ID   ZN346_PONAB             Reviewed;         310 AA.
AC   Q5R4W8;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Zinc finger protein 346;
GN   Name=ZNF346;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds with low affinity to dsDNA and ssRNA, and with high
CC       affinity to dsRNA, with no detectable sequence specificity.
CC       {ECO:0000250}.
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   -!- DOMAIN: The zinc-finger domains are required for binding to dsRNA, and
CC       also for nuclear localization. {ECO:0000250}.
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DR   EMBL; CR861122; CAH93198.1; -; mRNA.
DR   RefSeq; NP_001126881.1; NM_001133409.1.
DR   AlphaFoldDB; Q5R4W8; -.
DR   BMRB; Q5R4W8; -.
DR   SMR; Q5R4W8; -.
DR   GeneID; 100173894; -.
DR   KEGG; pon:100173894; -.
DR   CTD; 23567; -.
DR   InParanoid; Q5R4W8; -.
DR   OrthoDB; 1565630at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; 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; 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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Isopeptide bond; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; RNA-binding; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..310
FT                   /note="Zinc finger protein 346"
FT                   /id="PRO_0000191811"
FT   ZN_FING         70..104
FT                   /note="Matrin-type 1"
FT   ZN_FING         131..165
FT                   /note="Matrin-type 2"
FT   ZN_FING         198..232
FT                   /note="Matrin-type 3"
FT   ZN_FING         252..286
FT                   /note="Matrin-type 4"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..310
FT                   /note="Disordered"
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"
SQ   SEQUENCE   310 AA;  34629 MW;  54186F39707397C3 CRC64;
     MEYPAPAAVQ AADGGGAGPY NSSELLEGQE PDGVRFDRER ARRLWEAVSG AQPVGREEVE
     HMIQKNQCLF TNTQCKVCCA LLISESQKLA HYQSKKHANK VKRYLAIHGM ETLKGETKKL
     DSDQKSSRSK DKNQCCPICN MTFSSPVVAQ SHYLGKTHAK NLKLKQQSTK VEALSKRLTN
     PFLVASTLAL HQNREMIDPD KFCSLCHATF NDPVMAQQHY VGKKHRKQET KLKLMARYGR
     LADPAVTDFP AGKGYPCKTC KIVLNSIEQY QAHVSGFKHK NQSPKTVASS LGQIPMQRQP
     IQKDSTTLED