DRC1_CHLRE
ID DRC1_CHLRE Reviewed; 698 AA.
AC P0DL09; L7PCP1;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Dynein regulatory complex protein 1;
GN Name=DRC1;
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 [MRNA], PROTEIN SEQUENCE OF 186-196 AND 238-251,
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23354437; DOI=10.1038/ng.2533;
RA Wirschell M., Olbrich H., Werner C., Tritschler D., Bower R., Sale W.S.,
RA Loges N.T., Pennekamp P., Lindberg S., Stenram U., Carlen B., Horak E.,
RA Kohler G., Nurnberg P., Nurnberg G., Porter M.E., Omran H.;
RT "The nexin-dynein regulatory complex subunit DRC1 is essential for motile
RT cilia function in algae and humans.";
RL Nat. Genet. 45:262-268(2013).
RN [2]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH DRC4 AND DRC5,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23427265; DOI=10.1091/mbc.e12-11-0801;
RA Bower R., Tritschler D., Vanderwaal K., Perrone C.A., Mueller J., Fox L.,
RA Sale W.S., Porter M.E.;
RT "The N-DRC forms a conserved biochemical complex that maintains outer
RT doublet alignment and limits microtubule sliding in motile axonemes.";
RL Mol. Biol. Cell 24:1134-1152(2013).
RN [3]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=25411337; DOI=10.1091/mbc.e14-09-1367;
RA Oda T., Yanagisawa H., Kikkawa M.;
RT "Detailed structural and biochemical characterization of the nexin-dynein
RT regulatory complex.";
RL Mol. Biol. Cell 26:294-304(2015).
RN [4]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=29167384; DOI=10.1091/mbc.e17-08-0510;
RA Bower R., Tritschler D., Mills K.V., Heuser T., Nicastro D., Porter M.E.;
RT "DRC2/CCDC65 is a central hub for assembly of the nexin-dynein regulatory
RT complex and other regulators of ciliary and flagellar motility.";
RL Mol. Biol. Cell 29:137-153(2018).
CC -!- FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC) a
CC key regulator of ciliary/flagellar motility which maintains the
CC alignment and integrity of the distal axoneme and regulates microtubule
CC sliding in motile axonemes. Plays a critical role in the assembly of N-
CC DRC and also stabilizes the assembly of multiple inner dynein arms and
CC radial spokes. Coassembles with DRC2 to form a central scaffold needed
CC for assembly of the N-DRC and its attachment to the outer doublet
CC microtubules (PubMed:23427265, PubMed:25411337, PubMed:29167384,
CC PubMed:23354437). {ECO:0000269|PubMed:23354437,
CC ECO:0000269|PubMed:23427265, ECO:0000269|PubMed:25411337,
CC ECO:0000269|PubMed:29167384}.
CC -!- SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC),
CC composed of at least DRC1, DRC2, DRC3, DRC4, DRC5, DRC6, DRC7, DRC8,
CC DRC9, DRC10 and DRC11 (PubMed:23427265, PubMed:25411337,
CC PubMed:29167384). Interacts with DRC4 and DRC5 (PubMed:23427265).
CC {ECO:0000269|PubMed:23427265, ECO:0000269|PubMed:25411337,
CC ECO:0000269|PubMed:29167384}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:23354437}. Cytoplasm, cytoskeleton, flagellum
CC axoneme {ECO:0000269|PubMed:23427265, ECO:0000269|PubMed:25411337,
CC ECO:0000269|PubMed:29167384}.
CC -!- DISRUPTION PHENOTYPE: Defects in DRC1 give the pf3 phenotype
CC characterized by reduced swimming speed and abnormal ciliary waveform
CC characterized by reduced shear amplitude. Severe defects in assembly of
CC the N-DRC and several inner-arm structures seen.
CC {ECO:0000269|PubMed:23354437, ECO:0000269|PubMed:29167384}.
CC -!- SIMILARITY: Belongs to the DRC1 family. {ECO:0000305}.
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DR EMBL; JX311620; AFU81554.1; -; mRNA.
DR PDB; 7JU4; EM; 3.40 A; 1=1-698.
DR PDBsum; 7JU4; -.
DR AlphaFoldDB; P0DL09; -.
DR SMR; P0DL09; -.
DR GO; GO:0005858; C:axonemal dynein complex; IEA:InterPro.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR GO; GO:0070286; P:axonemal dynein complex assembly; IMP:UniProtKB.
DR InterPro; IPR039505; DRC1/2_N.
DR InterPro; IPR039750; DRC1/DRC2.
DR InterPro; IPR029440; DRC1_C.
DR PANTHER; PTHR21625; PTHR21625; 1.
DR Pfam; PF14772; NYD-SP28; 1.
DR Pfam; PF14775; NYD-SP28_assoc; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Flagellum.
FT CHAIN 1..698
FT /note="Dynein regulatory complex protein 1"
FT /id="PRO_0000421992"
FT REGION 27..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 183..367
FT /evidence="ECO:0000255"
FT COILED 655..685
FT /evidence="ECO:0000255"
SQ SEQUENCE 698 AA; 79331 MW; 2AA1D74EB4C5290B CRC64;
MDELQSQTER EARILARRKR IQERLAALRE GDHGGGKEGE NKEEIGKGKQ QIIESKRRLM
RVKYRTDQDV SSVRVAGDDR ENQHRIQEEQ TRQDLRAKLL AEAEQSARQN AAVAMRWADL
FSIEVPQDLY NEIESQRQAC ERIIASKDKL IGEIKGELKK KDDEFVKTLK RQAEDIDTLL
QYMSRQFVEV QNAYKEELDE IENAFLQERS DLLESNRREM QELFDKRSRL EQDFMDRYLA
AVEAYQSQLE GHRQMDAEEY HILKIRLETD IQNLEQHLEA MRATYQLNTE KLEYNYRVLK
EREKENTQTI ESQKKKLSRQ RDILSSLKQR YAETDRRYRD DNMKLTDEYK RITEQFKDLQ
SKFRHFELVD TKKYKEVWGM KEADVAALVR QLLQADKVLH EQQLGWDWRP PDDAVFAPVH
GDAGSGGGAA AAATGGAAGG AAAAGGVGPN GEEESEEDAA ARVREAELAE RLRDGRNWGA
LGLLCDEAGF LIDIKARNMI ERLPKDEQGQ VKAEAILRSL GIADGSAFDA LLEALSADSN
IELRAKGMVA PQGRGMAEEK SDRGGTAVLV HPDEAVRRLK AFVEVYGTGP SRGPGGGGGG
GGGMSGPMRV QGAMRRAAER EQEFWSRMTH VISDKHTRVW GALEKQLEKY LALLQERAGS
LRDVESLQHQ NNELRALLNQ YLSSRINDEL QIPPTQII
