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Database: UniProt
Entry: A0A0D9S1F3_CHLSB
LinkDB: A0A0D9S1F3_CHLSB
Original site: A0A0D9S1F3_CHLSB 
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
//
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