RSH6A_MOUSE
ID RSH6A_MOUSE Reviewed; 708 AA.
AC Q8CDR2; Q99MM8; Q99MM9;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Radial spoke head protein 6 homolog A {ECO:0000305};
DE AltName: Full=Radial spoke head-like protein 1;
GN Name=Rsph6a {ECO:0000312|MGI:MGI:1927643}; Synonyms=Rshl1;
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], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/10; TISSUE=Testis;
RX PubMed=11237735; DOI=10.1006/bbrc.2001.4465;
RA Eriksson M., Ansved T., Anvret M., Carey N.;
RT "A mammalian radial spokehead-like gene, RSHL1, at the myotonic dystrophy-1
RT locus.";
RL Biochem. Biophys. Res. Commun. 281:835-841(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
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 [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 FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP INTERACTION WITH RSPH1; RSPH4A; RSPH9 AND RSPH10B, DEVELOPMENTAL STAGE, AND
RP ALTERNATIVE SPLICING.
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, TISSUE SPECIFICITY, PHOSPHORYLATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=30239614; DOI=10.1093/biolre/ioy202;
RA Paudel B., Gervasi M.G., Porambo J., Caraballo D.A., Tourzani D.A.,
RA Mager J., Platt M.D., Salicioni A.M., Visconti P.E.;
RT "Sperm capacitation is associated with phosphorylation of the testis-
RT specific radial spoke protein Rsph6.";
RL Biol. Reprod. 100:440-454(2019).
CC -!- FUNCTION: Essential for sperm flagellar assembly and male fertility.
CC {ECO:0000269|PubMed:30185526, ECO:0000269|PubMed:30239614}.
CC -!- SUBUNIT: Interacts with RSPH1, RSPH4A, RSPH9 and RSPH10B.
CC {ECO:0000269|PubMed:30185526}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:30185526, ECO:0000269|PubMed:30239614}. Cytoplasm,
CC cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:30239614}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CDR2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CDR2-2; Sequence=VSP_060558;
CC -!- TISSUE SPECIFICITY: Expressed in testis (at protein level).
CC {ECO:0000269|PubMed:11237735, ECO:0000269|PubMed:30185526,
CC ECO:0000269|PubMed:30239614}.
CC -!- DEVELOPMENTAL STAGE: First detected during the haploid phase of
CC spermatogenesis when secondary spermatocytes begin to appear at about
CC postnatal day 18 (PubMed:30185526). Expression is maintained in mature
CC sperm (PubMed:30239614). {ECO:0000269|PubMed:30185526,
CC ECO:0000269|PubMed:30239614}.
CC -!- PTM: Phosphorylated by PKA. Phosphorylation increases in capacitated
CC sperm. {ECO:0000269|PubMed:30239614}.
CC -!- DISRUPTION PHENOTYPE: Male mutant mice are infertile. Mutant
CC spermatozoa exhibit shorter tails, misshapen heads and immotility.
CC Manchette removal is impaired. {ECO:0000269|PubMed:30185526}.
CC -!- SIMILARITY: Belongs to the flagellar radial spoke RSP4/6 family.
CC {ECO:0000305}.
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DR EMBL; AF329192; AAK19323.1; -; mRNA.
DR EMBL; AF329191; AAK19322.1; -; mRNA.
DR EMBL; AC170864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK029699; BAC26571.1; -; mRNA.
DR CCDS; CCDS20887.1; -. [Q8CDR2-1]
DR CCDS; CCDS52052.1; -. [Q8CDR2-2]
DR RefSeq; NP_001153143.1; NM_001159671.1. [Q8CDR2-2]
DR RefSeq; NP_112545.2; NM_031255.2. [Q8CDR2-1]
DR AlphaFoldDB; Q8CDR2; -.
DR SMR; Q8CDR2; -.
DR STRING; 10090.ENSMUSP00000046526; -.
DR PhosphoSitePlus; Q8CDR2; -.
DR PaxDb; Q8CDR2; -.
DR PRIDE; Q8CDR2; -.
DR ProteomicsDB; 260995; -. [Q8CDR2-1]
DR ProteomicsDB; 329144; -.
DR Antibodypedia; 49254; 37 antibodies from 12 providers.
DR DNASU; 83434; -.
DR Ensembl; ENSMUST00000035521; ENSMUSP00000046526; ENSMUSG00000040866. [Q8CDR2-1]
DR Ensembl; ENSMUST00000076887; ENSMUSP00000076153; ENSMUSG00000040866. [Q8CDR2-2]
DR GeneID; 83434; -.
DR KEGG; mmu:83434; -.
DR UCSC; uc009fkj.2; mouse. [Q8CDR2-1]
DR UCSC; uc012faw.1; mouse.
DR CTD; 81492; -.
DR MGI; MGI:1927643; Rsph6a.
DR VEuPathDB; HostDB:ENSMUSG00000040866; -.
DR eggNOG; ENOG502QSU4; Eukaryota.
DR GeneTree; ENSGT00500000044869; -.
DR HOGENOM; CLU_021526_2_1_1; -.
DR InParanoid; Q8CDR2; -.
DR OMA; HGPYMRD; -.
DR OrthoDB; 619686at2759; -.
DR PhylomeDB; Q8CDR2; -.
DR TreeFam; TF324531; -.
DR BioGRID-ORCS; 83434; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8CDR2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8CDR2; protein.
DR Bgee; ENSMUSG00000040866; Expressed in seminiferous tubule of testis and 9 other tissues.
DR ExpressionAtlas; Q8CDR2; baseline and differential.
DR Genevisible; Q8CDR2; MM.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; ISA:MGI.
DR GO; GO:0001534; C:radial spoke; IEA:InterPro.
DR GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR GO; GO:0035082; P:axoneme assembly; IBA:GO_Central.
DR GO; GO:0003341; P:cilium movement; IBA:GO_Central.
DR GO; GO:0060294; P:cilium movement involved in cell motility; IEA:InterPro.
DR GO; GO:1905199; P:manchette disassembly; IMP:UniProtKB.
DR GO; GO:0044458; P:motile cilium assembly; IMP:UniProtKB.
DR InterPro; IPR006802; Radial_spoke.
DR PANTHER; PTHR13159; PTHR13159; 1.
DR Pfam; PF04712; Radial_spoke; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium; Cytoplasm; Cytoskeleton;
KW Flagellum; Reference proteome.
FT CHAIN 1..708
FT /note="Radial spoke head protein 6 homolog A"
FT /id="PRO_0000312761"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..708
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 287..542
FT /note="VTDSPVPNIMETAFYFEQAGVGLSSDESFRIFLALKQLVEQQPIHMCRFWGK
FT ILGLSRSYLVAEVEFREGEEEGEEEEVEEMMEGGEVLETHGEEEGEEDEEKVVDSVPKP
FT QWKPPPIIPKEESRSGTNKYLYFVCNEPGRPWTRLPHVTPAQIVCARKIKKFFTGFLDT
FT PVISYPPFPGNEANYLRAQIARISAATHISPLGFYQFGEEEGDEEEEGGAGRDSFEENP
FT DFEGIPVLELVDSMANWVHHTQHILPQ -> V (in isoform 2)"
FT /id="VSP_060558"
FT CONFLICT 221
FT /note="I -> L (in Ref. 1; AAK19323)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="E -> K (in Ref. 1; AAK19323)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 708 AA; 80202 MW; 467FD78288CEF1A5 CRC64;
MGEPPPNPDP SQTRRASQGS ERARSQEYSQ PLLTIPEDGL NRPPPQRGSR SSQGSQDLQG
TGLPHWPQRS SLVPDVQGDE GTEYHQSMPL GYTPGFPMEF SQQGYLDDSR MMEQFPQGQD
LLEQLESTYQ GSASGILGQL NLYPREDEIF SQDTQHGPYL RDDPSLHLRP SDLGFMPIVG
EVPDPEPREL AIQNAKAYLL RTSMSCNLSL YEHLVNLLTK ILNQRPEDPL SILESLNRTM
QWEWFHPKLD TLRDDPEMQP TYEMAEKQKA LFIRGGGEGE QEMEEEVTDS PVPNIMETAF
YFEQAGVGLS SDESFRIFLA LKQLVEQQPI HMCRFWGKIL GLSRSYLVAE VEFREGEEEG
EEEEVEEMME GGEVLETHGE EEGEEDEEKV VDSVPKPQWK PPPIIPKEES RSGTNKYLYF
VCNEPGRPWT RLPHVTPAQI VCARKIKKFF TGFLDTPVIS YPPFPGNEAN YLRAQIARIS
AATHISPLGF YQFGEEEGDE EEEGGAGRDS FEENPDFEGI PVLELVDSMA NWVHHTQHIL
PQGRCTWVNP LQKTEEEEEL GEEEEKADEA MEEVEQEVGP PLLTPLSEDA EIMHLSPWTT
RLSCSLSPQY SVAIVRSNLW PGAYAYATGK KFENIYIGWG HKYSPENFNP MLPALIQQEY
PSGPEITEMS DPTVEEEQAL KAAQEQALAA AEEEEEDEEE EEDEDLED
