DJB13_MOUSE
ID DJB13_MOUSE Reviewed; 316 AA.
AC Q80Y75; Q8CJA2;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=DnaJ homolog subfamily B member 13;
DE AltName: Full=Testis and spermatogenesis cell-related protein 6;
DE AltName: Full=Testis spermatocyte apoptosis-related gene 6 protein;
DE AltName: Full=Testis spermatogenesis apoptosis-related gene 3 protein;
DE AltName: Full=Testis spermatogenesis apoptosis-related gene 6 protein;
GN Name=Dnajb13; Synonyms=Tsarg, Tsarg3, Tsarg6;
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 [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=12673577;
RA Liu G., Lu G.-X., Fu J.-J., Liu S.-F., Xing X.-W., Li L.;
RT "Molecular cloning of TSARG3 gene related to apoptosis in human
RT spermatogenic cells.";
RL Zhonghua Yi Xue Yi Chuan Xue Za Zhi 20:107-110(2003).
RN [2]
RP SEQUENCE REVISION, FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=14673507;
RA Liu G., Lu G.-X., Fu J.-J., Liu S.-F., Xing X.-W.;
RT "Molecular cloning of mTSARG3 gene related to apoptosis in mouse
RT spermatogenic cells.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:1133-1139(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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=Testis;
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).
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=19919626; DOI=10.1111/j.1439-0531.2009.01473.x;
RA Guan J., Ekwurtzel E., Kvist U., Hultenby K., Yuan L.;
RT "DNAJB13 is a radial spoke protein of mouse '9+2' axoneme.";
RL Reprod. Domest. Anim. 45:992-996(2010).
RN [6]
RP FUNCTION.
RX PubMed=27530713; DOI=10.1038/srep31666;
RA Oji A., Noda T., Fujihara Y., Miyata H., Kim Y.J., Muto M., Nozawa K.,
RA Matsumura T., Isotani A., Ikawa M.;
RT "CRISPR/Cas9 mediated genome editing in ES cells and its application for
RT chimeric analysis in mice.";
RL Sci. Rep. 6:31666-31666(2016).
RN [7]
RP SUBCELLULAR LOCATION, INTERACTION WITH SUN5, AND DEVELOPMENTAL STAGE.
RX PubMed=29298896; DOI=10.1074/jbc.ra117.000861;
RA Shang Y., Yan J., Tang W., Liu C., Xiao S., Guo Y., Yuan L., Chen L.,
RA Jiang H., Guo X., Qiao J., Li W.;
RT "Mechanistic insights into acephalic spermatozoa syndrome-associated
RT mutations in the human SUN5 gene.";
RL J. Biol. Chem. 293:2395-2407(2018).
CC -!- FUNCTION: Plays a role in the formation of the central complex of
CC ciliary and flagellar axonemes. {ECO:0000250|UniProtKB:P59910,
CC ECO:0000269|PubMed:27530713}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with SUN5
CC (PubMed:29298896). {ECO:0000250|UniProtKB:P59910,
CC ECO:0000269|PubMed:29298896}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:29298896}. Cell projection, cilium
CC {ECO:0000269|PubMed:19919626}. Note=Localizes both to epithelial motile
CC cilium and the sperm flagellum (By similarity). In spermatids, rapidly
CC enriched in the coupling apparatus with the elongation of the
CC spermatid. Tightly attached to the implantation fossa during the
CC maturation of the spermatid. In mature spermatzoa evenly distributed
CC along the flagellum at the radial spoke of the axoneme
CC (PubMed:29298896, PubMed:19919626). {ECO:0000250|UniProtKB:P59910,
CC ECO:0000269|PubMed:19919626, ECO:0000269|PubMed:29298896}.
CC -!- TISSUE SPECIFICITY: Expressed in ciliated cell-containing tissues such
CC as testis, brain, lung, ovary and oviduct.
CC {ECO:0000269|PubMed:14673507, ECO:0000269|PubMed:19919626,
CC ECO:0000269|PubMed:29298896}.
CC -!- DEVELOPMENTAL STAGE: Expressed during spermiogenesis.
CC {ECO:0000269|PubMed:29298896}.
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DR EMBL; AF419292; AAN32703.2; -; mRNA.
DR EMBL; BC048501; AAH48501.1; -; mRNA.
DR CCDS; CCDS21499.1; -.
DR RefSeq; NP_705755.2; NM_153527.2.
DR AlphaFoldDB; Q80Y75; -.
DR SMR; Q80Y75; -.
DR STRING; 10090.ENSMUSP00000059074; -.
DR PhosphoSitePlus; Q80Y75; -.
DR REPRODUCTION-2DPAGE; Q80Y75; -.
DR MaxQB; Q80Y75; -.
DR PaxDb; Q80Y75; -.
DR PRIDE; Q80Y75; -.
DR ProteomicsDB; 279713; -.
DR Antibodypedia; 31001; 87 antibodies from 22 providers.
DR DNASU; 69387; -.
DR Ensembl; ENSMUST00000207405; ENSMUSP00000147019; ENSMUSG00000030708.
DR GeneID; 69387; -.
DR KEGG; mmu:69387; -.
DR UCSC; uc009inc.1; mouse.
DR CTD; 374407; -.
DR MGI; MGI:1916637; Dnajb13.
DR VEuPathDB; HostDB:ENSMUSG00000030708; -.
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000158090; -.
DR HOGENOM; CLU_017633_10_2_1; -.
DR InParanoid; Q80Y75; -.
DR OMA; AMQKFRI; -.
DR OrthoDB; 1393097at2759; -.
DR PhylomeDB; Q80Y75; -.
DR TreeFam; TF105141; -.
DR BioGRID-ORCS; 69387; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Dnajb13; mouse.
DR PRO; PR:Q80Y75; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q80Y75; protein.
DR Bgee; ENSMUSG00000030708; Expressed in seminiferous tubule of testis and 68 other tissues.
DR ExpressionAtlas; Q80Y75; baseline and differential.
DR Genevisible; Q80Y75; MM.
DR GO; GO:0005930; C:axoneme; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0097224; C:sperm connecting piece; IDA:UniProtKB.
DR GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:1904158; P:axonemal central apparatus assembly; ISS:UniProtKB.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Cell projection; Chaperone; Cilium; Cilium biogenesis/degradation;
KW Flagellum; Reference proteome.
FT CHAIN 1..316
FT /note="DnaJ homolog subfamily B member 13"
FT /id="PRO_0000071040"
FT DOMAIN 4..68
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT CONFLICT 133
FT /note="V -> I (in Ref. 2; AAN32703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 36155 MW; 38BBC8271A18C9B5 CRC64;
MGLDYYAVLQ VTRNSEDAQI KKAYRKLALK NHPLKSSEPG APEIFKQIAE AYDVLSDPVK
RGIYDKFGEE GLKGGIPLEF GSQTPWTTGY VFHGNPDKVF HEFFGGDNPF SEFFDAEGND
IDLNFGGLWG RGVQKQDPPI ERDLYLSLED LFFGCTKKIK ISRRVLNEDR YSSTIKDKIL
TIDVRPGWRQ GTRITFEKEG DQGPNIIPAD IIFIVKEKLH PRFRREHDNL FFVYPIPLGK
ALTCCTVEVK TLDDRLLNIP INDIVHPKYF KIVPGEGMPL PENPSKKGDL FIFFDIQFPT
RLTPQKKQML RQALLT
