ID   RSP3_CHLRE              Reviewed;         516 AA.
AC   P12759;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Flagellar radial spoke protein 3 {ECO:0000305};
GN   Name=RSP3 {ECO:0000303|PubMed:17967944};
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].
RC   STRAIN=21gr / CC-1690;
RX   PubMed=2745550; DOI=10.1083/jcb.109.1.235;
RA   Williams B.D., Velleca M.A., Curry A.M., Rosenbaum J.L.;
RT   "Molecular cloning and sequence analysis of the Chlamydomonas gene coding
RT   for radial spoke protein 3: flagellar mutation pf-14 is an ochre allele.";
RL   J. Cell Biol. 109:235-245(1989).
RN   [2]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH FAP91.
RX   PubMed=17967944; DOI=10.1083/jcb.200703107;
RA   Dymek E.E., Smith E.F.;
RT   "A conserved CaM- and radial spoke associated complex mediates regulation
RT   of flagellar dynein activity.";
RL   J. Cell Biol. 179:515-526(2007).
CC   -!- FUNCTION: Protein 3 may attach the radial spoke to the outer doublet
CC       microtubule or is required to form a stable spoke structure.
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.
CC   -!- SUBUNIT: Interacts with FAP91. {ECO:0000269|PubMed:17967944}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC       {ECO:0000305|PubMed:17967944}. Note=Radial spoke.
CC       {ECO:0000305|PubMed:17967944}.
CC   -!- PTM: Protein 3 is one of the 5 radial spoke proteins that are
CC       phosphorylated.
CC   -!- PTM: Protein 3a might only differ from protein 3 in being
CC       unphosphorylated.
CC   -!- SIMILARITY: Belongs to the flagellar radial spoke RSP3 family.
CC       {ECO:0000305}.
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DR   EMBL; X14549; CAA32685.1; -; Genomic_DNA.
DR   PIR; S05962; A31270.
DR   RefSeq; XP_001695406.1; XM_001695354.1.
DR   PDB; 7JRJ; EM; 3.03 A; G=160-516.
DR   PDB; 7JTK; EM; 3.20 A; E/F=1-516.
DR   PDB; 7JTS; EM; 6.10 A; E/F=1-516.
DR   PDBsum; 7JRJ; -.
DR   PDBsum; 7JTK; -.
DR   PDBsum; 7JTS; -.
DR   AlphaFoldDB; P12759; -.
DR   SMR; P12759; -.
DR   STRING; 3055.EDP01664; -.
DR   PRIDE; P12759; -.
DR   EnsemblPlants; PNW82729; PNW82729; CHLRE_06g291700v5.
DR   GeneID; 5721101; -.
DR   Gramene; PNW82729; PNW82729; CHLRE_06g291700v5.
DR   KEGG; cre:CHLRE_06g291700v5; -.
DR   eggNOG; ENOG502QQSZ; Eukaryota.
DR   HOGENOM; CLU_036980_1_0_1; -.
DR   OMA; TANIMFD; -.
DR   OrthoDB; 1143744at2759; -.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR   GO; GO:0001534; C:radial spoke; IDA:UniProtKB.
DR   GO; GO:2000155; P:positive regulation of cilium-dependent cell motility; IDA:UniProtKB.
DR   InterPro; IPR009290; Radial_spoke_3.
DR   PANTHER; PTHR21648; PTHR21648; 1.
DR   Pfam; PF06098; Radial_spoke_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell projection; Cilium; Cytoplasm; Cytoskeleton; Flagellum;
KW   Phosphoprotein.
FT   CHAIN           1..516
FT                   /note="Flagellar radial spoke protein 3"
FT                   /id="PRO_0000097493"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          60..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          140..143
FT                   /evidence="ECO:0007829|PDB:7JTK"
FT   STRAND          148..151
FT                   /evidence="ECO:0007829|PDB:7JTK"
FT   HELIX           154..260
FT                   /evidence="ECO:0007829|PDB:7JTK"
FT   HELIX           282..352
FT                   /evidence="ECO:0007829|PDB:7JRJ"
FT   HELIX           354..359
FT                   /evidence="ECO:0007829|PDB:7JRJ"
FT   HELIX           370..388
FT                   /evidence="ECO:0007829|PDB:7JRJ"
FT   HELIX           472..482
FT                   /evidence="ECO:0007829|PDB:7JRJ"
FT   HELIX           487..498
FT                   /evidence="ECO:0007829|PDB:7JRJ"
FT   HELIX           500..502
FT                   /evidence="ECO:0007829|PDB:7JTK"
FT   TURN            504..506
FT                   /evidence="ECO:0007829|PDB:7JTK"
SQ   SEQUENCE   516 AA;  56785 MW;  E9288F002C48093F CRC64;
     MVQAKAQQQL YTHAAEPKAV QQRRAKYRED ETTQTLPTAN IMFDRRVVRG NTYAARILPA
     DATQTQTKGP SPASTKKRTT RTLPPRTPEA VDGRRHIDIQ TDVYLEELTD TVPEADTSTQ
     TDAFLDRPPT PLFVPQKTGT DAITQIENGD LFDFDFEVEP ILEVLVGKVL EQGLMEVLEE
     EELAAMRAHQ EHFEQIRNAE LVATQRMEAA ERRKLEEKER RMQQERERVE RERVVRQKVA
     ASAFARGYLS GIVNTVFDRL VSSGYIYDPV MREVETAFMP WLKEQAIGYL ARGVVARRVV
     DKLVEDAAAA LAANRSTLAD KAASTAATVD AWAERQAKME AELQGKELEA VRRRPTFVLR
     ELKPAVASAD AVEAAAAELT AQAEEAANAK WEADKAEAAE KARAEAEAAA EEQKALLEEL
     AATAAAEAEE RGEEPPAEPP SLPDGVEPVD VEAEVAKAVE AVPKPPVKEV TDIDILSYMM
     DKGAITKDAI IQALAVHALG DKAYTNHPAF AEAEGA