RSP6_CHLRE
ID RSP6_CHLRE Reviewed; 459 AA.
AC Q01657;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Flagellar radial spoke protein 6;
GN Name=RSP6;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=1508197; DOI=10.1128/mcb.12.9.3967-3977.1992;
RA Curry A.M., Williams B.D., Rosenbaum J.L.;
RT "Sequence analysis reveals homology between two proteins of the flagellar
RT radial spoke.";
RL Mol. Cell. Biol. 12:3967-3977(1992).
RN [2]
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 [3]
RP METHYLATION AT ARG-267 AND ARG-398.
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:0000269|PubMed:1508197}.
CC -!- SUBUNIT: The radial spoke head is made of five different polypeptides
CC (RSP1, RSP4, RSP6, RSP9, and RSP10). {ECO:0000269|PubMed:1508197}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC {ECO:0000269|PubMed:1508197}. Note=Radial spoke.
CC {ECO:0000269|PubMed:1508197}.
CC -!- PTM: Asymmetrically dimethylated at Arg-267 and Arg-398 during
CC flagellum resorption. Probably methylated by PRMT1.
CC {ECO:0000269|PubMed:24152136}.
CC -!- SIMILARITY: Belongs to the flagellar radial spoke RSP4/6 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M87526; AAA33093.1; -; Genomic_DNA.
DR PIR; B44498; B44498.
DR RefSeq; XP_001700729.1; XM_001700677.1.
DR PDB; 7JR9; EM; 2.95 A; D=1-459.
DR PDB; 7JRJ; EM; 3.03 A; D=1-459.
DR PDB; 7JTK; EM; 3.20 A; K/L=1-459.
DR PDBsum; 7JR9; -.
DR PDBsum; 7JRJ; -.
DR PDBsum; 7JTK; -.
DR AlphaFoldDB; Q01657; -.
DR SMR; Q01657; -.
DR STRING; 3055.EDP06983; -.
DR iPTMnet; Q01657; -.
DR EnsemblPlants; PNW83461; PNW83461; CHLRE_05g242550v5.
DR GeneID; 5726278; -.
DR Gramene; PNW83461; PNW83461; CHLRE_05g242550v5.
DR KEGG; cre:CHLRE_05g242550v5; -.
DR eggNOG; ENOG502QSU4; Eukaryota.
DR HOGENOM; CLU_021526_0_0_1; -.
DR OMA; LPNVNEI; -.
DR OrthoDB; 619686at2759; -.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR GO; GO:0001534; C:radial spoke; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; IEA:InterPro.
DR GO; GO:0060294; P:cilium movement involved in cell motility; IEA:InterPro.
DR InterPro; IPR006802; Radial_spoke.
DR PANTHER; PTHR13159; PTHR13159; 2.
DR Pfam; PF04712; Radial_spoke; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cilium; Cytoplasm; Cytoskeleton; Flagellum;
KW Methylation.
FT CHAIN 1..459
FT /note="Flagellar radial spoke protein 6"
FT /id="PRO_0000097495"
FT REGION 309..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 267
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:24152136"
FT MOD_RES 398
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:24152136"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:7JRJ"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:7JTK"
FT HELIX 23..36
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:7JR9"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:7JRJ"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:7JR9"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:7JR9"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 147..156
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 163..172
FT /evidence="ECO:0007829|PDB:7JR9"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 195..203
FT /evidence="ECO:0007829|PDB:7JR9"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:7JTK"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:7JR9"
FT HELIX 247..262
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:7JR9"
FT HELIX 290..294
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:7JRJ"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:7JR9"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:7JTK"
FT STRAND 381..388
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 391..398
FT /evidence="ECO:0007829|PDB:7JR9"
FT STRAND 400..406
FT /evidence="ECO:0007829|PDB:7JR9"
SQ SEQUENCE 459 AA; 48846 MW; CF1DAC577B803517 CRC64;
MAADVGQALA FLQQVKTTQG ASIYEGLKAA LAKVLEDRPV NAVEALETSV LSTPPAANLS
VPLVPAASAA AAAAAVAKAS LFGDPEPVLD PESGEPIDPD APNEFECEDV EGDGDLLDGL
GVGLGRQEMY AAMLAVKRLG EDAKRGVSTV RFFGKFFGTQ ADYYVFETTL QSNPDMPEAP
EGTIPLEPYG EGVNAYIYFV SNTLGGPLQQ LPYVTPEQIK ASRLLRRYLT GRLDAPVSAF
PAFPGNEANY LRALIARISA ATVCCPRGFF TADDDSAELS ANDEWVPLKG REMALPVNWS
HRYAHLKGQG RTVTHKRDPP DEEEEPEKNF WTAEEMEAGP PPLATLDTDA PLPAATGDKV
PPPAWSPVFA SASVTTRNQV AGVRSNRWPG AVCACAGRHF TSMYVGWGIK AGGEWSPCPP
PPPVPQWGAP AAGVEGGQQL LLECNDLPPK PAPPEEEDE
