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DNLZ_MOUSE
ID   DNLZ_MOUSE              Reviewed;         177 AA.
AC   Q9D113; B2RTG5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=D2Bwg1335e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May function as a co-chaperone towards HSPA9/mortalin which,
CC       by itself, is prone to self-aggregation. {ECO:0000250}.
CC   -!- SUBUNIT: Oligomerizes in a concentration-dependent fashion. Interacts
CC       with HSPA9 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
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DR   EMBL; AK004089; BAB23162.1; -; mRNA.
DR   EMBL; AK142070; BAE24931.1; -; mRNA.
DR   EMBL; AL732541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC139333; AAI39334.1; -; mRNA.
DR   EMBL; BC139334; AAI39335.1; -; mRNA.
DR   CCDS; CCDS38083.1; -.
DR   RefSeq; NP_001132975.1; NM_001139503.1.
DR   RefSeq; NP_001132976.1; NM_001139504.1.
DR   RefSeq; NP_081104.1; NM_026828.3.
DR   AlphaFoldDB; Q9D113; -.
DR   SMR; Q9D113; -.
DR   BioGRID; 206849; 2.
DR   STRING; 10090.ENSMUSP00000028295; -.
DR   PhosphoSitePlus; Q9D113; -.
DR   EPD; Q9D113; -.
DR   MaxQB; Q9D113; -.
DR   PaxDb; Q9D113; -.
DR   PeptideAtlas; Q9D113; -.
DR   PRIDE; Q9D113; -.
DR   ProteomicsDB; 277357; -.
DR   Antibodypedia; 77454; 5 antibodies from 5 providers.
DR   Ensembl; ENSMUST00000028295; ENSMUSP00000028295; ENSMUSG00000075467.
DR   GeneID; 52838; -.
DR   KEGG; mmu:52838; -.
DR   UCSC; uc008iur.2; mouse.
DR   CTD; 728489; -.
DR   MGI; MGI:106559; Dnlz.
DR   VEuPathDB; HostDB:ENSMUSG00000075467; -.
DR   eggNOG; KOG3277; Eukaryota.
DR   GeneTree; ENSGT00390000008220; -.
DR   HOGENOM; CLU_093902_5_0_1; -.
DR   InParanoid; Q9D113; -.
DR   OMA; PGLRWLW; -.
DR   OrthoDB; 1626191at2759; -.
DR   PhylomeDB; Q9D113; -.
DR   TreeFam; TF313165; -.
DR   BioGRID-ORCS; 52838; 25 hits in 75 CRISPR screens.
DR   ChiTaRS; Dnlz; mouse.
DR   PRO; PR:Q9D113; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9D113; protein.
DR   Bgee; ENSMUSG00000075467; Expressed in embryonic brain and 254 other tissues.
DR   Genevisible; Q9D113; MM.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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..53
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           54..177
FT                   /note="DNL-type zinc finger protein"
FT                   /id="PRO_0000317167"
FT   ZN_FING         68..165
FT                   /note="DNL-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT   REGION          155..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00834"
SQ   SEQUENCE   177 AA;  19403 MW;  90B09E8088E364A2 CRC64;
     MLRTALSRMP TLLRSVRTRD SGPRRLWDLG ARLKTAERLR GWAWGWASGW RSSSSAPGSG
     RAAALGRVEA DHYQLVYTCK VCGTRSSKRI SKLAYHQGVV IVTCPGCQNH HIIADNLSWF
     SDLKGKRNIE EILAARGEEV RRVSGDGALE LILEAAVPPD TPEGDEDPPN PGKMGQS
 
 
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