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CCD39_MOUSE
ID   CCD39_MOUSE             Reviewed;         937 AA.
AC   Q9D5Y1; B2RSM0; Q8CDG6;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Coiled-coil domain-containing protein 39 {ECO:0000305};
GN   Name=Ccdc39 {ECO:0000312|MGI:MGI:1289263};
GN   Synonyms=D3Ertd789e {ECO:0000312|MGI:MGI:1289263};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888 AND SER-896, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=21131972; DOI=10.1038/ng.726;
RA   Merveille A.C., Davis E.E., Becker-Heck A., Legendre M., Amirav I.,
RA   Bataille G., Belmont J., Beydon N., Billen F., Clement A., Clercx C.,
RA   Coste A., Crosbie R., de Blic J., Deleuze S., Duquesnoy P., Escalier D.,
RA   Escudier E., Fliegauf M., Horvath J., Hill K., Jorissen M., Just J.,
RA   Kispert A., Lathrop M., Loges N.T., Marthin J.K., Momozawa Y.,
RA   Montantin G., Nielsen K.G., Olbrich H., Papon J.F., Rayet I., Roger G.,
RA   Schmidts M., Tenreiro H., Towbin J.A., Zelenika D., Zentgraf H.,
RA   Georges M., Lequarre A.S., Katsanis N., Omran H., Amselem S.;
RT   "CCDC39 is required for assembly of inner dynein arms and the dynein
RT   regulatory complex and for normal ciliary motility in humans and dogs.";
RL   Nat. Genet. 43:72-78(2011).
CC   -!- FUNCTION: Required for assembly of dynein regulatory complex (DRC) and
CC       inner dynein arm (IDA) complexes, which are responsible for ciliary
CC       beat regulation, thereby playing a central role in motility in cilia
CC       and flagella. Probably acts together with CCDC40 to form a molecular
CC       ruler that determines the 96 nanometer (nm) repeat length and
CC       arrangements of components in cilia and flagella. Not required for
CC       outer dynein arm complexes assembly. {ECO:0000250|UniProtKB:A8IQT2,
CC       ECO:0000250|UniProtKB:Q9UFE4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000250|UniProtKB:Q9UFE4}. Note=CCDC40 is required for
CC       localization to axonemes. {ECO:0000250|UniProtKB:Q9UFE4}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in tissues rich in ciliated
CC       cells. Expressed in olfactory and vomeronasal sensory neurons and the
CC       respiratory epithelium. Expressed in node cells carrying motile cilia,
CC       in upper and lower airways, and in ependymal and choroid plexus cells.
CC       {ECO:0000269|PubMed:21131972}.
CC   -!- SIMILARITY: Belongs to the CCDC39 family. {ECO:0000305}.
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DR   EMBL; AK030087; BAC26777.1; -; mRNA.
DR   EMBL; AK014839; BAB29574.1; -; mRNA.
DR   EMBL; CH466530; EDL35029.1; -; Genomic_DNA.
DR   EMBL; BC138917; AAI38918.1; -; mRNA.
DR   EMBL; BC138920; AAI38921.1; -; mRNA.
DR   CCDS; CCDS17304.1; -.
DR   RefSeq; NP_080498.1; NM_026222.2.
DR   AlphaFoldDB; Q9D5Y1; -.
DR   SMR; Q9D5Y1; -.
DR   BioGRID; 206277; 3.
DR   STRING; 10090.ENSMUSP00000029222; -.
DR   iPTMnet; Q9D5Y1; -.
DR   PhosphoSitePlus; Q9D5Y1; -.
DR   MaxQB; Q9D5Y1; -.
DR   PaxDb; Q9D5Y1; -.
DR   PRIDE; Q9D5Y1; -.
DR   ProteomicsDB; 265364; -.
DR   Antibodypedia; 79042; 110 antibodies from 16 providers.
DR   DNASU; 51938; -.
DR   Ensembl; ENSMUST00000029222; ENSMUSP00000029222; ENSMUSG00000027676.
DR   GeneID; 51938; -.
DR   KEGG; mmu:51938; -.
DR   UCSC; uc008oxi.1; mouse.
DR   CTD; 339829; -.
DR   MGI; MGI:1289263; Ccdc39.
DR   VEuPathDB; HostDB:ENSMUSG00000027676; -.
DR   eggNOG; ENOG502QS0D; Eukaryota.
DR   GeneTree; ENSGT00390000015010; -.
DR   HOGENOM; CLU_009793_2_0_1; -.
DR   InParanoid; Q9D5Y1; -.
DR   OMA; LYRTQRQ; -.
DR   OrthoDB; 355514at2759; -.
DR   PhylomeDB; Q9D5Y1; -.
DR   TreeFam; TF329312; -.
DR   BioGRID-ORCS; 51938; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Ccdc39; mouse.
DR   PRO; PR:Q9D5Y1; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9D5Y1; protein.
DR   Bgee; ENSMUSG00000027676; Expressed in spermatocyte and 196 other tissues.
DR   Genevisible; Q9D5Y1; MM.
DR   GO; GO:0097729; C:9+2 motile cilium; EXP:MGI.
DR   GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR   GO; GO:0005929; C:cilium; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:GOC.
DR   GO; GO:0070286; P:axonemal dynein complex assembly; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0090660; P:cerebrospinal fluid circulation; IMP:MGI.
DR   GO; GO:0003341; P:cilium movement; ISO:MGI.
DR   GO; GO:0060285; P:cilium-dependent cell motility; ISS:UniProtKB.
DR   GO; GO:0071907; P:determination of digestive tract left/right asymmetry; ISO:MGI.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR   GO; GO:0071910; P:determination of liver left/right asymmetry; ISO:MGI.
DR   GO; GO:0035469; P:determination of pancreatic left/right asymmetry; ISO:MGI.
DR   GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; ISS:UniProtKB.
DR   GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IMP:MGI.
DR   GO; GO:0061966; P:establishment of left/right asymmetry; IMP:MGI.
DR   GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR   GO; GO:0030317; P:flagellated sperm motility; ISO:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0001947; P:heart looping; ISO:MGI.
DR   GO; GO:0036159; P:inner dynein arm assembly; IMP:MGI.
DR   GO; GO:0030324; P:lung development; ISO:MGI.
DR   GO; GO:0044458; P:motile cilium assembly; ISO:MGI.
DR   GO; GO:0061512; P:protein localization to cilium; IMP:MGI.
DR   GO; GO:0003356; P:regulation of cilium beat frequency; ISO:MGI.
DR   InterPro; IPR033290; CCDC39.
DR   PANTHER; PTHR18962; PTHR18962; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..937
FT                   /note="Coiled-coil domain-containing protein 39"
FT                   /id="PRO_0000234494"
FT   REGION          866..937
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          16..137
FT                   /evidence="ECO:0000255"
FT   COILED          165..339
FT                   /evidence="ECO:0000255"
FT   COILED          365..615
FT                   /evidence="ECO:0000255"
FT   COILED          664..816
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        867..900
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        911..937
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         888
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         896
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        183
FT                   /note="M -> L (in Ref. 1; BAC26777)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        193
FT                   /note="D -> H (in Ref. 1; BAC26777)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   937 AA;  110072 MW;  D8FA9D3A9CC52393 CRC64;
     MCSEFLSELH WEDGFAIPVA NQENKILEDQ LAKLREEKSN LQDQLHDYEE RINSMTSHLK
     NVNQEFLFTQ SLYKARESEI ESEEHFKAIA ERELGRVKNE TQLLEKEMAI IRERKSQMEN
     NIFKTTQKLD DLKCQMNWDQ QALEAWLEES AHKDSDSLTL QKYSQQDDNK IRALTLQLEK
     LTMEYNEKRK LLDSELTETL SAQLELDKAA QDFRKIHLER QELIQQWENT IEQMQRRDQE
     IDNCALALSR IKQEAREKEG VVKEKIKFLE NEVENNIEYE RKISVAERKV SKCRMDYQRH
     EGNRSQLKDE LDTLKTTLNR TSSDLQALRK NISKVKKDIF DETLRLQKLK HHNEVVKHKL
     KMITEKTLSI EEKATNMEDM LKEEEKGLKE VEVQLGIVKD VLFKKVQELQ NEIAKEKALV
     SEIEGTRSSL KHLNKQLHKL DFETLKQQEI MYSQDFYIQQ VERRMSRLKG EINSEEKQAL
     EAKILELKKT MDEKKSTLSL LESQIKKLHN DLYFIKKSNG KNNDEKESLM NKISELNLFI
     DRSEKELSKA KAVKEDMMIE DNLLKLQVKR ARELLYSKAE EVLSLEKRKQ QLGKDMEERA
     EEIKVHKAML TSQIRCVEQQ RKTMSSEFHE RLSKIDKLKN RYEILTVVML PPEGEEEKTQ
     SYYVIKAAQE KEELQREGDS LDAKINKAEK EIYALQNTLQ VLNSCNSNYK QSFKKVTPSS
     DEYALKIQLE EQKRTADERY RCKQRQIREL QEDIQSMENT FEVIGHLANN AKEKLTEKQT
     LAFQLRKETE EQKPKLQRIT KQCGRLRREI RILKQTDNET LEEQDIQLRE IIQFHKDIDQ
     MLVNAMENAE IHAIFKTYFE QNGLELPTAR GPSSRSSSQS SSLSSFRSLE DVTLQSPPTA
     KVIQLRFPEP PPATNDSSRS ASSGSNSNIP KEKKLSK
 
 
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