ID   DAAF8_XENLA             Reviewed;        1572 AA.
AC   A0A1L8EYB2;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Dynein axonemal assembly factor 8 {ECO:0000305};
DE   AltName: Full=Dynein axonemal-associated protein 1 {ECO:0000303|PubMed:33263282};
GN   Name=dnaaf8; Synonyms=c16orf71, daap1 {ECO:0000303|PubMed:33263282};
GN   ORFNames=XELAEV_18045439mg {ECO:0000312|EMBL:OCT64336.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000312|EMBL:OCT64336.1};
RN   [1] {ECO:0000312|Proteomes:UP000186698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J {ECO:0000312|Proteomes:UP000186698};
RX   PubMed=27762356; DOI=10.1038/nature19840;
RA   Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA   Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA   Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA   Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA   Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA   Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA   Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA   Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA   Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA   Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA   Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA   Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA   Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT   "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL   Nature 538:336-343(2016).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP   AND INTERACTION WITH DNAI2.
RX   PubMed=33263282; DOI=10.7554/elife.58662;
RA   Lee C., Cox R.M., Papoulas O., Horani A., Drew K., Devitt C.C., Brody S.L.,
RA   Marcotte E.M., Wallingford J.B.;
RT   "Functional partitioning of a liquid-like organelle during assembly of
RT   axonemal dyneins.";
RL   Elife 9:0-0(2020).
CC   -!- FUNCTION: In cyliated cells, dynein axonemal particle-specific protein
CC       required for deployment of ODA to the axoneme. Interacts with outer
CC       dynein arm (ODA) subunits. {ECO:0000269|PubMed:33263282}.
CC   -!- SUBUNIT: Interacts with DNAI2. {ECO:0000269|PubMed:33263282}.
CC   -!- SUBCELLULAR LOCATION: Dynein axonemal particle
CC       {ECO:0000269|PubMed:33263282}. Note=Location is restricted to the outer
CC       dynein arm (ODA) sub-region of dynein axonemal particles (DynAPs).
CC       {ECO:0000269|PubMed:33263282}.
CC   -!- TISSUE SPECIFICITY: Expression is enriched in multiciliated cells in
CC       the epidermis and the nephrostomes of the pronephros.
CC       {ECO:0000269|PubMed:33263282}.
CC   -!- DISRUPTION PHENOTYPE: Mutant multiciliated cells show a severe loss of
CC       ODAs from motile cilia. {ECO:0000269|PubMed:33263282}.
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DR   EMBL; CM004482; OCT64336.1; -; Genomic_DNA.
DR   RefSeq; XP_018092012.1; XM_018236523.1.
DR   AlphaFoldDB; A0A1L8EYB2; -.
DR   SMR; A0A1L8EYB2; -.
DR   STRING; 8355.A0A1L8EYB2; -.
DR   GeneID; 108701634; -.
DR   KEGG; xla:108701634; -.
DR   CTD; 108701634; -.
DR   Xenbase; XB-GENE-22063499; dnaaf8.L.
DR   OMA; STARFAW; -.
DR   OrthoDB; 45213at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 108701634; Expressed in testis and 11 other tissues.
DR   GO; GO:0120293; C:dynein axonemal particle; IDA:UniProtKB.
DR   GO; GO:0070840; F:dynein complex binding; IDA:UniProtKB.
DR   GO; GO:0036158; P:outer dynein arm assembly; IMP:UniProtKB.
DR   Gene3D; 3.30.70.141; -; 3.
DR   InterPro; IPR031531; DNAAF8.
DR   InterPro; IPR034907; NDK-like_dom.
DR   InterPro; IPR036850; NDK-like_dom_sf.
DR   Pfam; PF15773; DUF4701; 1.
DR   Pfam; PF00334; NDK; 1.
DR   SMART; SM00562; NDK; 1.
DR   SUPFAM; SSF54919; SSF54919; 4.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..1572
FT                   /note="Dynein axonemal assembly factor 8"
FT                   /id="PRO_0000452438"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          324..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          849..871
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1249..1382
FT                   /note="NDK"
FT   COMPBIAS        333..355
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        849..864
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1572 AA;  175127 MW;  C65D062E4F619BFA CRC64;
     MASEQDGFLP AATRGDSNWS GVSGWESALS AMRAEVPSID SDDSSLSDCE EEELHIFQRE
     DTNLIPDLSI ELLDDGELNS EVVTRQMSLE KVEFSDSLEP SPNVCVPLSV QKAELDDTIN
     SRNPETEQLC PEPIDNIQTE SMVGIKDSEK EDGFRHVLHS SVTTVLKPQI NSNVDSEYEI
     HPGNTEKEHL STSALSSKPV GLSLQFLECL EQWDLNALLH QLKEEEVQER EMPPLILSME
     ESTERRHKLI MEKLVEFAAQ QSEEVSSVPQ LEEKEKEGTI SKSSFRPYPD QKMYLKGSGK
     HPQSFSTICL DLRTTVSKMG QVTSLEQNPE NPSQRNEQKE KHHLNKTDHT GKSLLLRNRH
     NIQNDSLSDA NMSNSESLSK EKKELGTPTQ RKQRPKSKVD ISPKLQEMVG REEKDGREEQ
     EKEKEILQYL PPKSLINSRA DEFAQREKQE KEKKARLRML TQLEDLKPRS SVNGRQPMAE
     ATPILFHPET SYCPGISSLP DVARSGVETL LLTICLSSCG QVFIPGQHGA RSSYPSLFLA
     NTFHCLLTWL ISLVPGVNTH GKVNAPFHVL GLQQAWQEEG LALYACLSPR QIATQSSPKI
     RKHKGKQDLR GTSSFYQRVS LFLSHNTLQS VIWWSEDVVE RLQGKLFPLP TEVPAVRLSS
     IATLNSAPEA VEKVFSSACG FYWQTLETEE KINPLLSEIP TDSETEVVSV IVFERMLSNP
     TAFHHTLHII QTEGLDVCGV RLLYPQANAL HSYIDTVPSS YTGGDGQTLP VLALALRGTQ
     AEHIWAEIAG PFDPQLARLT DQYSLNAMYG FKRGEPIMHW ARKSGRLLQE LSLWFGGRIP
     PSGSFNIGFQ NPYSRSTQPR SANLRSRSDS EKDVTAFHDT DRCRPPALLT ASILGDVFLV
     VSPAVPSAAY GDVIDICLHR GFALYGLRRL RLSAKRSAML SMSSTQVSIF CPNVPHSQTD
     AQPCRQPRLH CFLLLLRKEN AAHHTSGLIQ ALMNELAERG LLGAIHAKFS YICEVDPSFC
     FHVAPYTDNL LQSLGGSLHA MPDLSTVPMD MLSLRPFASD PEDEQVVVLT MSGKHTLRRA
     GYFLQKILRP TLKTPASNTG SVHDGFELLG LKWLPSLSRL QAKEITPYEV GDRPWQRSIE
     HLISNPALLC ALRRSNAFAV LQHTIKQLAP TLGMEHPQLI ASATPEIAFR QAALIFSDRD
     LVSDPESRSS LMYIPPTGIN CRAGGTEDRR GTTESIFTYM LSGPPVLYTV LLLKPRIWSS
     ALGKILYKVH QQKFILVGMK PVSLTTAMCS QILPEDVKKS EALCLTHCDY LTSGPCLALC
     LQRRGAVLKL LDVLGPEDPE LCRAQDQFLW RAQYGTSAVQ NGMYGSTSYQ AAIRDIKTFF
     PEGLLFEEST VLQAEQIPKL TSDILVCSRS HRQTVKNPAC GPELPTTDLP FTSALCQTTC
     LLFPPHMLRT SPPPYIPALE QLMAKEFHIT AARLTAFDQL QAQLVAEMYS PGNYLTAKIK
     LLTEGPCLLV AAQRDNAVTC FPSLVHSDDR HNMSAQTLTE QVLCPQTESQ ANKMLSCFFD
     SLTPDSIHQI LH