ID   DNLZ_XENLA              Reviewed;         188 AA.
AC   Q0IH40;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=DNL-type zinc finger protein;
DE   AltName: Full=mtHsp70-escort protein;
DE   Flags: Precursor;
GN   Name=dnlz;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May function as a co-chaperone towards HSPA9/mortalin which,
CC       by itself, is prone to self-aggregation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
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; BC123327; AAI23328.1; -; mRNA.
DR   RefSeq; NP_001090392.1; NM_001096923.1.
DR   AlphaFoldDB; Q0IH40; -.
DR   SMR; Q0IH40; -.
DR   DNASU; 779303; -.
DR   GeneID; 779303; -.
DR   KEGG; xla:779303; -.
DR   CTD; 779303; -.
DR   Xenbase; XB-GENE-940252; dnlz.S.
DR   OMA; VWERQVP; -.
DR   OrthoDB; 1626191at2759; -.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 779303; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR024158; Mt_import_TIM15.
DR   InterPro; IPR007853; Znf_DNL-typ.
DR   PANTHER; PTHR20922; PTHR20922; 1.
DR   Pfam; PF05180; zf-DNL; 1.
DR   PROSITE; PS51501; ZF_DNL; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Metal-binding; Mitochondrion; Reference proteome;
KW   Transit peptide; Zinc; Zinc-finger.
FT   TRANSIT         1..68
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           69..188
FT                   /note="DNL-type zinc finger protein"
FT                   /id="PRO_0000317168"
FT   ZN_FING         77..174
FT                   /note="DNL-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT   REGION          169..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
SQ   SEQUENCE   188 AA;  20286 MW;  86B877C05A899A60 CRC64;
     MLFQSCGLLS ALGRIGSRSP VTRGILARAA VVWARDVDGN WGAPTVSRLV TGHLHKCVRP
     PWTVPLAGRL YCTLPAAPSS HYRLIYTCKV CATRSSKTIS KVAYHKGVVI VRCPGCENHH
     IIADNLGWFS DLEGRRNIEE ILAAKGEQVQ RLVGDDAVEI LLRNAGESAT QDGDKTGEAE
     SAGNKLLS