DAAF1_PERLE
ID DAAF1_PERLE Reviewed; 622 AA.
AC B6D5P3;
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 leucopus (White-footed mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Peromyscus.
OX NCBI_TaxID=10041;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=PGSC16;
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; EU836299; ACI22868.1; -; mRNA.
DR AlphaFoldDB; B6D5P3; -.
DR SMR; B6D5P3; -.
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_0000363931"
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 481..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..41
FT /note="Basic and acidic residues"
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 570..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; 69351 MW; 99335D43E259E2DD CRC64;
MHPEVSEPQA DGATEPSLEE SAGDHGRAGP 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
TQQKIEVFVE ESFKVKDELF PEKPGGEEEL AVVEDRTMEE PDLPGSLAQS QTLLVATAEE
STSSVAATDG TGTEDTEAIA LETKERLFID DLPDLEDVDG MDMSMEDQTK EMGIPKIQVI
SSLSDDSDPE LNDSPLPMLE HTPTGSTGVL SNIFAVCKDS SKAVRVPLTD ICEPRATTEL
ETQGQVFSTT PPRPLIQELE EDGRGENESK PSLPAQSSED GDSQLPEATL LGDRAENEAQ
SSLDLGKPSP RASLEDIEFG LD