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CCD39_CHLRE
ID   CCD39_CHLRE             Reviewed;         894 AA.
AC   A8IQE0;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Coiled-coil domain-containing protein 39 {ECO:0000305};
DE   AltName: Full=Flagellar-associated protein 59 {ECO:0000303|PubMed:15998802};
GN   Name=CCDC39; Synonyms=FAP59 {ECO:0000303|PubMed:15998802};
GN   ORFNames=CHLREDRAFT_189109 {ECO:0000312|EMBL:EDP04876.1};
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   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CCDC40/FAP172, DISRUPTION
RP   PHENOTYPE, AND PHOSPHORYLATION.
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 CCDC40/FAP172 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 CCDC40/FAP172. {ECO:0000269|PubMed:25395538}.
CC   -!- INTERACTION:
CC       A8IQE0; A8IQT2: CCDC40; NbExp=2; IntAct=EBI-16127597, EBI-16127612;
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC       {ECO:0000269|PubMed:25395538}.
CC   -!- PTM: Phosphorylated in flagella. {ECO:0000269|PubMed:25395538}.
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 CCDC39 family. {ECO:0000305}.
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DR   EMBL; DS496120; EDP04876.1; -; Genomic_DNA.
DR   RefSeq; XP_001691768.1; XM_001691716.1.
DR   AlphaFoldDB; A8IQE0; -.
DR   SMR; A8IQE0; -.
DR   DIP; DIP-61434N; -.
DR   IntAct; A8IQE0; 1.
DR   STRING; 3055.EDP04876; -.
DR   PaxDb; A8IQE0; -.
DR   PRIDE; A8IQE0; -.
DR   GeneID; 5717298; -.
DR   eggNOG; ENOG502QS0D; Eukaryota.
DR   HOGENOM; CLU_009793_2_0_1; -.
DR   InParanoid; A8IQE0; -.
DR   OrthoDB; 355514at2759; -.
DR   GO; GO:0005930; C:axoneme; IEA:InterPro.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0003341; P:cilium movement; IEA:InterPro.
DR   GO; GO:0036159; P:inner dynein arm assembly; IEA:InterPro.
DR   InterPro; IPR033290; CCDC39.
DR   PANTHER; PTHR18962; PTHR18962; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
KW   Flagellum; Phosphoprotein.
FT   CHAIN           1..894
FT                   /note="Coiled-coil domain-containing protein 39"
FT                   /id="PRO_0000405820"
FT   REGION          844..894
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          32..143
FT                   /evidence="ECO:0000255"
FT   COILED          187..411
FT                   /evidence="ECO:0000255"
FT   COILED          461..609
FT                   /evidence="ECO:0000255"
FT   COILED          647..788
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        846..879
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   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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