ID   DAAF1_PERPL             Reviewed;         622 AA.
AC   B6D5P1;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Dynein axonemal assembly factor 1;
DE   AltName: Full=Leucine-rich repeat-containing protein 50;
GN   Name=Dnaaf1; Synonyms=Lrrc50;
OS   Peromyscus polionotus (Oldfield mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Neotominae; Peromyscus.
OX   NCBI_TaxID=42413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=PGSC14;
RX   PubMed=18689890; DOI=10.1534/genetics.107.085902;
RA   Turner L.M., Chuong E.B., Hoekstra H.E.;
RT   "Comparative analysis of testis protein evolution in rodents.";
RL   Genetics 179:2075-2089(2008).
CC   -!- FUNCTION: Cilium-specific protein required for the stability of the
CC       ciliary architecture. Plays a role in cytoplasmic preassembly of dynein
CC       arms (By similarity). Involved in regulation of microtubule-based cilia
CC       and actin-based brush border microvilli (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNAAF1 family. {ECO:0000305}.
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DR   EMBL; EU836297; ACI22866.1; -; mRNA.
DR   AlphaFoldDB; B6D5P1; -.
DR   SMR; B6D5P1; -.
DR   GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR   GO; GO:0070840; F:dynein complex binding; ISS:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0036159; P:inner dynein arm assembly; IEA:InterPro.
DR   GO; GO:0036158; P:outer dynein arm assembly; IEA:InterPro.
DR   Gene3D; 3.80.10.10; -; 2.
DR   InterPro; IPR027734; DNAAF1.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR45973:SF19; PTHR45973:SF19; 1.
DR   PROSITE; PS51450; LRR; 6.
PE   2: Evidence at transcript level;
KW   Cell projection; Cilium; Leucine-rich repeat; Phosphoprotein; Repeat.
FT   CHAIN           1..622
FT                   /note="Dynein axonemal assembly factor 1"
FT                   /id="PRO_0000363932"
FT   REPEAT          101..123
FT                   /note="LRR 1"
FT   REPEAT          124..145
FT                   /note="LRR 2"
FT   REPEAT          146..167
FT                   /note="LRR 3"
FT   REPEAT          168..189
FT                   /note="LRR 4"
FT   REPEAT          190..211
FT                   /note="LRR 5"
FT   REPEAT          215..236
FT                   /note="LRR 6"
FT   DOMAIN          249..288
FT                   /note="LRRCT"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..340
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..552
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         349
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6AYH9"
FT   MOD_RES         464
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D2H9"
FT   MOD_RES         487
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D2H9"
SQ   SEQUENCE   622 AA;  69142 MW;  1A1BC4C1897FC9C7 CRC64;
     MHPEVSEQQA DGATEPSLEE SAGDHSGAGP GVRKEEINET KETCVGPSTT SCQSQKQQSG
     DSRLDCRSGY ARNDRDDRGP RMTKEFLQKL CKQHKLYITP ALNDTLYLHF KGFDRIENLE
     EYTGLRCLWL ECNGIQRIEN LQAQSELRCL FLQVNLLHKI ENLEPLQKLD ALNLSNNYIK
     TIENLSCLPV LNTLQMAHNR LETVADIQHL RECLRLCVLD LSHNMLSDPE ILSVLESMPC
     LRVLNLMGNP VTKHIPNYRR TVTVRLKQLT YLDDRPVFPK DRACAEAWAR GGYAAEKEER
     LQWESREHKK ITDSLEALAM IKRRAEERKK ARDKGETPLP DSEESSSTSP EAQDKPPLGE
     TQQKIEVLVE ESFKAKDELF PEKPGGEEEL AVVADRTMEE PDLPGSLAQS QTPLVATAEE
     STSSVAATDG TGIEDTEAIA LENKERLFID DLPDLEDVDG MDISMEDQTK ETGIPKIQVI
     SSLSDDSDPE LNDSPLPMLE HTPTGSTGVL SNIFAVCKDS SKAARVPLTD IYEPRATTAP
     ETQGQVFSTT PPRPLIQELE EDGRGENESK QSLPAQSSED GDSQLPEATL LGDRAENEAQ
     SSLDLGKPSP RASLEDIEFG LD