ID   DNLZ_DANRE              Reviewed;         183 AA.
AC   A1L1P7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=DNL-type zinc finger protein;
DE   AltName: Full=mtHsp70-escort protein;
DE   Flags: Precursor;
GN   Name=dnlz; ORFNames=zgc:158228;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-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}.
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DR   EMBL; BC129164; AAI29165.1; -; mRNA.
DR   RefSeq; NP_001074117.1; NM_001080648.1.
DR   AlphaFoldDB; A1L1P7; -.
DR   SMR; A1L1P7; -.
DR   STRING; 7955.ENSDARP00000090162; -.
DR   PaxDb; A1L1P7; -.
DR   GeneID; 791166; -.
DR   KEGG; dre:791166; -.
DR   CTD; 728489; -.
DR   ZFIN; ZDB-GENE-070112-1482; dnlz.
DR   eggNOG; KOG3277; Eukaryota.
DR   InParanoid; A1L1P7; -.
DR   OrthoDB; 1626191at2759; -.
DR   PhylomeDB; A1L1P7; -.
DR   PRO; PR:A1L1P7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
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..62
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           63..183
FT                   /note="DNL-type zinc finger protein"
FT                   /id="PRO_0000317169"
FT   ZN_FING         76..173
FT                   /note="DNL-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT   REGION          160..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT   BINDING         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
SQ   SEQUENCE   183 AA;  20428 MW;  4BE8D3154B41705B CRC64;
     MNSRLCYLLF RPRLLRSRGA GVLSVPETQR VTLARVRHEE SNSAFTNSTL RSDVGHDTGL
     GLSFCRSFST EAIGQLQSTH YHLVYTCKVC STRSMKKISK LAYHKGVVIV TCPGCKNHHV
     IADNLKWFSD LEGKRNIEEI LAAKGESVRR VEGSEALEIV NEESRNNPDE QKPAHLSDGS
     DKT