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Coiled-coil domain-containing protein 39 (Flagellar-associated protein 59)

 CCD39_CHLRE             Reviewed;         894 AA.
A8IQE0;
08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 1.
16-JAN-2019, entry version 35.
RecName: Full=Coiled-coil domain-containing protein 39 {ECO:0000305};
AltName: Full=Flagellar-associated protein 59 {ECO:0000303|PubMed:15998802};
Name=CCDC39; Synonyms=FAP59 {ECO:0000303|PubMed:15998802};
ORFNames=CHLREDRAFT_189109 {ECO:0000312|EMBL:EDP04876.1};
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]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CCDC40/FAP172,
DISRUPTION PHENOTYPE, AND PHOSPHORYLATION.
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
CCDC40/FAP172 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 CCDC40/FAP172.
{ECO:0000269|PubMed:25395538}.
-!- INTERACTION:
A8IQT2:CCDC40; NbExp=2; IntAct=EBI-16127597, EBI-16127612;
-!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
{ECO:0000269|PubMed:25395538}.
-!- PTM: Phosphorylated in flagella. {ECO:0000269|PubMed:25395538}.
-!- 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 CCDC39 family. {ECO:0000305}.
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EMBL; DS496120; EDP04876.1; -; Genomic_DNA.
RefSeq; XP_001691768.1; XM_001691716.1.
SMR; A8IQE0; -.
DIP; DIP-61434N; -.
IntAct; A8IQE0; 1.
STRING; 3055.EDP04876; -.
PaxDb; A8IQE0; -.
PRIDE; A8IQE0; -.
GeneID; 5717298; -.
KEGG; cre:CHLREDRAFT_189109; -.
eggNOG; ENOG410IHS4; Eukaryota.
eggNOG; ENOG410ZNZ9; LUCA.
InParanoid; A8IQE0; -.
OrthoDB; 355514at2759; -.
GO; GO:0005930; C:axoneme; IBA:GO_Central.
GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
GO; GO:0003341; P:cilium movement; IBA:GO_Central.
GO; GO:0060285; P:cilium-dependent cell motility; IBA:GO_Central.
GO; GO:0036159; P:inner dynein arm assembly; IBA:GO_Central.
InterPro; IPR033290; CCDC39.
PANTHER; PTHR18962; PTHR18962; 1.
1: Evidence at protein level;
Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
Flagellum; Phosphoprotein.
CHAIN 1 894 Coiled-coil domain-containing protein 39.
/FTId=PRO_0000405820.
COILED 32 143 {ECO:0000255}.
COILED 187 411 {ECO:0000255}.
COILED 461 609 {ECO:0000255}.
COILED 647 788 {ECO:0000255}.
SEQUENCE 894 AA; 101488 MW; 2E0A53532FA9E717 CRC64;
MANIDPYRTE EELVEDDEEV DMSFLPPFAK GTENEVLYVE NARMERRLER TERALETNMD
RLHIMDEHLK NVQQELKYTQ TRVEAKNKEI ESEKHLNAMA EREMGRLKKD IGKMEAERQE
LADKINGLQN QIYKNNEKLD QFKMLMNWNQ EELEQWALAE RQKAEDNAAL EKYRHADDGK
VKELTLALER VSKQVVGRKE ELEAEVVETQ AAQIQLDKAA EDFRKLHVER QDLIRQWEEA
VEAMRHRDAA IAAASEQFAM QKDVLRERKR ELDAQARFLE NETLNTKEAD ARVAYYEREV
GKQRDVLARE QARTEELNNQ VELVKATLSK AATELAQRTV ENKQAREDLD AKRQKLDAAR
KRFVVLKRKL ENEFGNLDSM EAKASELEAM RRGEEARLKA ILKEHELLKK EQYKRSQVLF
DLRQKERELI SEISGGQGQN KNLAARIHAL DEQVVARAGG VRSEEETRAL NARIEKLTAI
LEGVKRAEDD LLAARRANTS LRADRAKLDE TISTLKLEND MVSRQVKGSV EAREKALVDH
DVLALEVKRL RDILAAHADE VFSLENRKQQ LALSMEERKQ EVEVHRDGLR AELRLLREDV
HRITLELKER LLRCEKLQAK FEIISAKHRG SGEDDGEERT QAYYVIKAAQ EREALQREGD
DLDGRIRVAE KEVAALEATL AQLMAVNTNF AASYKKVGSK EAFEERAALR DKLDKAYDKL
KARRADEAAI AGDIQVSEAR LSNLGQEQRS LQALVDDMTR RKAEAQRQLD EQREKLGRAL
GRTDKLRQKL GLANSPQGAD VELAEVRDVT RAMLLELKAL ALANPGAMIA EACEAAGIRL
PSGGSNPPSL GGSRPGSARS QTSLGSVRSA RSVASQQRGG MGGSPAVRTI QLGA


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Pathways :
WP1689: Porphyrin and chlorophyll metabolism
WP2272: Pathogenic Escherichia coli infection
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism

Related Genes :
[CCDC39] Coiled-coil domain-containing protein 39
[CHCHD10 C22orf16] Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial (Protein N27C7-4)
[CHCHD6 CHCM1 MIC25] MICOS complex subunit MIC25 (Coiled-coil-helix cristae morphology protein 1) (Coiled-coil-helix-coiled-coil-helix domain-containing protein 6)
[GCC2 KIAA0336 RANBP2L4] GRIP and coiled-coil domain-containing protein 2 (185 kDa Golgi coiled-coil protein) (GCC185) (CLL-associated antigen KW-11) (CTCL tumor antigen se1-1) (Ran-binding protein 2-like 4) (RanBP2L4) (Renal carcinoma antigen NY-REN-53)
[SPDL1 CCDC99] Protein Spindly (hSpindly) (Arsenite-related gene 1 protein) (Coiled-coil domain-containing protein 99) (Rhabdomyosarcoma antigen MU-RMS-40.4A) (Spindle apparatus coiled-coil domain-containing protein 1)
[Calcoco1 CocoA Kiaa1536] Calcium-binding and coiled-coil domain-containing protein 1 (Coiled-coil coactivator protein)
[CCDC39 FAP59 CHLREDRAFT_189109] Coiled-coil domain-containing protein 39 (Flagellar-associated protein 59)
[CALCOCO1 KIAA1536 PP13275 UNQ2436/PRO4996] Calcium-binding and coiled-coil domain-containing protein 1 (Calphoglin) (Coiled-coil coactivator protein) (Sarcoma antigen NY-SAR-3)
[BECN1 GT197] Beclin-1 (Coiled-coil myosin-like BCL2-interacting protein) (Protein GT197) [Cleaved into: Beclin-1-C 35 kDa; Beclin-1-C 37 kDa]
[CCDC40 FAP172 CHLREDRAFT_170513] Coiled-coil domain-containing protein 40 homolog (Flagellar-associated protein 172)
[CALCOCO2 NDP52] Calcium-binding and coiled-coil domain-containing protein 2 (Antigen nuclear dot 52 kDa protein) (Nuclear domain 10 protein NDP52) (Nuclear domain 10 protein 52) (Nuclear dot protein 52)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[FYCO1 ZFYVE7] FYVE and coiled-coil domain-containing protein 1 (Zinc finger FYVE domain-containing protein 7)
[CCDC40 KIAA1640] Coiled-coil domain-containing protein 40
[Rock1] Rho-associated protein kinase 1 (EC 2.7.11.1) (Rho-associated, coiled-coil-containing protein kinase 1) (Rho-associated, coiled-coil-containing protein kinase I) (ROCK-I) (p160 ROCK-1) (p160ROCK)
[ABRAXAS1 ABRA1 CCDC98 FAM175A UNQ496/PRO1013] BRCA1-A complex subunit Abraxas 1 (Coiled-coil domain-containing protein 98) (Protein FAM175A)
[ROCK1] Rho-associated protein kinase 1 (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-35) (Rho-associated, coiled-coil-containing protein kinase 1) (Rho-associated, coiled-coil-containing protein kinase I) (ROCK-I) (p160 ROCK-1) (p160ROCK)
[MORC2 KIAA0852 ZCWCC1] ATPase MORC2 (EC 3.6.1.3) (MORC family CW-type zinc finger protein 2) (Zinc finger CW-type coiled-coil domain protein 1)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[CCHCR1 C6orf18 HCR] Coiled-coil alpha-helical rod protein 1 (Alpha-helical coiled-coil rod protein) (Putative gene 8 protein) (Pg8)
[CHCHD3 MIC19 MINOS3] MICOS complex subunit MIC19 (Coiled-coil-helix-coiled-coil-helix domain-containing protein 3)
[Chchd3 Mic19] MICOS complex subunit Mic19 (Coiled-coil-helix-coiled-coil-helix domain-containing protein 3)
[CCDC88B BRLZ] Coiled-coil domain-containing protein 88B (Brain leucine zipper domain-containing protein) (Gipie) (Hook-related protein 3) (HkRP3)
[SGF29 CCDC101] SAGA-associated factor 29 (Coiled-coil domain-containing protein 101) (SAGA complex-associated factor 29)
[CEP83 CCDC41] Centrosomal protein of 83 kDa (Cep83) (Coiled-coil domain-containing protein 41) (Renal carcinoma antigen NY-REN-58)
[MCU C10orf42 CCDC109A] Calcium uniporter protein, mitochondrial (HsMCU) (Coiled-coil domain-containing protein 109A)
[APP A4 AD1] Amyloid-beta precursor protein (APP) (ABPP) (APPI) (Alzheimer disease amyloid protein) (Amyloid precursor protein) (Amyloid-beta A4 protein) (Cerebral vascular amyloid peptide) (CVAP) (PreA4) (Protease nexin-II) (PN-II) [Cleaved into: N-APP; Soluble APP-alpha (S-APP-alpha); Soluble APP-beta (S-APP-beta); C99 (Beta-secretase C-terminal fragment) (Beta-CTF); Amyloid-beta protein 42 (Abeta42) (Beta-APP42); Amyloid-beta protein 40 (Abeta40) (Beta-APP40); C83 (Alpha-secretase C-terminal fragment) (Alpha-CTF); P3(42); P3(40); C80; Gamma-secretase C-terminal fragment 59 (Amyloid intracellular domain 59) (AICD-59) (AID(59)) (Gamma-CTF(59)); Gamma-secretase C-terminal fragment 57 (Amyloid intracellular domain 57) (AICD-57) (AID(57)) (Gamma-CTF(57)); Gamma-secretase C-terminal fragment 50 (Amyloid intracellular domain 50) (AICD-50) (AID(50)) (Gamma-CTF(50)); C31]
[CCDC151] Coiled-coil domain-containing protein 151
[WAC KIAA1844] WW domain-containing adapter protein with coiled-coil
[Pre C,C C core E PC pre-C pre-C/C PreC preC PreC/C preC/C precore-core HBVgp4] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)

Bibliography :
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