ID A0A0D9S1F3_CHLSB Unreviewed; 699 AA.
AC A0A0D9S1F3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Dynein axonemal assembly factor 1 {ECO:0000256|ARBA:ARBA00024429, ECO:0000256|RuleBase:RU364076};
GN Name=DNAAF1 {ECO:0000313|Ensembl:ENSCSAP00000014692.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000014692.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000014692.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000014692.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Cilium-specific protein required for the stability of the
CC ciliary architecture. Plays a role in cytoplasmic preassembly of dynein
CC arms. Involved in regulation of microtubule-based cilia and actin-based
CC brush border microvilli. {ECO:0000256|RuleBase:RU364076}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000256|ARBA:ARBA00004138, ECO:0000256|RuleBase:RU364076}.
CC -!- SIMILARITY: Belongs to the DNAAF1 family.
CC {ECO:0000256|ARBA:ARBA00006453, ECO:0000256|RuleBase:RU364076}.
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DR EMBL; AQIB01129881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01129882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0D9S1F3; -.
DR STRING; 60711.ENSCSAP00000014692; -.
DR Ensembl; ENSCSAT00000001386.1; ENSCSAP00000014692.1; ENSCSAG00000003365.1.
DR eggNOG; ENOG502QQFE; Eukaryota.
DR GeneTree; ENSGT00940000158494; -.
DR OMA; LFVKECF; -.
DR Proteomes; UP000029965; Chromosome 5.
DR Bgee; ENSCSAG00000003365; Expressed in adrenal cortex and 2 other cell types or tissues.
DR GO; GO:0005930; C:axoneme; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0070840; F:dynein complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003341; P:cilium movement; IEA:Ensembl.
DR GO; GO:0071907; P:determination of digestive tract left/right asymmetry; IEA:Ensembl.
DR GO; GO:0071910; P:determination of liver left/right asymmetry; IEA:Ensembl.
DR GO; GO:0035469; P:determination of pancreatic left/right asymmetry; IEA:Ensembl.
DR GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0036159; P:inner dynein arm assembly; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0044458; P:motile cilium assembly; IEA:Ensembl.
DR GO; GO:0036158; P:outer dynein arm assembly; IEA:Ensembl.
DR GO; GO:0003356; P:regulation of cilium beat frequency; IEA:Ensembl.
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; 4.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|RuleBase:RU364076};
KW Cilium {ECO:0000256|ARBA:ARBA00023069, ECO:0000256|RuleBase:RU364076};
KW Leucine-rich repeat {ECO:0000256|RuleBase:RU364076};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Repeat {ECO:0000256|RuleBase:RU364076}.
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 699 AA; 77030 MW; E30AC2A858E12E23 CRC64;
MHPKPSEPAA GGAAELDCTQ ESGVEESAGD HGSAGPGGCK EEINDPKEIC VGSSATSYQS
QQKLSGDNGS GGHFAHPRED REDRGPRMTK SFLQKLCKQH KLYTTPALND TLYLHFKGFD
RIENLEEYTG LRCLWLQSNG IQRIENLEAQ TELRCLFLQV NLLHKIENLE ALQKLDALNL
SNNYIKTIEN LSCLPVLNTL QMAHNHLETV EDIQHLRECL TLCVLDLSHN KLSDPEILSI
LESMPDLRVL NLMGNPVIRH IPNYRRTVTV RLKHLTYLDD RPVFPKDRAC AEAWARGGYA
AEKEERQQWE SRERKKITDS IEALAMIKRR AEERKRQRES QERVGETTSS DDGENVPASE
EGKEEPPGDR ETRQKMELFV KESFEAKDEL CPEKPSGGEE LPVEVKREDG DREPEGTLPA
ETPPPPPPVE VKGEDGDQEP EGTLPAETPP PPPPVEVKRE DGDQEPEGTL PVEALPPPPL
GAAGEERTPQ AVATEGGFVT EPGGTRMEDL ETVRLETKET FCIDDLPDLE DDDETGKSLE
DQNMCFPKIE VISNLSDDSD PELDYTSLPV LENLPADTLS NIFAVSKDTS KAARAPFTGI
FIKEAKRDLE IPKQDTESPR PLIQELSDED PPGQPPMSPT CQRDAAPLTS SGDGDSDFLA
ASSAVPTESA TTPSETCVGV AQPSSPTWDL TALPAPKAS
//