ID   ZN346_DANRE             Reviewed;         301 AA.
AC   A2RV29;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Zinc finger protein 346 {ECO:0000312|ZFIN:ZDB-GENE-070209-152};
DE   AltName: Full=Just another zinc finger protein {ECO:0000250|UniProtKB:Q9R0B7};
DE            Short=Protein jaz;
GN   Name=znf346 {ECO:0000312|ZFIN:ZDB-GENE-070209-152}; ORFNames=zgc:158750;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000312|EMBL:AAI33151.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAI33151.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds preferentially to dsRNA, but also to RNA-DNA hybrids.
CC       {ECO:0000250|UniProtKB:Q8AVN9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8AVN9}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q8AVN9}. Note=Primarily nuclear.
CC       {ECO:0000250|UniProtKB:Q8AVN9}.
CC   -!- DOMAIN: The zinc-finger domains are required for binding to dsRNA, and
CC       also for nuclear localization. {ECO:0000250|UniProtKB:Q9R0B7}.
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DR   EMBL; BC133150; AAI33151.1; -; mRNA.
DR   RefSeq; NP_001075218.1; NM_001081749.1.
DR   AlphaFoldDB; A2RV29; -.
DR   SMR; A2RV29; -.
DR   STRING; 7955.ENSDARP00000080221; -.
DR   PaxDb; A2RV29; -.
DR   PeptideAtlas; A2RV29; -.
DR   GeneID; 560756; -.
DR   KEGG; dre:560756; -.
DR   CTD; 23567; -.
DR   ZFIN; ZDB-GENE-070209-152; znf346.
DR   eggNOG; ENOG502RVNK; Eukaryota.
DR   InParanoid; A2RV29; -.
DR   OrthoDB; 1565630at2759; -.
DR   PhylomeDB; A2RV29; -.
DR   PRO; PR:A2RV29; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR   InterPro; IPR022755; Znf_C2H2_jaz.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF12171; zf-C2H2_jaz; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SMART; SM00451; ZnF_U1; 4.
DR   SUPFAM; SSF57667; SSF57667; 4.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat; RNA-binding;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..301
FT                   /note="Zinc finger protein 346"
FT                   /id="PRO_0000348933"
FT   ZN_FING         55..85
FT                   /note="Matrin-type 1"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         117..141
FT                   /note="Matrin-type 2"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         180..210
FT                   /note="Matrin-type 3"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         230..257
FT                   /note="Matrin-type 4"
FT                   /evidence="ECO:0000255"
FT   REGION          151..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8AVN9"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8AVN9"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8AVN9"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8AVN9"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8AVN9"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8AVN9"
FT   BINDING         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8AVN9"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8AVN9"
SQ   SEQUENCE   301 AA;  33695 MW;  3DF2B5205D12D227 CRC64;
     MERLVQRMYC LGMRDPPPAN IMAQQEPNGD FPYLPSGAAE VNRMIKENSD LFSDSQCKVC
     SAVLISESQK LAHYQSKKHA SKVRRYMSIH GSEEPIAKRF KPSGDDQSNV DEKDKYKACS
     VCNMTFSSPV VAQSHYQGKV HSKNLRMQSI GSQTPALPQP EAQAKKDDGM QGPAEQDPNR
     FCSICQASFN NPLMAQQHYS GKKHKKHMNK QKLMETFGPS TAPASTVKGY PCTVCNIELN
     SVEQYQAHIS GSKHKNHAKP KKGPNAFAPP PDNYQPDYQY PTNEDCLEDP AEWDSFNVAY
     E