ID RSPH1_MOUSE Reviewed; 301 AA.
AC Q8VIG3; Q9DAL5;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 27-MAR-2024, entry version 146.
DE RecName: Full=Radial spoke head 1 homolog;
DE AltName: Full=Male meiotic metaphase chromosome-associated acidic protein;
DE AltName: Full=Meichroacidin;
DE AltName: Full=Testis-specific gene A2 protein;
GN Name=Rsph1; Synonyms=Tsga2;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Testis;
RX PubMed=9578619; DOI=10.1006/dbio.1998.8885;
RA Tsuchida J., Nishina Y., Wakabayashi N., Nozaki M., Sakai Y., Nishimune Y.;
RT "Molecular cloning and characterization of meichroacidin (male meiotic
RT metaphase chromosome-associated acidic protein).";
RL Dev. Biol. 197:67-76(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 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.
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 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).
RN [7]
RP FUNCTION, IDENTIFICATION IN RADIAL SPOKE COMPLEX 1, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=36417862; DOI=10.1016/j.celrep.2022.111683;
RA Zhang X., Xiao Z., Zhang J., Xu C., Liu S., Cheng L., Zhou S., Zhao S.,
RA Zhang Y., Wu J., Wang Y., Liu M.;
RT "Differential requirements of IQUB for the assembly of radial spoke 1 and
RT the motility of mouse cilia and flagella.";
RL Cell Rep. 41:111683-111683(2022).
RN [8] {ECO:0007744|PDB:7DMP}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN RADIAL SPOKE COMPLEX 1 AND RADIAL SPOKE COMPLEX 2, INTERACTION WITH
RP RSPH3B; RSPH4A AND RSPH6A, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=34871179; DOI=10.1073/pnas.2021180118;
RA Zheng W., Li F., Ding Z., Liu H., Zhu L., Xu C., Li J., Gao Q., Wang Y.,
RA Fu Z., Peng C., Yan X., Zhu X., Cong Y.;
RT "Distinct architecture and composition of mouse axonemal radial spoke head
RT revealed by cryo-EM.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:e2021180118-e2021180118(2021).
CC -!- FUNCTION: Functions as part of axonemal radial spoke complexes that
CC play an important part in the motility of sperm and cilia.
CC {ECO:0000269|PubMed:34871179, ECO:0000269|PubMed:36417862,
CC ECO:0000269|PubMed:9578619}.
CC -!- SUBUNIT: Component of the axonemal radial spoke 1 (RS1) and 2 (RS2)
CC complexes, at least composed of spoke head proteins RSPH1, RSPH3, RSPH9
CC and the cilia-specific component RSPH4A or sperm-specific component
CC RSPH6A, spoke stalk proteins RSPH14, DNAJB13, DYDC1, ROPN1L and NME5,
CC and the RS1 complex-specific anchor protein IQUB (PubMed:36417862,
CC PubMed:34871179). Interacts with RSPH3B (PubMed:34871179). Interacts
CC with RSPH4A (PubMed:34871179). Interacts with RSPH6A (PubMed:30185526,
CC PubMed:34871179). {ECO:0000269|PubMed:30185526,
CC ECO:0000269|PubMed:34871179, ECO:0000269|PubMed:36417862}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9578619}.
CC Chromosome {ECO:0000269|PubMed:9578619}. Cytoplasm, cytoskeleton,
CC cilium axoneme {ECO:0000269|PubMed:32203505,
CC ECO:0000269|PubMed:34871179}. Cytoplasm, cytoskeleton, flagellum
CC axoneme {ECO:0000269|PubMed:36417862}. Note=Cytoplasmic in late
CC spermatocytes, secondary spermatocytes and round spermatids. Gathered
CC around metaphase chromosomes during meiotic divisions.
CC {ECO:0000269|PubMed:9578619}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VIG3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VIG3-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Expressed in the trachea, ependymal cells, oviduct
CC and ependymal cells (at protein level) (PubMed:32203505,
CC PubMed:34871179). Germ cell specific. Specifically expressed in testis,
CC and to a lower extent in ovary. Not expressed in somatic tissues
CC (PubMed:9578619). {ECO:0000269|PubMed:32203505,
CC ECO:0000269|PubMed:34871179, ECO:0000269|PubMed:9578619}.
CC -!- DEVELOPMENTAL STAGE: During male germ cell development it is not
CC detected until 12 days. Significant expression is detected from 14-day-
CC old through to adult testis. Expression is first detected in the
CC pachytene spermatocytes at stage V, becomes stronger from the late
CC pachytene spermatocytes to round spermatid stage, and then gradually
CC decreases as the morphogenesis proceeds further. Not expressed in germ
CC cells located in the first layer of the seminiferous epithelium
CC (spermatogonia, leptotene and zygotene spermatocytes).
CC {ECO:0000269|PubMed:9578619}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB83693.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB006535; BAB83693.1; ALT_FRAME; mRNA.
DR EMBL; AK005739; BAB24214.1; -; mRNA.
DR EMBL; BC049584; AAH49584.1; -; mRNA.
DR CCDS; CCDS28604.1; -. [Q8VIG3-1]
DR RefSeq; NP_079566.1; NM_025290.3. [Q8VIG3-1]
DR PDB; 7DMP; EM; 3.20 A; A/a=1-301.
DR PDBsum; 7DMP; -.
DR AlphaFoldDB; Q8VIG3; -.
DR EMDB; EMD-30766; -.
DR SMR; Q8VIG3; -.
DR BioGRID; 204343; 1.
DR ComplexPortal; CPX-8161; Radial spoke complex, ciliiar variant.
DR ComplexPortal; CPX-8162; Radial spoke complex, flagellar variant.
DR STRING; 10090.ENSMUSP00000024832; -.
DR iPTMnet; Q8VIG3; -.
DR PhosphoSitePlus; Q8VIG3; -.
DR REPRODUCTION-2DPAGE; Q8VIG3; -.
DR EPD; Q8VIG3; -.
DR MaxQB; Q8VIG3; -.
DR PaxDb; 10090-ENSMUSP00000024832; -.
DR ProteomicsDB; 256938; -. [Q8VIG3-1]
DR Antibodypedia; 9520; 70 antibodies from 25 providers.
DR DNASU; 22092; -.
DR Ensembl; ENSMUST00000024832.9; ENSMUSP00000024832.8; ENSMUSG00000024033.11. [Q8VIG3-1]
DR GeneID; 22092; -.
DR KEGG; mmu:22092; -.
DR UCSC; uc008buu.1; mouse. [Q8VIG3-1]
DR AGR; MGI:1194909; -.
DR CTD; 89765; -.
DR MGI; MGI:1194909; Rsph1.
DR VEuPathDB; HostDB:ENSMUSG00000024033; -.
DR eggNOG; KOG0231; Eukaryota.
DR GeneTree; ENSGT00940000157240; -.
DR HOGENOM; CLU_032017_2_0_1; -.
DR InParanoid; Q8VIG3; -.
DR OMA; IYEGAWF; -.
DR OrthoDB; 120475at2759; -.
DR PhylomeDB; Q8VIG3; -.
DR TreeFam; TF329346; -.
DR BioGRID-ORCS; 22092; 3 hits in 78 CRISPR screens.
DR ChiTaRS; Rsph1; mouse.
DR PRO; PR:Q8VIG3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8VIG3; Protein.
DR Bgee; ENSMUSG00000024033; Expressed in seminiferous tubule of testis and 152 other cell types or tissues.
DR ExpressionAtlas; Q8VIG3; baseline and differential.
DR Genevisible; Q8VIG3; MM.
DR GO; GO:0097729; C:9+2 motile cilium; IDA:UniProtKB.
DR GO; GO:0005930; C:axoneme; IDA:MGI.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0072687; C:meiotic spindle; IDA:MGI.
DR GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001520; C:outer dense fiber; IDA:MGI.
DR GO; GO:0001534; C:radial spoke; IDA:UniProtKB.
DR GO; GO:0001535; C:radial spoke head; IDA:UniProtKB.
DR GO; GO:0120336; C:radial spoke head 1; IDA:MGI.
DR GO; GO:0120338; C:radial spoke head 3; IDA:MGI.
DR GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR GO; GO:0035082; P:axoneme assembly; ISS:UniProtKB.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IC:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; IC:UniProtKB.
DR GO; GO:0007618; P:mating; IC:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 2.
DR InterPro; IPR003409; MORN.
DR PANTHER; PTHR43215; RADIAL SPOKE HEAD 1 HOMOLOG; 1.
DR PANTHER; PTHR43215:SF14; RADIAL SPOKE HEAD 1 HOMOLOG; 1.
DR Pfam; PF02493; MORN; 7.
DR SMART; SM00698; MORN; 6.
DR SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Chromosome; Cilium;
KW Cytoplasm; Cytoskeleton; Flagellum; Meiosis; Reference proteome; Repeat.
FT CHAIN 1..301
FT /note="Radial spoke head 1 homolog"
FT /id="PRO_0000065663"
FT REPEAT 20..43
FT /note="MORN 1"
FT REPEAT 44..66
FT /note="MORN 2"
FT REPEAT 67..89
FT /note="MORN 3"
FT REPEAT 90..112
FT /note="MORN 4"
FT REPEAT 113..135
FT /note="MORN 5"
FT REPEAT 159..181
FT /note="MORN 6"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 39
FT /note="P -> S (in Ref. 1; BAB83693)"
FT /evidence="ECO:0000305"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:7DMP"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:7DMP"
SQ SEQUENCE 301 AA; 34181 MW; 704ABEFB94DFC90E CRC64;
MSDLGSEELE EEGENDLGEY EGERNEVGER HGHGKARLPN GDTYEGSYEF GKRHGQGTYK
FKNGARYTGD YVKNKKHGQG TFIYPDGSRY EGEWADDQRH GQGVYYYVNN DTYTGEWFNH
QRHGQGTYLY AETGSKYVGT WVHGQQEGAA ELIHLNHRYQ GKFMNKNPVG PGKYVFDIGC
EQHGEYRLTD TERGEEEEEE ETLVNIVPKW KALNITELAL WTPTLSEEQP PPEGQGQEEP
QGLTGVGDPS EDIQAEGFEG ELEPRGADED VDTFRQESQE NSYDIDQGNL NFDEEPSDLQ
D
//
