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RSH4A_MOUSE
ID   RSH4A_MOUSE             Reviewed;         716 AA.
AC   Q8BYM7; B2RQN0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Radial spoke head protein 4 homolog A;
DE   AltName: Full=Radial spoke head-like protein 3;
GN   Name=Rsph4a; Synonyms=Rshl3;
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 GENOMIC DNA].
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-716.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung;
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   TISSUE SPECIFICITY.
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).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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:32203505). Essential for
CC       triplet radial spokes (RS1, RS2 and RS3) head assembly in the motile
CC       cilia (PubMed:32203505). {ECO:0000269|PubMed:32203505}.
CC   -!- SUBUNIT: Interacts with RSPH6A. {ECO:0000269|PubMed:30185526}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:32203505}.
CC       Note=Radial spoke. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in the trachea, ependymal cells and
CC       oviduct (at protein level) (PubMed:32203505, PubMed:30239614).
CC       Expressed in brain, kidney and testis. {ECO:0000269|PubMed:30239614,
CC       ECO:0000269|PubMed:32203505}.
CC   -!- DISRUPTION PHENOTYPE: Mice show hydrocephalus and the tracheal and
CC       ependymal cell cilia show clockwise rotation motion instead of planar
CC       beating (PubMed:32203505). All three types of radial spoke heads (RS1,
CC       RS2 and RS3) are missing in the tracheal cilia (PubMed:32203505).
CC       {ECO:0000269|PubMed:32203505}.
CC   -!- SIMILARITY: Belongs to the flagellar radial spoke RSP4/6 family.
CC       {ECO:0000305}.
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DR   EMBL; AC153961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC138000; AAI38001.1; -; mRNA.
DR   EMBL; BC138001; AAI38002.1; -; mRNA.
DR   EMBL; AK038980; BAC30192.1; -; mRNA.
DR   CCDS; CCDS48534.1; -.
DR   RefSeq; NP_001156429.1; NM_001162957.1.
DR   PDB; 7DMP; EM; 3.20 A; B/b=1-716.
DR   PDBsum; 7DMP; -.
DR   AlphaFoldDB; Q8BYM7; -.
DR   SMR; Q8BYM7; -.
DR   STRING; 10090.ENSMUSP00000131647; -.
DR   iPTMnet; Q8BYM7; -.
DR   PhosphoSitePlus; Q8BYM7; -.
DR   MaxQB; Q8BYM7; -.
DR   PaxDb; Q8BYM7; -.
DR   PRIDE; Q8BYM7; -.
DR   ProteomicsDB; 256783; -.
DR   Antibodypedia; 32513; 56 antibodies from 11 providers.
DR   Ensembl; ENSMUST00000169670; ENSMUSP00000131647; ENSMUSG00000039552.
DR   GeneID; 212892; -.
DR   KEGG; mmu:212892; -.
DR   UCSC; uc007euh.2; mouse.
DR   CTD; 345895; -.
DR   MGI; MGI:3027894; Rsph4a.
DR   VEuPathDB; HostDB:ENSMUSG00000039552; -.
DR   eggNOG; ENOG502QSU4; Eukaryota.
DR   GeneTree; ENSGT00500000044869; -.
DR   HOGENOM; CLU_021526_1_0_1; -.
DR   InParanoid; Q8BYM7; -.
DR   OMA; AQFQKKM; -.
DR   OrthoDB; 619686at2759; -.
DR   PhylomeDB; Q8BYM7; -.
DR   TreeFam; TF324531; -.
DR   BioGRID-ORCS; 212892; 0 hits in 70 CRISPR screens.
DR   ChiTaRS; Rsph4a; mouse.
DR   PRO; PR:Q8BYM7; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q8BYM7; protein.
DR   Bgee; ENSMUSG00000039552; Expressed in choroid plexus epithelium and 49 other tissues.
DR   Genevisible; Q8BYM7; MM.
DR   GO; GO:0005930; C:axoneme; ISO:MGI.
DR   GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0001534; C:radial spoke; ISS:UniProtKB.
DR   GO; GO:0001535; C:radial spoke head; IMP:MGI.
DR   GO; GO:0035082; P:axoneme assembly; ISO:MGI.
DR   GO; GO:0003341; P:cilium movement; ISO:MGI.
DR   GO; GO:0060294; P:cilium movement involved in cell motility; IEA:InterPro.
DR   GO; GO:0120221; P:maintenance of ciliary planar beating movement pattern; IMP:MGI.
DR   GO; GO:0062177; P:radial spoke 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   3D-structure; Cell projection; Cilium; Cilium biogenesis/degradation;
KW   Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT   CHAIN           1..716
FT                   /note="Radial spoke head protein 4 homolog A"
FT                   /id="PRO_0000313739"
FT   REGION          1..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          668..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..582
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        702..716
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         395
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   HELIX           278..290
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   HELIX           314..324
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   HELIX           332..344
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   TURN            345..348
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          354..358
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          361..363
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          365..370
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          372..374
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          421..424
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          427..438
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   TURN            448..450
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   TURN            453..456
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          463..465
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   HELIX           480..491
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          496..503
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   HELIX           532..537
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          539..544
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   HELIX           596..598
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          607..613
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          618..620
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          623..627
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   TURN            628..632
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          634..637
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   STRAND          642..648
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   TURN            674..676
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   HELIX           684..687
FT                   /evidence="ECO:0007829|PDB:7DMP"
FT   TURN            688..692
FT                   /evidence="ECO:0007829|PDB:7DMP"
SQ   SEQUENCE   716 AA;  80146 MW;  F7C76BEFB1DDEAB8 CRC64;
     MENSTSLKQE KENQEPGEAE RLWQGESDVS PQEPGPPSPE YREEEQRTDT EPAPRMSPSW
     SHQSRVSLST GDLTAGPEVS SSPPPPPLQF HSTPLNTETT QDPVAASPTE KTANGIADTG
     TPYSDPWESS SAAKQSTSHY TSHAEESTFP QSQTPQPDLC GLRDASRNKS KHKGLRFDLL
     QEEGSDSNCD PDQPEVGASE AAQSMLEVAI QNAKAYLLST SSKSGLNLYD HLSKVLTKIL
     DERPADAVDI IENISQDVKM AHFNKKLDTL HNEYEMLPAY EIAETQKALF LQGHLEGADS
     ELEEEMAESS LPNVMESAYY FEQAGVGLGT DETYRVFLAL KQLTDTHPIQ RCRFWGKILG
     LEMNYIVAEV EFRDGEDEEE VEEEGIAEER DNGGSEAGEE EEEELPKSLY KAPQVIPKEE
     SRTGANKYVY FVCNVPGRPW VRLPSVTPAQ IVTARKIKKF FTGRLDAAVI SYPPFPGNES
     NYLRAQIARI SAGTHVSPLG FYQFGEEEGE EEEVEGGRDS YEENPDFEGI QVIDLVESLS
     NWVHHVQYIL PQGRCNWFNP IQKDEDEEEE EEEDEEKGEE PDYIEQEVGP PLLTPISEDL
     GIQNIPSWTT QLSSNLIPQY AIAVLRSNLW PGAYAFSNGK KFENFYIGWG HKYCVENYTP
     PSPPPVYQEY PSGPEITEMN DPSVEEEQAF RMTQEPVALS TEENEGTEDE DEDDED
 
 
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