DAAF5_MOUSE
ID DAAF5_MOUSE Reviewed; 853 AA.
AC B9EJR8;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Dynein axonemal assembly factor 5 {ECO:0000250|UniProtKB:Q86Y56};
DE AltName: Full=HEAT repeat-containing protein 2 {ECO:0000305};
GN Name=Dnaaf5 {ECO:0000312|MGI:MGI:3616079};
GN Synonyms=Heatr2 {ECO:0000312|MGI:MGI:3616079};
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 {ECO:0000312|EMBL:AAI47493.1};
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, Spleen, and 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 [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=25232951; DOI=10.1371/journal.pgen.1004577;
RA Diggle C.P., Moore D.J., Mali G., zur Lage P., Ait-Lounis A., Schmidts M.,
RA Shoemark A., Garcia Munoz A., Halachev M.R., Gautier P., Yeyati P.L.,
RA Bonthron D.T., Carr I.M., Hayward B., Markham A.F., Hope J.E.,
RA von Kriegsheim A., Mitchison H.M., Jackson I.J., Durand B., Reith W.,
RA Sheridan E., Jarman A.P., Mill P.;
RT "HEATR2 plays a conserved role in assembly of the ciliary motile
RT apparatus.";
RL PLoS Genet. 10:E1004577-E1004577(2014).
CC -!- FUNCTION: Cytoplasmic protein involved in the delivery of the dynein
CC machinery to the motile cilium. It is required for the assembly of the
CC axonemal dynein inner and outer arms, two structures attached to the
CC peripheral outer doublet A microtubule of the axoneme, that play a
CC crucial role in cilium motility. {ECO:0000250|UniProtKB:Q86Y56}.
CC -!- SUBUNIT: Interacts with DNAI2; probably involved in outer arm dynein
CC assembly. {ECO:0000250|UniProtKB:Q86Y56}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25232951}.
CC Cytoplasmic granule {ECO:0000250|UniProtKB:Q86Y56}. Note=Observed only
CC in the cytoplasm of ciliated cells and absent from cilia.
CC {ECO:0000269|PubMed:25232951}.
CC -!- TISSUE SPECIFICITY: Expressed in ciliated cells including ependymal
CC cells lining the lateral ventricles and multiciliated epithelium of
CC oviduct ampulla. {ECO:0000269|PubMed:25232951}.
CC -!- DEVELOPMENTAL STAGE: Enriched in tissues with differentiating ciliated
CC cells including 18.5 dpc trachea and bronchus.
CC {ECO:0000269|PubMed:25232951}.
CC -!- SIMILARITY: Belongs to the DNAAF5 family. {ECO:0000305}.
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DR EMBL; AC125065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC147492; AAI47493.1; -; mRNA.
DR CCDS; CCDS39349.1; -.
DR RefSeq; NP_001074734.1; NM_001081265.1.
DR AlphaFoldDB; B9EJR8; -.
DR SMR; B9EJR8; -.
DR IntAct; B9EJR8; 11.
DR STRING; 10090.ENSMUSP00000026975; -.
DR iPTMnet; B9EJR8; -.
DR PhosphoSitePlus; B9EJR8; -.
DR EPD; B9EJR8; -.
DR MaxQB; B9EJR8; -.
DR PaxDb; B9EJR8; -.
DR PeptideAtlas; B9EJR8; -.
DR PRIDE; B9EJR8; -.
DR ProteomicsDB; 279145; -.
DR Antibodypedia; 10790; 90 antibodies from 18 providers.
DR DNASU; 433956; -.
DR Ensembl; ENSMUST00000026975; ENSMUSP00000026975; ENSMUSG00000025857.
DR GeneID; 433956; -.
DR KEGG; mmu:433956; -.
DR UCSC; uc009afz.1; mouse.
DR CTD; 54919; -.
DR MGI; MGI:3616079; Dnaaf5.
DR VEuPathDB; HostDB:ENSMUSG00000025857; -.
DR eggNOG; ENOG502QRXT; Eukaryota.
DR GeneTree; ENSGT00390000005666; -.
DR HOGENOM; CLU_010823_1_0_1; -.
DR InParanoid; B9EJR8; -.
DR OMA; RKHMGPL; -.
DR OrthoDB; 123510at2759; -.
DR PhylomeDB; B9EJR8; -.
DR TreeFam; TF326738; -.
DR BioGRID-ORCS; 433956; 25 hits in 74 CRISPR screens.
DR ChiTaRS; Dnaaf5; mouse.
DR PRO; PR:B9EJR8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; B9EJR8; protein.
DR Bgee; ENSMUSG00000025857; Expressed in animal zygote and 253 other tissues.
DR ExpressionAtlas; B9EJR8; baseline and differential.
DR Genevisible; B9EJR8; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0045505; F:dynein intermediate chain binding; ISO:MGI.
DR GO; GO:0003341; P:cilium movement; ISS:UniProtKB.
DR GO; GO:0036159; P:inner dynein arm assembly; ISS:UniProtKB.
DR GO; GO:0036158; P:outer dynein arm assembly; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR034085; TOG.
DR SMART; SM01349; TOG; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cilium biogenesis/degradation; Cytoplasm; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q86Y56"
FT CHAIN 2..853
FT /note="Dynein axonemal assembly factor 5"
FT /id="PRO_0000431656"
FT REPEAT 69..107
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 200..238
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 240..276
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 278..316
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 374..412
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 597..636
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 694..732
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 736..774
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 782..820
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q86Y56"
SQ SEQUENCE 853 AA; 93851 MW; 5F46E03E978DCC72 CRC64;
MAAPAEAEVA AAPGLTEAAE AAELTRALSR LLPGLETESK LGRRRALEAL EQVLEEAVRP
GADSAAFQGP WARLLLPRLL RLLSDPAEGC RALAAHLLDL GLRRAARPRD ALPRLLPALS
ARLARPELAR PPPEPCEELR LALVQLLHLA VDLGGAALAP HLDDAVRALR AALLDPFAAV
RREGCECAAA LARATPEHFH MQSESLIGPL MQTISHQHWK VRVAVIEATG TVIQFGSGNS
VDDVLSHFAQ RLFDDVPQVR QAVTSVVGGW LLNLRDRYSF LHKLTPLLLS SFSDEMPEIR
QTATSLWEKV GLQWQQENEA DLKDKLDFAS PPPPNYPEHE SRPGLGCREL VFRNLSKVLP
AICHDITDWV VGTRVKAAQL LPVLLLHAED HITQHLEIVL RTLHQACTDE EKAVVGSCIR
AAELIGTFVS PEVFLKLILA MLKKAPSASG LLILASVIRG CPRNALQPHV TVIATELAQE
HICQGSENNL YLEHLLLCVQ ALLSVCQEDC RAASLQFLEV LVTIMAVSDA VGLEKKAQKT
MDTLAEVEDI PSSQDLYRKH VGALLERLTA SHGEWAVHSV QLLKFTVLLT QAGPAVGEAL
QHVIPTLRAC LQPSTDPHMR LKLFSILSMM LLRPKDTVDS QGQFRGYLDM VINDILAPNL
QWHAGRTAAA IRTAAISCLW ALISSDILSA KQVQEAQETL MPQVLATLED DSQTTRLMSC
RIINMFLKNS GDTMEPEKFL KVYPELLKRL DDVSNDVRMA AASALLTWLK CIESLDGKSA
YQSSVQFLYR ELLVHLDDPE SAIQDTVLEV LKEGSVLFPD VLVRETEAVV HKHRSATYCE
QLLQHMQTMA AAR
