ID   RSPH9_MOUSE             Reviewed;         276 AA.
AC   Q9D9V4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Radial spoke head protein 9 homolog;
GN   Name=Rsph9;
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 MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
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=19200523; DOI=10.1016/j.ajhg.2009.01.011;
RA   Castleman V.H., Romio L., Chodhari R., Hirst R.A., de Castro S.C.P.,
RA   Parker K.A., Ybot-Gonzalez P., Emes R.D., Wilson S.W., Wallis C.,
RA   Johnson C.A., Herrera R.J., Rutman A., Dixon M., Shoemark A., Bush A.,
RA   Hogg C., Gardiner R.M., Reish O., Greene N.D.E., O'Callaghan C., Purton S.,
RA   Chung E.M.K., Mitchison H.M.;
RT   "Mutations in radial spoke head protein genes RSPH9 and RSPH4A cause
RT   primary ciliary dyskinesia with central-microtubular-pair abnormalities.";
RL   Am. J. Hum. Genet. 84:197-209(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   INTERACTION WITH RSPH6A, AND SUBCELLULAR LOCATION.
RX   PubMed=30185526; DOI=10.1242/jcs.221648;
RA   Abbasi F., Miyata H., Shimada K., Morohoshi A., Nozawa K., Matsumura T.,
RA   Xu Z., Pratiwi P., Ikawa M.;
RT   "RSPH6A is required for sperm flagellum formation and male fertility in
RT   mice.";
RL   J. Cell Sci. 131:0-0(2018).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=30383886; DOI=10.1111/boc.201800060;
RA   Zhu L., Liu H., Chen Y., Yan X., Zhu X.;
RT   "Rsph9 is critical for ciliary radial spoke assembly and central pair
RT   microtubule stability.";
RL   Biol. Cell 111:29-38(2019).
RN   [7]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=32203505; DOI=10.1371/journal.pgen.1008664;
RA   Yoke H., Ueno H., Narita A., Sakai T., Horiuchi K., Shingyoji C.,
RA   Hamada H., Shinohara K.;
RT   "Rsph4a is essential for the triplet radial spoke head assembly of the
RT   mouse motile cilia.";
RL   PLoS Genet. 16:e1008664-e1008664(2020).
CC   -!- FUNCTION: Component of the axonemal radial spoke head which plays an
CC       important role in ciliary motility (PubMed:30383886). Essential for
CC       both the radial spoke head assembly and the central pair microtubule
CC       stability in ependymal motile cilia (PubMed:30383886). Required for
CC       motility of olfactory and neural cilia and for the structural integrity
CC       of ciliary axonemes in both 9+0 and 9+2 motile cilia (By similarity).
CC       {ECO:0000250|UniProtKB:Q5TYW6, ECO:0000269|PubMed:30383886}.
CC   -!- SUBUNIT: Interacts with RSPH6A. {ECO:0000269|PubMed:30185526}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000269|PubMed:30383886, ECO:0000305,
CC       ECO:0000305|PubMed:32203505}. Cell projection, cilium, flagellum
CC       {ECO:0000269|PubMed:30185526}. Cell projection, kinocilium
CC       {ECO:0000250|UniProtKB:Q5TYW6}. Note=Radial spoke. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in the testis, trachea, lung and oviduct
CC       (at protein level). {ECO:0000269|PubMed:30383886,
CC       ECO:0000269|PubMed:32203505}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the embryonic node at 7.5 dpc and in
CC       the nasal, lung, tracheal and brain ventricle epithelium at 18.5-19.5
CC       dpc. {ECO:0000269|PubMed:19200523}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated depletion in the ependymal cilia
CC       results in a near complete central pair apparatus loss and alters the
CC       ciliary beat pattern from planar to rotational (PubMed:30383886).
CC       Multiple radial spokes proteins, including those in the head, are
CC       markedly down-regulated in the cilia (PubMed:30383886).
CC       {ECO:0000269|PubMed:30383886}.
CC   -!- SIMILARITY: Belongs to the flagellar radial spoke RSP9 family.
CC       {ECO:0000305}.
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DR   EMBL; AK006440; BAB24590.1; -; mRNA.
DR   EMBL; BC019423; AAH19423.1; -; mRNA.
DR   CCDS; CCDS28820.1; -.
DR   RefSeq; NP_083614.1; NM_029338.3.
DR   PDB; 7DMP; EM; 3.20 A; C/c=1-276.
DR   PDBsum; 7DMP; -.
DR   AlphaFoldDB; Q9D9V4; -.
DR   SMR; Q9D9V4; -.
DR   STRING; 10090.ENSMUSP00000024762; -.
DR   PhosphoSitePlus; Q9D9V4; -.
DR   MaxQB; Q9D9V4; -.
DR   PaxDb; Q9D9V4; -.
DR   PRIDE; Q9D9V4; -.
DR   ProteomicsDB; 262714; -.
DR   Antibodypedia; 30558; 80 antibodies from 17 providers.
DR   DNASU; 75564; -.
DR   Ensembl; ENSMUST00000024762; ENSMUSP00000024762; ENSMUSG00000023966.
DR   GeneID; 75564; -.
DR   KEGG; mmu:75564; -.
DR   UCSC; uc008crt.1; mouse.
DR   CTD; 221421; -.
DR   MGI; MGI:1922814; Rsph9.
DR   VEuPathDB; HostDB:ENSMUSG00000023966; -.
DR   eggNOG; ENOG502QR99; Eukaryota.
DR   GeneTree; ENSGT00390000018686; -.
DR   HOGENOM; CLU_068343_1_0_1; -.
DR   InParanoid; Q9D9V4; -.
DR   OMA; HGYIYIG; -.
DR   OrthoDB; 978175at2759; -.
DR   PhylomeDB; Q9D9V4; -.
DR   TreeFam; TF323644; -.
DR   BioGRID-ORCS; 75564; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Rsph9; mouse.
DR   PRO; PR:Q9D9V4; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q9D9V4; protein.
DR   Bgee; ENSMUSG00000023966; Expressed in spermatid and 162 other tissues.
DR   ExpressionAtlas; Q9D9V4; baseline and differential.
DR   Genevisible; Q9D9V4; MM.
DR   GO; GO:0097729; C:9+2 motile cilium; ISO:MGI.
DR   GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR   GO; GO:0060091; C:kinocilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0031514; C:motile cilium; IDA:UniProtKB.
DR   GO; GO:1904158; P:axonemal central apparatus assembly; IMP:UniProtKB.
DR   GO; GO:0035082; P:axoneme assembly; IGI:BHF-UCL.
DR   GO; GO:0003341; P:cilium movement; IGI:BHF-UCL.
DR   GO; GO:0060294; P:cilium movement involved in cell motility; IBA:GO_Central.
DR   GO; GO:0044458; P:motile cilium assembly; IBA:GO_Central.
DR   GO; GO:0062177; P:radial spoke assembly; IMP:UniProtKB.
PE   1: Evidence at protein level;
KW   3D-structure; Cell projection; Cilium; Cilium biogenesis/degradation;
KW   Cytoplasm; Cytoskeleton; Flagellum; Reference proteome.
FT   CHAIN           1..276
FT                   /note="Radial spoke head protein 9 homolog"
FT                   /id="PRO_0000089562"
FT   HELIX           6..8
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          15..17
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   TURN            22..24
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   HELIX           25..38
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          44..48
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          59..62
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          72..75
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          77..81
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   HELIX           90..95
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          105..108
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   HELIX           136..148
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   TURN            156..158
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          163..165
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   HELIX           178..180
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          182..184
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          188..191
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          226..232
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          237..244
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          247..251
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          253..255
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          259..262
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   HELIX           272..275
FT                   /evidence="ECO:0007829|PDB:7DMP"
SQ   SEQUENCE   276 AA;  31331 MW;  5C9D9B8679CE4750 CRC64;
     MDADSLLLSL ELASGSGQGL SPDRRASLLT SLMLVKRDYR FARVLFWGRI LGLVADYYIA
     QGLSEDQLAP RKTLYSLNCT EWSLLPPATE EMAMQISVVS GRFMGDPSHE YEHTELQKVN
     EGEKVFDEEV VVQIKEETRL VSIIDQIDKA VAIIPRGALF KTPFGVTHVN RTFEGLPLSE
     VRKLSSYFHF REAIDLKNKT LLEKSDLEPS LDFLDSLEYD IPRGSWSIQM ERGNALVVLR
     SLLWPGLTFY HAPRTKNYGY IYVGTGEKNM DLPFML