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 27-MAR-2024, entry version 92.
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 AGR; Xenbase:XB-GENE-967548; -.
DR CTD; 380471; -.
DR Xenbase; XB-GENE-967548; znf346.S.
DR OrthoDB; 3094294at2759; -.
DR EvolutionaryTrace; Q8AVN9; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 380471; Expressed in blastula and 19 other cell types or 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 Gene3D; 3.30.160.60; Classic Zinc Finger; 7.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR46144:SF5; ZINC FINGER PROTEIN 346; 1.
DR PANTHER; PTHR46144; ZINC FINGER PROTEIN 385B-LIKE; 1.
DR Pfam; PF12874; zf-met; 7.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SMART; SM00451; ZnF_U1; 7.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 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
//
