RSP5_CHLRE
ID RSP5_CHLRE Reviewed; 527 AA.
AC Q27YU7; A8IY36;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Flagellar radial spoke protein 5 {ECO:0000303|PubMed:16507594};
DE EC=1.-.-.- {ECO:0000305};
GN Name=RSP5 {ECO:0000303|PubMed:16507594};
GN ORFNames=CHLREDRAFT_190792 {ECO:0000312|EMBL:EDP03020.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055 {ECO:0000312|EMBL:ABC02018.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16507594; DOI=10.1242/jcs.02811;
RA Yang P., Diener D.R., Yang C., Kohno T., Pazour G.J., Dienes J.M.,
RA Agrin N.S., King S.M., Sale W.S., Kamiya R., Rosenbaum J.L., Witman G.B.;
RT "Radial spoke proteins of Chlamydomonas flagella.";
RL J. Cell Sci. 6:1165-1174(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503, and cw92;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [3]
RP METHYLATION AT ARG-191 AND ARG-366.
RX PubMed=24152136; DOI=10.1021/bi4011623;
RA Werner-Peterson R., Sloboda R.D.;
RT "Methylation of structural components of the axoneme occurs during
RT flagellar disassembly.";
RL Biochemistry 52:8501-8509(2013).
CC -!- FUNCTION: Flagellar radial spokes contribute to the regulation of
CC dynein arm activity and thus the pattern of flagellar bending. They
CC consist of a thin stalk, which is attached to the a subfiber of the
CC outer doublet microtubule, and a bulbous head, which is attached to the
CC stalk and appears to interact with the projections from the central
CC pair of microtubules. {ECO:0000305|PubMed:16507594}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC {ECO:0000269|PubMed:16507594}. Note=Radial spoke.
CC {ECO:0000269|PubMed:16507594}.
CC -!- PTM: Asymmetrically dimethylated at Arg-191 and Arg-366 during
CC flagellum resorption. Probably methylated by PRMT1.
CC {ECO:0000269|PubMed:24152136}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP03020.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ298247; ABC02018.1; -; mRNA.
DR EMBL; DS496127; EDP03020.1; ALT_SEQ; Genomic_DNA.
DR PDB; 7JRJ; EM; 3.03 A; H=1-527.
DR PDB; 7JTK; EM; 3.20 A; I/J=1-521.
DR PDBsum; 7JRJ; -.
DR PDBsum; 7JTK; -.
DR AlphaFoldDB; Q27YU7; -.
DR SMR; Q27YU7; -.
DR STRING; 3055.EDP03020; -.
DR iPTMnet; Q27YU7; -.
DR PaxDb; Q27YU7; -.
DR PRIDE; Q27YU7; -.
DR ProMEX; Q27YU7; -.
DR EnsemblPlants; PNW76202; PNW76202; CHLRE_12g544000v5.
DR Gramene; PNW76202; PNW76202; CHLRE_12g544000v5.
DR eggNOG; KOG1575; Eukaryota.
DR HOGENOM; CLU_523131_0_0_1; -.
DR OrthoDB; 1106773at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Flagellum; Methylation; Oxidoreductase.
FT CHAIN 1..527
FT /note="Flagellar radial spoke protein 5"
FT /id="PRO_0000431951"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 101..153
FT /evidence="ECO:0000255"
FT MOD_RES 191
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:24152136"
FT MOD_RES 366
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:24152136"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 98..116
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 127..155
FT /evidence="ECO:0007829|PDB:7JRJ"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 208..225
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 250..268
FT /evidence="ECO:0007829|PDB:7JRJ"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 284..290
FT /evidence="ECO:0007829|PDB:7JRJ"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 369..377
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:7JRJ"
FT TURN 387..391
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:7JRJ"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:7JTK"
FT HELIX 415..425
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 428..444
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 449..458
FT /evidence="ECO:0007829|PDB:7JRJ"
FT TURN 459..461
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:7JRJ"
FT TURN 474..479
FT /evidence="ECO:0007829|PDB:7JRJ"
FT TURN 481..484
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 486..489
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 508..514
FT /evidence="ECO:0007829|PDB:7JRJ"
SQ SEQUENCE 527 AA; 55880 MW; EDF6DEC875E88EEA CRC64;
MSEPGEEPVA APAGPAPDPV LNELYGSERP AVELLPGVPL SPIVNSCWLP ADAKAMLAES
WIPVPPEDAG EEAGPPPPAF EAAAPEYNEL VRRLAKTAPF RKWNELTIQA KQLEQEVAGL
KGPDAEAKQA ELENVKVQIA DAEAAVAEVK QSFSDDPLSL TGWMQALTDL ADGGMTTFEV
SGQGWPYCSL RQLFGEMPSA APPAGFFDGV ERVLGTFKRR YEKERGPGSV QLMLKLAPNV
FSDAWSTGGA PAAVAAVEAY VERARANVFG PDGGVTPEGV PEPLDLVQLV WWDFAAADPL
PVLKALQRMA TDQLQVDEDS GEVSVSEPKK IRGIGLVDFP ADRLKAAIQA GVPITCVQVE
HSVLVRSAQP VLDLCAKYGI KVLARGGTLG GLLSAKYLGA PPPDPVRGDA DLDSVPGCLD
AVNNVGGWAR LQAALAVIKG IADKHGVKPE TVALRWQIDA GCFPLVTTRW SSRVWRQFGY
EGWSSFEVSG GRPGVDGPLF QVESFLDVED VRALAGLAAV HLGPKAG
