CCD40_CHLRE
ID CCD40_CHLRE Reviewed; 576 AA.
AC A8IQT2;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Coiled-coil domain-containing protein 40 homolog {ECO:0000305};
DE AltName: Full=Flagellar-associated protein 172 {ECO:0000303|PubMed:15998802};
GN Name=CCDC40; Synonyms=FAP172 {ECO:0000303|PubMed:15998802};
GN ORFNames=CHLREDRAFT_170513 {ECO:0000312|EMBL:EDP04735.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503, and cw92;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15998802; DOI=10.1083/jcb.200504008;
RA Pazour G.J., Agrin N., Leszyk J., Witman G.B.;
RT "Proteomic analysis of a eukaryotic cilium.";
RL J. Cell Biol. 170:103-113(2005).
RN [3]
RP METHYLATION AT ARG-246 AND ARG-523.
RX PubMed=24152136; DOI=10.1021/bi4011623;
RA Werner-Peterson R., Sloboda R.D.;
RT "Methylation of structural components of the axoneme occurs during
RT flagellar disassembly.";
RL Biochemistry 52:8501-8509(2013).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CCDC39/FAP59, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=25395538; DOI=10.1126/science.1260214;
RA Oda T., Yanagisawa H., Kamiya R., Kikkawa M.;
RT "Cilia and flagella. A molecular ruler determines the repeat length in
RT eukaryotic cilia and flagella.";
RL Science 346:857-860(2014).
CC -!- FUNCTION: Required for assembly of dynein regulatory complex (DRC) and
CC inner dynein arm complexes, which are responsible for ciliary beat
CC regulation, by acting as a molecular ruler that determines the 96
CC nanometer (nm) repeat length and arrangements of components in cilia
CC and flagella (PubMed:25395538). Together with CCDC39/FAP59 forms a 96-
CC nm-long complex in flagella. This complex does not act as a physical
CC ruler, but rather act as a negative regulator for radial spokes: the
CC complex lays along specific protofilaments, masking radial spoke
CC binding sites and allowing recruitment of inner dynein arm (IDA) and
CC nexin-dynein regulatory complexes (N-DRC) (PubMed:25395538).
CC {ECO:0000269|PubMed:25395538}.
CC -!- SUBUNIT: Interacts with CCDC39/FAP59. {ECO:0000269|PubMed:25395538}.
CC -!- INTERACTION:
CC A8IQT2; A8IQE0: CCDC39; NbExp=2; IntAct=EBI-16127612, EBI-16127597;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:25395538}.
CC -!- PTM: Asymmetrically dimethylated at Arg-246 and Arg-523 during
CC flagellum resorption. Probably methylated by PRMT1.
CC {ECO:0000269|PubMed:24152136}.
CC -!- DISRUPTION PHENOTYPE: Short and immotile flagella. Inner dynein arm
CC (IDA) and nexin-dynein regulatory complex (N-DRC) components are absent
CC or severely reduced. Radial spokes are attached to doublet microtubules
CC with an irregular periodicity of 32 nm instead of 96 nm.
CC {ECO:0000269|PubMed:25395538}.
CC -!- SIMILARITY: Belongs to the CCDC40 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The length of things - Issue
CC 170 of June 2015;
CC URL="https://web.expasy.org/spotlight/back_issues/170/";
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DR EMBL; DS496120; EDP04735.1; -; Genomic_DNA.
DR RefSeq; XP_001691627.1; XM_001691575.1.
DR AlphaFoldDB; A8IQT2; -.
DR SMR; A8IQT2; -.
DR DIP; DIP-61435N; -.
DR IntAct; A8IQT2; 1.
DR STRING; 3055.EDP04735; -.
DR iPTMnet; A8IQT2; -.
DR PaxDb; A8IQT2; -.
DR GeneID; 5717350; -.
DR eggNOG; ENOG502QQ91; Eukaryota.
DR HOGENOM; CLU_473593_0_0_1; -.
DR InParanoid; A8IQT2; -.
DR OrthoDB; 323186at2759; -.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0035082; P:axoneme assembly; IEA:InterPro.
DR InterPro; IPR037386; CCDC40.
DR PANTHER; PTHR16275; PTHR16275; 2.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
KW Flagellum; Methylation.
FT CHAIN 1..576
FT /note="Coiled-coil domain-containing protein 40 homolog"
FT /id="PRO_0000431956"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 33..175
FT /evidence="ECO:0000255"
FT COILED 232..269
FT /evidence="ECO:0000255"
FT COILED 311..397
FT /evidence="ECO:0000255"
FT COMPBIAS 468..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 246
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:24152136"
FT MOD_RES 523
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:24152136"
SQ 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
