-MMU-69895; Transcriptional activation of cell cycle inhibitor p21.
DR BioGRID-ORCS; 29813; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Zfp385a; mouse.
DR PRO; PR:Q8VD12; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8VD12; protein.
DR Bgee; ENSMUSG00000000552; Expressed in retinal neural layer and 229 other tissues.
DR ExpressionAtlas; Q8VD12; baseline and differential.
DR Genevisible; Q8VD12; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:MGI.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0007599; P:hemostasis; IMP:MGI.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:MGI.
DR GO; GO:0007611; P:learning or memory; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0035855; P:megakaryocyte development; IMP:MGI.
DR GO; GO:0010609; P:mRNA localization resulting in post-transcriptional regulation of gene expression; IMP:MGI.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0070889; P:platelet alpha granule organization; IMP:MGI.
DR GO; GO:0030220; P:platelet formation; IMP:MGI.
DR GO; GO:1902164; P:positive regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; ISS:UniProtKB.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:MGI.
DR GO; GO:2000765; P:regulation of cytoplasmic translation; IMP:MGI.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SMART; SM00451; ZnF_U1; 3.
DR SUPFAM; SSF57667; SSF57667; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell projection; Cytoplasm; DNA damage;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Transcription; Transcription regulation;
KW Translation regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..386
FT /note="Zinc finger protein 385A"
FT /id="PRO_0000422970"
FT ZN_FING 74..98
FT /note="Matrin-type 1"
FT ZN_FING 201..225
FT /note="Matrin-type 2"
FT ZN_FING 261..285
FT /note="Matrin-type 3"
FT REGION 88..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..351
FT /note="Necessary for binding to ITPR1, CEBPA and p53/TP53
FT mRNAs"
FT REGION 279..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PM9"
FT MOD_RES 248
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96PM9"
FT VAR_SEQ 1..21
FT /note="MILGSLSRAGPLPLLRQPPIM -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047450"
FT CONFLICT 232
FT /note="R -> G (in Ref. 1; AAF24093)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="P -> A (in Ref. 1; AAF24093)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="L -> V (in Ref. 1; AAF24093)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="Missing (in Ref. 1; AAF24093)"
FT /evidence="ECO:0000305"
FT CONFLICT 248..249
FT /note="TP -> NS (in Ref. 1; AAF24093)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="R -> G (in Ref. 1; AAF24093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 386 AA; 40447 MW; 5F435678A565BA21 CRC64;
MILGSLSRAG PLPLLRQPPI MQPPMDLKQI LPFPLEPAPT LGLFSNYSTM DPVQKAVLSH
TFGGPLLKTK RPVISCNVCQ IRFNSQSQAE AHYKGNRHAR RVKGIEAAKT RGREPSVRES
GDPAPAGSIP PSGDGVAPRP VSMENGLGPA PGSPEKQPGS PSPPSVPESG QGVTKGEGGT
SVPASLPGGS KEEEEKAKRL LYCALCKVAV NSLSQLEAHN KGTKHKTILE ARSGLGPIKA
YPRLGPPTPG EPEAPAQDRT FHCEICNVKV NSEVQLKQHI SSRRHRDGVA GKPNPLLSRH
KKPRGAAELA GTLTFSKELP KSLAGGLLPS PLAVAAVMAA AAGSPLSLRP APAAPLLQGP
PITHPLLHPA PGPIRTAHGP ILFSPY
