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Database: UniProt
Entry: B6D5P3
LinkDB: B6D5P3
Original site: B6D5P3 
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   22-FEB-2023, entry version 41.
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   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR45973:SF19; DYNEIN AXONEMAL ASSEMBLY FACTOR 1; 1.
DR   PANTHER; PTHR45973; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT SDS22-RELATED; 1.
DR   Pfam; PF14580; LRR_9; 1.
DR   SMART; SM00365; LRR_SD22; 3.
DR   SUPFAM; SSF52075; Outer arm dynein light chain 1; 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
//
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