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ODAD1_MOUSE
ID   ODAD1_MOUSE             Reviewed;         658 AA.
AC   Q3UX62; Q91WT0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Outer dynein arm-docking complex subunit 1;
DE   AltName: Full=Coiled-coil domain-containing protein 114;
GN   Name=Odad1; Synonyms=Ccdc114 {ECO:0000312|MGI:MGI:2446120};
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=Egg;
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 MRNA] OF 173-658.
RC   STRAIN=FVB/N; TISSUE=Colon;
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   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=23261303; DOI=10.1016/j.ajhg.2012.11.002;
RA   Onoufriadis A., Paff T., Antony D., Shoemark A., Micha D., Kuyt B.,
RA   Schmidts M., Petridi S., Dankert-Roelse J.E., Haarman E.G., Daniels J.M.,
RA   Emes R.D., Wilson R., Hogg C., Scambler P.J., Chung E.M., Pals G.,
RA   Mitchison H.M.;
RT   "Splice-Site mutations in the axonemal outer dynein arm docking complex
RT   gene CCDC114 cause primary ciliary dyskinesia.";
RL   Am. J. Hum. Genet. 92:88-98(2013).
CC   -!- FUNCTION: Component of the outer dynein arm-docking complex that
CC       mediates outer dynein arms (ODA) binding onto the doublet microtubule.
CC       Involved in mediating assembly of both ODAs and their axonemal docking
CC       complex onto ciliary microtubules (By similarity).
CC       {ECO:0000250|UniProtKB:F1N2N9, ECO:0000250|UniProtKB:Q96M63}.
CC   -!- SUBUNIT: Component of the outer dynein arm-docking complex along with
CC       ODAD2, ODAD3, ODAD4 and CLXN. Interacts with ODAD3. Interacts with
CC       ODAD4; this interaction may facilitate the recruitment and/or
CC       attachment of outer dynein arm docking complex proteins including
CC       ODAD1, ODAD3, and ODAD4 to ciliary axonemes. Interacts with DNAH9.
CC       Interacts with MNS1 (By similarity). Interacts with PIERCE1 and
CC       PIERCE2; the interactions link the outer dynein arms docking complex
CC       (ODA-DC) to the internal microtubule inner proteins (MIP) in cilium
CC       axoneme (By similarity). {ECO:0000250|UniProtKB:F1N2N9,
CC       ECO:0000250|UniProtKB:Q96M63}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000250|UniProtKB:Q96M63}.
CC   -!- TISSUE SPECIFICITY: Expressed in motile ciliated tissues.
CC       {ECO:0000269|PubMed:23261303}.
CC   -!- SIMILARITY: Belongs to the ODA1/DCC2 family. {ECO:0000305}.
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DR   EMBL; AK135860; BAE22701.1; -; mRNA.
DR   EMBL; BC013491; AAH13491.1; -; mRNA.
DR   RefSeq; NP_001028415.1; NM_001033243.2.
DR   AlphaFoldDB; Q3UX62; -.
DR   SMR; Q3UX62; -.
DR   BioGRID; 229242; 3.
DR   STRING; 10090.ENSMUSP00000042772; -.
DR   iPTMnet; Q3UX62; -.
DR   PhosphoSitePlus; Q3UX62; -.
DR   EPD; Q3UX62; -.
DR   MaxQB; Q3UX62; -.
DR   PaxDb; Q3UX62; -.
DR   PRIDE; Q3UX62; -.
DR   ProteomicsDB; 265576; -.
DR   DNASU; 211535; -.
DR   Ensembl; ENSMUST00000038720; ENSMUSP00000042772; ENSMUSG00000040189.
DR   UCSC; uc009gxz.1; mouse.
DR   MGI; MGI:2446120; Odad1.
DR   VEuPathDB; HostDB:ENSMUSG00000040189; -.
DR   eggNOG; ENOG502QSIU; Eukaryota.
DR   GeneTree; ENSGT00950000183364; -.
DR   HOGENOM; CLU_027546_3_1_1; -.
DR   InParanoid; Q3UX62; -.
DR   OMA; HCDGSMI; -.
DR   OrthoDB; 648380at2759; -.
DR   PhylomeDB; Q3UX62; -.
DR   TreeFam; TF323742; -.
DR   BioGRID-ORCS; 211535; 0 hits in 73 CRISPR screens.
DR   ChiTaRS; Ccdc114; mouse.
DR   PRO; PR:Q3UX62; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q3UX62; protein.
DR   Bgee; ENSMUSG00000040189; Expressed in choroid plexus of lateral ventricle and 81 other tissues.
DR   ExpressionAtlas; Q3UX62; baseline and differential.
DR   Genevisible; Q3UX62; MM.
DR   GO; GO:0005930; C:axoneme; ISO:MGI.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0036157; C:outer dynein arm; ISS:UniProtKB.
DR   GO; GO:0120228; C:outer dynein arm docking complex; ISS:UniProtKB.
DR   GO; GO:0003341; P:cilium movement; ISS:UniProtKB.
DR   GO; GO:0036158; P:outer dynein arm assembly; ISS:UniProtKB.
PE   2: Evidence at transcript level;
KW   Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..658
FT                   /note="Outer dynein arm-docking complex subunit 1"
FT                   /id="PRO_0000288808"
FT   REGION          496..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          11..156
FT                   /evidence="ECO:0000255"
FT   COILED          186..234
FT                   /evidence="ECO:0000255"
FT   COILED          303..380
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        505..525
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..552
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         500
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B1H228"
FT   MOD_RES         506
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B1H228"
FT   MOD_RES         507
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B1H228"
FT   MOD_RES         509
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B1H228"
SQ   SEQUENCE   658 AA;  74120 MW;  2D963762993C48B8 CRC64;
     MMELERRAYS KEVHQRLRKQ VEEIRQLEML RAKLQTQINV AQSQVKRLGD KKHLAEMECL
     LKSRAQVQVE IEALQEQNRA LDKQIQDWET HVLTQSKEAS APDLIMYQKM KIQRRIRILE
     DQLDRVTCHF DIHLVRNAAL REELELLRIE RGRYLNMDRK LKKEIHLLRE MVGALSTSST
     SAYTAREEAK TKMGMLQERA EKELAQSDTE AQILLRQISH LEQLHRFLKL KNDERQPDPR
     VVQKAEQRDW EVSEGLRKTS QEKLVLRYED TLGKLAQLTG ESDPDLLVEK YLELEERNFA
     EFNFINEQNS EIHHLQEEIK EMQEALVSEH ASQDKQRMQQ EQQCKMLQQD VDKMCSESEQ
     LEGRFQVLRG QLEKIKTDIQ VLFDKAKCDS SVIKDLLGVK TYMRDRDIGL FLSTIERRLV
     QLLTVQAFLQ VQNLAPLADA ALLALGQSLQ EPSKKTTPLK PPDTMEDSSG AVIKEDYPMS
     KEELLSQVMK SLQLQDEEES AKKLDSSPSL TLSSPQISLV TVPKHSKKTS VVPESILSHK
     TNRGRGTGSV SHVTFGDSAS AAGPVAMASA SASGAPVSSR SSQGGRGGFK PTSSSSYLGS
     TGYLETSRGR ESTAGGVHSQ SMGSELSRGL SSSSGHASSP APPSRPSSST SKDSRGYN
 
 
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