DAAF1_PERCA
ID DAAF1_PERCA Reviewed; 622 AA.
AC B6D5P6;
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 californicus (California mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Peromyscus.
OX NCBI_TaxID=42520;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=PGSC19;
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; EU836302; ACI22871.1; -; mRNA.
DR AlphaFoldDB; B6D5P6; -.
DR SMR; B6D5P6; -.
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_0000363930"
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..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..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..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..555
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; 68917 MW; 9DDC17870F6BF88A CRC64;
MHPEVSEQQA DGATEPSLEE SAGDHSGAGP GVRKEEINET KETCVGPSTT SCQSQKQQSG
DSRLECRSGY ARNDRDDRGP RMTKEFLQKL CKQHKLYITP ALNDTLYLHF KGFDRIENLE
EYTGLRCLWL ECNGIQRIEN LQAQSELRCL FLQVNLLHKI ENLEPLQKLD ALNLSNNYIK
TIENLSCLPV LNTLQMAHNR LETVADIQHL GECLRLCVLD LSHNMLSDPE ILSVLESMPC
LRVLNLMGNP VTKHIPNYRR TVTVRLKQLT YLDDRPVFPK DRACAEAWAR GGYAAEKEER
LQWESREHKK ITDSLEALAM IKRRAEERKK ARDKGETPLP DSEESSSTSP EAQEKPPLGE
TQEKIELFVK GSFKAKDELF PEKPGGEEEL AVVADRTVEE PDLSGSLAQS QIPLVATAEE
STSSVAATDG ARTEDTEAIA LETKERLFID DLPDLEDVDG MDISIEDQTK ETGIPKIQVV
SSLSDDSDPE LNDSSLPMLE HTPTGSTGIL SNIFAVCKDS SKAARVPLTD ICKPTATTEV
ETQGQVFSTT RPQPLIQELG EDGRGENEPN QSLPAQSSED GDSQLPEATP LGDRAENEAQ
SSLDLGEPSP RASLEDIEFG LD