RSP2_CHLRE
ID RSP2_CHLRE Reviewed; 738 AA.
AC Q6UBQ3;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Flagellar radial spoke protein 2 {ECO:0000303|PubMed:14871938};
GN Name=RSP2 {ECO:0000303|PubMed:14871938};
GN ORFNames=CHLREDRAFT_186281 {ECO:0000312|EMBL:EDP06497.1};
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:AAQ92371.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-23; 50-59; 288-308;
RP 529-538 AND 644-672, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14871938; DOI=10.1128/ec.3.1.72-81.2004;
RA Yang P., Yang C., Sale W.S.;
RT "Flagellar radial spoke protein 2 is a calmodulin binding protein required
RT for motility in Chlamydomonas reinhardtii.";
RL Eukaryot. Cell 3:72-81(2004).
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 IDENTIFICATION BY MASS SPECTROMETRY.
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 [4]
RP METHYLATION AT ARG-104; ARG-260; ARG-453; ARG-538 AND ARG-615.
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 (PubMed:16507594). Binds calmodulin in a calcium-
CC dependent manner (PubMed:14871938). {ECO:0000269|PubMed:14871938,
CC 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-104, Arg-260, Arg-453, Arg-538
CC and Arg-615 during flagellum resorption. Probably methylated by PRMT1.
CC {ECO:0000269|PubMed:24152136}.
CC -!- DISRUPTION PHENOTYPE: Absence of radial spokes.
CC {ECO:0000269|PubMed:14871938}.
CC -!- MISCELLANEOUS: In-gel analysis assays show kinase-like activity in
CC vitro. However, such activity has not been confirmed using recombinant
CC protein. {ECO:0000305|PubMed:14871938}.
CC -!- SIMILARITY: Belongs to the dpy-30 family. {ECO:0000305}.
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DR EMBL; AY373262; AAQ92371.1; -; mRNA.
DR EMBL; DS496115; EDP06497.1; -; Genomic_DNA.
DR RefSeq; XP_001702718.1; XM_001702666.1.
DR PDB; 7JRJ; EM; 3.03 A; I=1-738.
DR PDB; 7JTK; EM; 3.20 A; C/D=1-738.
DR PDBsum; 7JRJ; -.
DR PDBsum; 7JTK; -.
DR AlphaFoldDB; Q6UBQ3; -.
DR BMRB; Q6UBQ3; -.
DR SMR; Q6UBQ3; -.
DR STRING; 3055.EDP06497; -.
DR iPTMnet; Q6UBQ3; -.
DR PaxDb; Q6UBQ3; -.
DR PRIDE; Q6UBQ3; -.
DR EnsemblPlants; PNW77220; PNW77220; CHLRE_10g427300v5.
DR GeneID; 5728165; -.
DR Gramene; PNW77220; PNW77220; CHLRE_10g427300v5.
DR KEGG; cre:CHLRE_10g427300v5; -.
DR eggNOG; ENOG502R8D2; Eukaryota.
DR HOGENOM; CLU_376161_0_0_1; -.
DR InParanoid; Q6UBQ3; -.
DR OMA; RACSECA; -.
DR OrthoDB; 1328148at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0044666; C:MLL3/4 complex; IEA:InterPro.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR InterPro; IPR007858; Dpy-30_motif.
DR InterPro; IPR037856; Sdc1/DPY30.
DR PANTHER; PTHR23356; PTHR23356; 1.
DR Pfam; PF05186; Dpy-30; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calmodulin-binding; Cell projection; Cilium; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Flagellum; Methylation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:14871938"
FT CHAIN 2..738
FT /note="Flagellar radial spoke protein 2"
FT /id="PRO_0000431953"
FT REGION 134..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..149
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..412
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:24152136"
FT MOD_RES 260
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:24152136"
FT MOD_RES 453
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:24152136"
FT MOD_RES 538
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:24152136"
FT MOD_RES 615
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:24152136"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 36..97
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 103..117
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:7JRJ"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:7JRJ"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 306..332
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 342..359
FT /evidence="ECO:0007829|PDB:7JTK"
FT HELIX 462..474
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 476..484
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 491..503
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:7JTK"
FT HELIX 514..517
FT /evidence="ECO:0007829|PDB:7JRJ"
FT TURN 518..520
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 524..530
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:7JTK"
FT HELIX 540..551
FT /evidence="ECO:0007829|PDB:7JTK"
FT HELIX 556..562
FT /evidence="ECO:0007829|PDB:7JTK"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:7JTK"
FT HELIX 568..609
FT /evidence="ECO:0007829|PDB:7JTK"
SQ SEQUENCE 738 AA; 77363 MW; 506811B4975539AD CRC64;
MAPTQAGHDT AYLKETVGEA LARGCAAAIS AQPNDPVEYL GLWLLKYVKN AEVEGNFYRE
RQQDLQKKKD RLVKEAQSEQ AAKSVALTRK EAADALALVT AEPRELLEAA VKLVKQHTAA
GAAYAAVVAE PEEPDWVAPE DDEAAAVETE DEAAGGAALA EGEEPPPEPE PEPEAAPEDG
EGDAPAPKIP RPVDYSKKYF AYVAASAGQE HVLEADLYRP APPPEDADED FKPEPLPYSF
RVLDEKLPML YVPNVAAEER VKFFRKFPKI GSYQACGVAL PASGEFKALL AADTLFPEGS
GQPLSADDRD FVWEVSQSLS RALEAVQARA AEALAATSAA EAVEELKAKV AELREQAAAE
AAAAAPPPPA EGEEGEGEAP PAEEEPPAEE EAEEEEEEAE EGAEEGAEEG EEGEEAPPKP
KKKKKVFNPI PGLQAAIEKL TAAAEAATEA DARAQAAVAL EKQALDEVVA LASSHSDATL
SSLRNMLSVP QGTYHVVKAL LHLLGRPAAS FSTWKRAHSH FSPRLFEDMA AYDATAERDM
AVWGRVRSCY KAAPAAKKLD AEMPNTLFGS VALMYIKQVR RVARKAVLQR ELAAKLAKAQ
QDLADKQAAL VEAERVKAER EAEEARLAAE AEAAAAAEAE AAARAAAEAE AAAAAEAAAE
AAAEAAAAAA EAAAEAGEGE AVAEREAAPA EAEAAPAEGE AAPPAEGEGE AQPAQEGSNS
SSSSSDSSSS EESKAAAE
