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Coiled-coil domain-containing protein 40 homolog (Flagellar-associated protein 172)

 CCD40_CHLRE             Reviewed;         576 AA.
A8IQT2;
04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 1.
18-JUL-2018, entry version 34.
RecName: Full=Coiled-coil domain-containing protein 40 homolog {ECO:0000305};
AltName: Full=Flagellar-associated protein 172 {ECO:0000303|PubMed:15998802};
Name=CCDC40; Synonyms=FAP172 {ECO:0000303|PubMed:15998802};
ORFNames=CHLREDRAFT_170513 {ECO:0000312|EMBL:EDP04735.1};
Chlamydomonas reinhardtii (Chlamydomonas smithii).
Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae;
Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
NCBI_TaxID=3055;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CC-503, and cw92;
PubMed=17932292; DOI=10.1126/science.1143609;
Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K.,
Marechal-Drouard L., Marshall W.F., Qu L.H., Nelson D.R.,
Sanderfoot A.A., Spalding M.H., Kapitonov V.V., Ren Q., Ferris P.,
Lindquist E., Shapiro H., Lucas S.M., Grimwood J., Schmutz J.,
Cardol P., Cerutti H., Chanfreau G., Chen C.L., Cognat V., Croft M.T.,
Dent R., Dutcher S., Fernandez E., Fukuzawa H., Gonzalez-Ballester D.,
Gonzalez-Halphen D., Hallmann A., Hanikenne M., Hippler M., Inwood W.,
Jabbari K., Kalanon M., Kuras R., Lefebvre P.A., Lemaire S.D.,
Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L., Mittag M.,
Mittelmeier T., Moroney J.V., Moseley J., Napoli C., Nedelcu A.M.,
Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J., Purton S.,
Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L., Schroda M.,
Stern D., Umen J., Willows R., Wilson N., Zimmer S.L., Allmer J.,
Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P.,
Jorgensen R., Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T.,
Brokstein P., Dubchak I., Goodstein D., Hornick L., Huang Y.W.,
Jhaveri J., Luo Y., Martinez D., Ngau W.C., Otillar B., Poliakov A.,
Porter A., Szajkowski L., Werner G., Zhou K., Grigoriev I.V.,
Rokhsar D.S., Grossman A.R.;
"The Chlamydomonas genome reveals the evolution of key animal and
plant functions.";
Science 318:245-250(2007).
[2]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15998802; DOI=10.1083/jcb.200504008;
Pazour G.J., Agrin N., Leszyk J., Witman G.B.;
"Proteomic analysis of a eukaryotic cilium.";
J. Cell Biol. 170:103-113(2005).
[3]
METHYLATION AT ARG-246 AND ARG-523.
PubMed=24152136; DOI=10.1021/bi4011623;
Werner-Peterson R., Sloboda R.D.;
"Methylation of structural components of the axoneme occurs during
flagellar disassembly.";
Biochemistry 52:8501-8509(2013).
[4]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CCDC39/FAP59, AND
DISRUPTION PHENOTYPE.
PubMed=25395538; DOI=10.1126/science.1260214;
Oda T., Yanagisawa H., Kamiya R., Kikkawa M.;
"Cilia and flagella. A molecular ruler determines the repeat length in
eukaryotic cilia and flagella.";
Science 346:857-860(2014).
-!- FUNCTION: Required for assembly of dynein regulatory complex (DRC)
and inner dynein arm complexes, which are responsible for ciliary
beat regulation, by acting as a molecular ruler that determines
the 96 nanometer (nm) repeat length and arrangements of components
in cilia and flagella (PubMed:25395538). Together with
CCDC39/FAP59 forms a 96-nm-long complex in flagella. This complex
does not act as a physical ruler, but rather act as a negative
regulator for radial spokes: the complex lays along specific
protofilaments, masking radial spoke binding sites and allowing
recruitment of inner dynein arm (IDA) and nexin-dynein regulatory
complexes (N-DRC) (PubMed:25395538).
{ECO:0000269|PubMed:25395538}.
-!- SUBUNIT: Interacts with CCDC39/FAP59.
{ECO:0000269|PubMed:25395538}.
-!- INTERACTION:
A8IQE0:CCDC39; NbExp=2; IntAct=EBI-16127612, EBI-16127597;
-!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
{ECO:0000269|PubMed:25395538}.
-!- PTM: Asymmetrically dimethylated at Arg-246 and Arg-523 during
flagellum resorption. Probably methylated by PRMT1.
{ECO:0000269|PubMed:24152136}.
-!- DISRUPTION PHENOTYPE: Short and immotile flagella. Inner dynein
arm (IDA) and nexin-dynein regulatory complex (N-DRC) components
are absent or severely reduced. Radial spokes are attached to
doublet microtubules with an irregular periodicity of 32 nm
instead of 96 nm. {ECO:0000269|PubMed:25395538}.
-!- SIMILARITY: Belongs to the CCDC40 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The length of things
- Issue 170 of June 2015;
URL="https://web.expasy.org/spotlight/back_issues/170/";
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EMBL; DS496120; EDP04735.1; -; Genomic_DNA.
RefSeq; XP_001691627.1; XM_001691575.1.
SMR; A8IQT2; -.
DIP; DIP-61435N; -.
IntAct; A8IQT2; 1.
STRING; 3055.EDP04735; -.
iPTMnet; A8IQT2; -.
PaxDb; A8IQT2; -.
EnsemblPlants; EDP04735; EDP04735; CHLREDRAFT_170513.
GeneID; 5717350; -.
Gramene; EDP04735; EDP04735; CHLREDRAFT_170513.
KEGG; cre:CHLREDRAFT_170513; -.
InParanoid; A8IQT2; -.
GO; GO:0005930; C:axoneme; IBA:GO_Central.
GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
GO; GO:0035082; P:axoneme assembly; IBA:GO_Central.
GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; IBA:GO_Central.
InterPro; IPR037386; CCDC40.
PANTHER; PTHR16275; PTHR16275; 3.
1: Evidence at protein level;
Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
Flagellum; Methylation.
CHAIN 1 576 Coiled-coil domain-containing protein 40
homolog.
/FTId=PRO_0000431956.
COILED 33 175 {ECO:0000255}.
COILED 232 269 {ECO:0000255}.
COILED 311 397 {ECO:0000255}.
MOD_RES 246 246 Asymmetric dimethylarginine.
{ECO:0000269|PubMed:24152136}.
MOD_RES 523 523 Asymmetric dimethylarginine.
{ECO:0000269|PubMed:24152136}.
SEQUENCE 576 AA; 63599 MW; B24A1CC4E7F6B42D CRC64;
MADPMDQPST SDPVDNQIFG EQGGLRPDHP LLRRAQEALK VQFEANRTRL QEELREKANA
LKQAKARREA LGVELYGFQQ NLAKLQLNLE TTHQNYQCED QLNQLKQQLS LEEGDTKGER
SRRVCVCVCR VCCRIDTLQD NLKGTQQQLA LVSAQLEAQK RETRAALETL AEAEVGGCVR
DEALSAIQDG MREQQQQELS LVLEIEGYKK DVVREQLKHE SLTAVVRKVE GDAVFVQKQI
EGAQERQARL QEILAKLAKS LEHTEAEGEA DAVDRAITKV AAEGRAIEEE MLSALSDQTT
AEKATSKTAA DTQELRKRIR AEELAVVETE NELAKLQVDI LNTEAHNSRL GETLGLLDEE
LRDKGRTIEK YELEIKRRND EIEKKTREID ILNRRRDCRG SAALDTRPLQ APPPPQVKSD
LALTTPMYTP PPVPQPSVGM TVTTEKLVSD MEKALTKREI ISVKGRATAA KSKSSTPAGS
ATASSRASPS ASVASSTLTR NQLDRATTDL AKSIKDLEAG RYRPVVEDAA AVGEELGRAQ
DKLGRVVALL EGLRQAAPHL AGELDKVLCH VADVRA


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