ID   ZN346_XENLA             Reviewed;         524 AA.
AC   Q8AVN9; O42147;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Zinc finger protein 346 {ECO:0000250|UniProtKB:Q9R0B7};
DE   AltName: Full=Double-stranded RNA-binding protein ZFa;
DE            Short=DsRBP-ZFa {ECO:0000312|EMBL:AAC60260.1};
DE            Short=ZFa {ECO:0000303|PubMed:16051273};
DE   AltName: Full=Just another zinc finger protein {ECO:0000250|UniProtKB:Q9R0B7};
DE            Short=Protein jaz;
GN   Name=znf346 {ECO:0000250|UniProtKB:Q9R0B7};
GN   Synonyms=jaz {ECO:0000312|EMBL:AAH41713.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAC60260.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Head {ECO:0000269|PubMed:9268652};
RX   PubMed=9268652; DOI=10.1006/jmbi.1997.1177;
RA   Finerty P.J. Jr., Bass B.L.;
RT   "A Xenopus zinc finger protein that specifically binds dsRNA and RNA-DNA
RT   hybrids.";
RL   J. Mol. Biol. 271:195-208(1997).
RN   [2] {ECO:0000312|EMBL:AAH41713.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula {ECO:0000312|EMBL:AAH41713.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   STRUCTURE BY NMR OF 2-128 IN COMPLEX WITH ZINC IONS.
RX   PubMed=16051273; DOI=10.1016/j.jmb.2005.06.032;
RA   Moeller H.M., Martinez-Yamout M.A., Dyson H.J., Wright P.E.;
RT   "Solution structure of the N-terminal zinc fingers of the Xenopus laevis
RT   double-stranded RNA-binding protein ZFa.";
RL   J. Mol. Biol. 351:718-730(2005).
CC   -!- FUNCTION: Binds preferentially to dsRNA, but also to RNA-DNA hybrids.
CC       {ECO:0000269|PubMed:9268652}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9268652}. Cytoplasm
CC       {ECO:0000269|PubMed:9268652}. Note=Primarily nuclear.
CC       {ECO:0000269|PubMed:9268652}.
CC   -!- DOMAIN: The zinc-finger domains are required for binding to dsRNA, and
CC       also for nuclear localization. {ECO:0000250|UniProtKB:Q9R0B7}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF005083; AAC60260.1; -; mRNA.
DR   EMBL; BC041713; AAH41713.1; -; mRNA.
DR   RefSeq; NP_001080778.1; NM_001087309.1.
DR   PDB; 1ZU1; NMR; -; A=2-128.
DR   PDBsum; 1ZU1; -.
DR   AlphaFoldDB; Q8AVN9; -.
DR   SMR; Q8AVN9; -.
DR   DNASU; 380471; -.
DR   GeneID; 380471; -.
DR   KEGG; xla:380471; -.
DR   CTD; 380471; -.
DR   Xenbase; XB-GENE-967548; znf346.S.
DR   OrthoDB; 1565630at2759; -.
DR   EvolutionaryTrace; Q8AVN9; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 380471; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   DisProt; DP01733; -.
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; 7.
DR   SMART; SM00451; ZnF_U1; 7.
DR   SUPFAM; SSF57667; SSF57667; 7.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; RNA-binding; Zinc; Zinc-finger.
FT   CHAIN           1..524
FT                   /note="Zinc finger protein 346"
FT                   /id="PRO_0000348934"
FT   ZN_FING         34..64
FT                   /note="Matrin-type 1"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         92..126
FT                   /note="Matrin-type 2"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         162..192
FT                   /note="Matrin-type 3"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         226..260
FT                   /note="Matrin-type 4"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         286..316
FT                   /note="Matrin-type 5"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         343..373
FT                   /note="Matrin-type 6"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         400..430
FT                   /note="Matrin-type 7"
FT                   /evidence="ECO:0000255"
FT   REGION          453..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:16051273"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:16051273"
FT   BINDING         52
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:16051273"
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:16051273"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:16051273"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:16051273"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:16051273"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:16051273"
FT   CONFLICT        397
FT                   /note="G -> V (in Ref. 1; AAC60260)"
FT                   /evidence="ECO:0000305"
FT   HELIX           17..26
FT                   /evidence="ECO:0007829|PDB:1ZU1"
FT   TURN            27..30
FT                   /evidence="ECO:0007829|PDB:1ZU1"
FT   STRAND          33..36
FT                   /evidence="ECO:0007829|PDB:1ZU1"
FT   TURN            37..40
FT                   /evidence="ECO:0007829|PDB:1ZU1"
FT   HELIX           46..54
FT                   /evidence="ECO:0007829|PDB:1ZU1"
FT   HELIX           56..68
FT                   /evidence="ECO:0007829|PDB:1ZU1"
FT   TURN            93..95
FT                   /evidence="ECO:0007829|PDB:1ZU1"
FT   TURN            98..101
FT                   /evidence="ECO:0007829|PDB:1ZU1"
FT   HELIX           107..114
FT                   /evidence="ECO:0007829|PDB:1ZU1"
FT   HELIX           117..127
FT                   /evidence="ECO:0007829|PDB:1ZU1"
SQ   SEQUENCE   524 AA;  55546 MW;  E55736038AC13D5C CRC64;
     MADEFGNGDA LDLPVGKDAV NSLIRENSHI FSDTQCKVCS AVLISESQKL AHYQSRKHAN
     KVRRYMAINQ GEDSVPAKKF KAAPAEISDG EDRSKCCPVC NMTFSSPVVA ESHYIGKTHI
     KNLRLREQGG VKEGMVNQAK KTRTPTVATK SDNKMDHSDR AKFCKLCHST FNNPLMAEQH
     YAGKKHKKQE TKTQIMTIYT SSGQTPAQAP IPLNLNSPMP GSGSAGKGFS CDKCNIVLNS
     IEQYQAHVSG AKHKNQLMSM TPLSEEGHQA VVAPSAIASG SAGKGFSCDT CNIVLNSIEQ
     YQAHISGAKH KNHLKSMTPL SEEGHTAAVA PSAFASGSAG KGFSCDTCNI VLNSIEQYQA
     HISGAKHKNH LMSMTPLSEE GHTAAVAPSA FASGSAGKGF SCDTCNIVLN SIEQYQAHVS
     GAKHKNQLMS MTPSSEEGLP SAVGPSAFAS PLSAGGALSS GGPSGRGFCP SGDLTPKGPS
     SFGSLPPLGS LLPPLYPPAH SSQPYVHDDT MSPDGYNYFN EDFE