DNLZ_HUMAN
ID DNLZ_HUMAN Reviewed; 178 AA.
AC Q5SXM8; B2RUX5; B9EJE1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=DNL-type zinc finger protein;
DE AltName: Full=Hsp70-escort protein 1;
DE Short=HEP1;
DE AltName: Full=mtHsp70-escort protein;
DE Flags: Precursor;
GN Name=DNLZ; Synonyms=C9orf151;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=23462535; DOI=10.1016/j.ijbiomac.2013.02.009;
RA Dores-Silva P.R., Minari K., Ramos C.H., Barbosa L.R., Borges J.C.;
RT "Structural and stability studies of the human mtHsp70-escort protein 1: An
RT essential mortalin co-chaperone.";
RL Int. J. Biol. Macromol. 56:140-148(2013).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May function as a co-chaperone towards HSPA9/mortalin which,
CC by itself, is prone to self-aggregation. {ECO:0000269|PubMed:23462535}.
CC -!- SUBUNIT: Oligomerizes in a concentration-dependent fashion. Interacts
CC with HSPA9. {ECO:0000269|PubMed:23462535}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23462535}.
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DR EMBL; AL592301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC146915; AAI46916.1; -; mRNA.
DR EMBL; BC146924; AAI46925.1; -; mRNA.
DR CCDS; CCDS35179.1; -.
DR RefSeq; NP_001074318.1; NM_001080849.2.
DR AlphaFoldDB; Q5SXM8; -.
DR SMR; Q5SXM8; -.
DR BioGRID; 608915; 34.
DR IntAct; Q5SXM8; 18.
DR STRING; 9606.ENSP00000360803; -.
DR iPTMnet; Q5SXM8; -.
DR PhosphoSitePlus; Q5SXM8; -.
DR BioMuta; DNLZ; -.
DR DMDM; 74743980; -.
DR EPD; Q5SXM8; -.
DR jPOST; Q5SXM8; -.
DR MassIVE; Q5SXM8; -.
DR MaxQB; Q5SXM8; -.
DR PaxDb; Q5SXM8; -.
DR PeptideAtlas; Q5SXM8; -.
DR PRIDE; Q5SXM8; -.
DR ProteomicsDB; 63998; -.
DR Antibodypedia; 77454; 5 antibodies from 5 providers.
DR DNASU; 728489; -.
DR Ensembl; ENST00000371738.4; ENSP00000360803.3; ENSG00000213221.5.
DR GeneID; 728489; -.
DR KEGG; hsa:728489; -.
DR MANE-Select; ENST00000371738.4; ENSP00000360803.3; NM_001080849.3; NP_001074318.1.
DR UCSC; uc004chf.3; human.
DR CTD; 728489; -.
DR DisGeNET; 728489; -.
DR GeneCards; DNLZ; -.
DR HGNC; HGNC:33879; DNLZ.
DR HPA; ENSG00000213221; Low tissue specificity.
DR neXtProt; NX_Q5SXM8; -.
DR OpenTargets; ENSG00000213221; -.
DR PharmGKB; PA162384018; -.
DR VEuPathDB; HostDB:ENSG00000213221; -.
DR eggNOG; KOG3277; Eukaryota.
DR GeneTree; ENSGT00390000008220; -.
DR HOGENOM; CLU_093902_5_0_1; -.
DR InParanoid; Q5SXM8; -.
DR OMA; PGLRWLW; -.
DR OrthoDB; 1626191at2759; -.
DR PhylomeDB; Q5SXM8; -.
DR TreeFam; TF313165; -.
DR PathwayCommons; Q5SXM8; -.
DR SignaLink; Q5SXM8; -.
DR BioGRID-ORCS; 728489; 349 hits in 1078 CRISPR screens.
DR ChiTaRS; DNLZ; human.
DR GenomeRNAi; 728489; -.
DR Pharos; Q5SXM8; Tdark.
DR PRO; PR:Q5SXM8; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5SXM8; protein.
DR Bgee; ENSG00000213221; Expressed in apex of heart and 94 other tissues.
DR ExpressionAtlas; Q5SXM8; baseline and differential.
DR Genevisible; Q5SXM8; HS.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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 1: Evidence at protein level;
KW Chaperone; Metal-binding; Mitochondrion; Reference proteome;
KW Transit peptide; Zinc; Zinc-finger.
FT TRANSIT 1..49
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 50..178
FT /note="DNL-type zinc finger protein"
FT /id="PRO_0000317166"
FT ZN_FING 64..161
FT /note="DNL-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT REGION 151..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT VARIANT 169
FT /note="P -> H (in dbSNP:rs3812553)"
FT /id="VAR_053993"
FT VARIANT 178
FT /note="S -> T (in dbSNP:rs3812552)"
FT /id="VAR_053994"
SQ SEQUENCE 178 AA; 19204 MW; 5BB1094917DDD85B CRC64;
MLRTALRGAP RLLSRVQPRA PCLRRLWGRG ARPEVAGRRR AWAWGWRRSS SEQGPGPAAA
LGRVEAAHYQ LVYTCKVCGT RSSKRISKLA YHQGVVIVTC PGCQNHHIIA DNLGWFSDLN
GKRNIEEILT ARGEQVHRVA GEGALELVLE AAGAPTSTAA PEAGEDEGPP SPGKTEPS
