DAAF1_RAT
ID DAAF1_RAT Reviewed; 633 AA.
AC Q6AYH9;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Dynein axonemal assembly factor 1;
DE AltName: Full=Leucine-rich repeat-containing protein 50;
GN Name=Dnaaf1; Synonyms=Lrrc50;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; THR-462; SER-465 AND
RP SER-488, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC079038; AAH79038.1; -; mRNA.
DR RefSeq; NP_001014176.1; NM_001014154.1.
DR AlphaFoldDB; Q6AYH9; -.
DR SMR; Q6AYH9; -.
DR STRING; 10116.ENSRNOP00000020917; -.
DR iPTMnet; Q6AYH9; -.
DR PhosphoSitePlus; Q6AYH9; -.
DR PaxDb; Q6AYH9; -.
DR PRIDE; Q6AYH9; -.
DR Ensembl; ENSRNOT00000020917; ENSRNOP00000020917; ENSRNOG00000015590.
DR GeneID; 361419; -.
DR KEGG; rno:361419; -.
DR UCSC; RGD:1310542; rat.
DR CTD; 123872; -.
DR RGD; 1310542; Dnaaf1.
DR eggNOG; ENOG502QQFE; Eukaryota.
DR GeneTree; ENSGT00940000158494; -.
DR HOGENOM; CLU_027574_0_0_1; -.
DR InParanoid; Q6AYH9; -.
DR PhylomeDB; Q6AYH9; -.
DR TreeFam; TF315818; -.
DR PRO; PR:Q6AYH9; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000015590; Expressed in testis and 8 other tissues.
DR ExpressionAtlas; Q6AYH9; baseline and differential.
DR Genevisible; Q6AYH9; RN.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0070840; F:dynein complex binding; ISS:UniProtKB.
DR GO; GO:0070286; P:axonemal dynein complex assembly; ISO:RGD.
DR GO; GO:0035082; P:axoneme assembly; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0003341; P:cilium movement; ISO:RGD.
DR GO; GO:0071907; P:determination of digestive tract left/right asymmetry; ISO:RGD.
DR GO; GO:0071910; P:determination of liver left/right asymmetry; ISO:RGD.
DR GO; GO:0035469; P:determination of pancreatic left/right asymmetry; ISO:RGD.
DR GO; GO:0001947; P:heart looping; ISO:RGD.
DR GO; GO:0036159; P:inner dynein arm assembly; ISO:RGD.
DR GO; GO:0060972; P:left/right pattern formation; ISO:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0044458; P:motile cilium assembly; ISO:RGD.
DR GO; GO:0036158; P:outer dynein arm assembly; ISO:RGD.
DR GO; GO:0003356; P:regulation of cilium beat frequency; ISO:RGD.
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 1: Evidence at protein level;
KW Cell projection; Cilium; Leucine-rich repeat; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..633
FT /note="Dynein axonemal assembly factor 1"
FT /id="PRO_0000232891"
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..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..633
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 43..66
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 538..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 462
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 633 AA; 69956 MW; EFC7D371075A1FB2 CRC64;
MHPEASEPPV DSAAEPSLEE SAGDHGDAGP GVRKEEINET KETCVGPCTT SCQSQQQPSG
DNGSDGLFTH SRDDRDDRGP RMTKQFLQKL CKQHKLYVTP ALNDTLYLHF KGFDRIENLE
EYTGLRCLWL ECNGIQRIEN LQAQSELRCL FLQVNLLHKI ENLEPLQKLD ALNLSNNYIK
TIENLSCLPV LNTLQMAHNR LETVADIEHL RECLQLCVLD LSHNSLSDPE ILSVLETMPC
LRVLNLMGNP VTKHIPNYRR TVTVRLKHLT YLDDRPVFPK DRACAEAWAR GGYAAEKEER
HQWESREHKK ITDSLEALAM IKRRAEERKK ARDRGETPLP ESEKSIPTSP EAQEKPPKGE
TQQKMESFVK ESFEAKDELF PEKPGEGEEL SVVVGNRAVE DADLSGNLAH TQTPVVVTPE
EVTSPVEATD GARTEDTEAI ALETKEKLFI DDLPDLEDVD GTDVSVEDQT KDTGIRKIQA
ISSLSDDSDL ELEELPLSVF EGTPISPTGA LSHIFAVSKD PSEAARVPFA DICMPTATTD
LETQSQDPST ASSHPLIQEL GEDELTEGES NQPLPPQSCA SDPTLAQSSE GGDSQLPAAT
PLGDGAENEA QSSLYPEEPS TRIGLEDIEF GLD
