ZN346_MOUSE
ID ZN346_MOUSE Reviewed; 294 AA.
AC Q9R0B7;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Zinc finger protein 346;
DE AltName: Full=Just another zinc finger protein;
GN Name=Znf346; Synonyms=Jaz, Zfp346;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF HIS-91; HIS-152; HIS-203 AND HIS-257.
RX PubMed=10488071; DOI=10.1074/jbc.274.39.27399;
RA Yang M., May W.S., Ito T.;
RT "JAZ requires the double-stranded RNA-binding zinc finger motifs for
RT nuclear localization.";
RL J. Biol. Chem. 274:27399-27406(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C3H/He; TISSUE=Osteoblast;
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).
CC -!- FUNCTION: Binds with low affinity to dsDNA and ssRNA, and with high
CC affinity to dsRNA, with no detectable sequence specificity (By
CC similarity) (PubMed:10488071). May bind to specific miRNA hairpins (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9UL40,
CC ECO:0000269|PubMed:10488071}.
CC -!- SUBUNIT: Forms a heteromeric complex with XPO5 and ILF3. Found in a
CC nuclear export complex with XPO5, RAN, ILF3, ZNF346 and double-stranded
CC RNA. Interacts with XPO5. Interacts with ILF3 in an RNA-independent
CC manner (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Note=Nuclear at steady state, primarily in the
CC nucleolus. Shuttles between the nucleus and cytoplasm when associated
CC with XPO5 (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including heart,
CC brain, spleen, lung, liver, muscle, kidney and testis. Exogenous
CC expression induced apoptosis. {ECO:0000269|PubMed:10488071}.
CC -!- DOMAIN: The zinc-finger domains are required for binding to dsRNA, and
CC also for nuclear localization.
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DR EMBL; AF083339; AAD52017.1; -; mRNA.
DR EMBL; BC055075; AAH55075.1; -; mRNA.
DR CCDS; CCDS26539.1; -.
DR RefSeq; NP_036147.1; NM_012017.2.
DR AlphaFoldDB; Q9R0B7; -.
DR SMR; Q9R0B7; -.
DR BioGRID; 205063; 2.
DR STRING; 10090.ENSMUSP00000021937; -.
DR iPTMnet; Q9R0B7; -.
DR PhosphoSitePlus; Q9R0B7; -.
DR EPD; Q9R0B7; -.
DR MaxQB; Q9R0B7; -.
DR PaxDb; Q9R0B7; -.
DR PRIDE; Q9R0B7; -.
DR Antibodypedia; 17273; 313 antibodies from 32 providers.
DR DNASU; 26919; -.
DR Ensembl; ENSMUST00000021937; ENSMUSP00000021937; ENSMUSG00000021481.
DR GeneID; 26919; -.
DR KEGG; mmu:26919; -.
DR UCSC; uc007qpy.1; mouse.
DR CTD; 26919; -.
DR MGI; MGI:1349417; Zfp346.
DR VEuPathDB; HostDB:ENSMUSG00000021481; -.
DR eggNOG; ENOG502RVNK; Eukaryota.
DR GeneTree; ENSGT00940000159101; -.
DR InParanoid; Q9R0B7; -.
DR OrthoDB; 1565630at2759; -.
DR PhylomeDB; Q9R0B7; -.
DR TreeFam; TF350019; -.
DR BioGRID-ORCS; 26919; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Zfp346; mouse.
DR PRO; PR:Q9R0B7; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9R0B7; protein.
DR Bgee; ENSMUSG00000021481; Expressed in embryonic post-anal tail and 261 other tissues.
DR ExpressionAtlas; Q9R0B7; baseline and differential.
DR Genevisible; Q9R0B7; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043065; P:positive regulation of apoptotic process; 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; 4.
DR SMART; SM00451; ZnF_U1; 4.
DR SUPFAM; SSF57667; SSF57667; 4.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; RNA-binding; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..294
FT /note="Zinc finger protein 346"
FT /id="PRO_0000191810"
FT ZN_FING 70..104
FT /note="Matrin-type 1"
FT ZN_FING 131..165
FT /note="Matrin-type 2"
FT ZN_FING 182..216
FT /note="Matrin-type 3"
FT ZN_FING 236..270
FT /note="Matrin-type 4"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL40"
FT CROSSLNK 114
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UL40"
FT CROSSLNK 170
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UL40"
FT MUTAGEN 91
FT /note="H->A: No loss of dsRNA binding capacity. Binding
FT capacity was reduced 40-60%; when associated with A-203.
FT Binding capacity was reduced to 5-10%; when associated with
FT A-152 and A-203. Loss of binding capacity; when associated
FT with A-152; A-203 and A-257."
FT /evidence="ECO:0000269|PubMed:10488071"
FT MUTAGEN 152
FT /note="H->A: No loss of dsRNA binding capacity. Loss of 40-
FT 60% dsRNA binding; when associated with A-203. Binding
FT capacity was reduced to 5-10%; when associated with A-91
FT and A-203. Loss of binding capacity; when associated with
FT A-91; A-203 and A-257."
FT /evidence="ECO:0000269|PubMed:10488071"
FT MUTAGEN 203
FT /note="H->A: No loss of dsRNA binding capacity. Binding
FT capacity was reduced 40-60%; when associated with A-91.
FT Binding capacity was reduced to 5-10%; when associated with
FT A-91 and A-152. Loss of binding capacity; when associated
FT with A-91; A-152 and A-257."
FT /evidence="ECO:0000269|PubMed:10488071"
FT MUTAGEN 257
FT /note="H->A: No loss of dsRNA binding capacity. Loss of 5-
FT 10 % dsRNA binding capacity; when associated with A-152 and
FT A-203. Loss of binding capacity; when associated with A-91;
FT A-152 and A-203."
FT /evidence="ECO:0000269|PubMed:10488071"
SQ SEQUENCE 294 AA; 32698 MW; 6BD916262EDBA71E CRC64;
MECPAPDATD AADPGEAGPY KGSEEPEGRE PDGVRFDRER ARRLWEAVSG AQPAGREEVE
HMIQKNQCLF TSTQCKVCCA MLISESQKLA HYQSKKHANK VKRYLAIHGM ETIKGDVKRL
DSDQKSSRSK DKNHCCPICN MTFSSPAVAQ SHYLGKTHAK SLKLKQQSTK GAALQQNREM
LDPDKFCSLC HSTFNDPAMA QQHYMGKRHR KQETKLKLMA HYGRLADPAV SDLPAGKGYP
CKTCKIVLNS IEQYQAHVSG FKHKNQSPKT LVTLGSQTPV QTQPTPKDSS TVQD
