DRC2_CHLRE
ID DRC2_CHLRE Reviewed; 573 AA.
AC A8JB22;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 2.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Dynein regulatory complex subunit 2 {ECO:0000303|PubMed:25411337};
DE AltName: Full=Coiled-coil domain-containing protein 65 homolog;
DE AltName: Full=Flagellar-associated protein 250 {ECO:0000303|PubMed:15998802};
GN Name=DRC2 {ECO:0000303|PubMed:25411337};
GN Synonyms=CCDC65, FAP250 {ECO:0000303|PubMed:15998802};
GN ORFNames=CHLREDRAFT_106450 {ECO:0000312|EMBL:EDO98958.1};
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 [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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15998802; DOI=10.1083/jcb.200504008;
RA Pazour G.J., Agrin N., Leszyk J., Witman G.B.;
RT "Proteomic analysis of a eukaryotic cilium.";
RL J. Cell Biol. 170:103-113(2005).
RN [3]
RP METHYLATION AT ARG-96 AND ARG-142.
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).
RN [4]
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 [5]
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 [6]
RP FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
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 (PubMed:23427265, PubMed:25411337). Plays a
CC critical role in the assembly of N-DRC and also stabilizes the assembly
CC of multiple inner dynein arms and radial spokes. Coassembles with DRC1
CC to form a central scaffold needed for assembly of the N-DRC and its
CC attachment to the outer doublet microtubules (PubMed:29167384).
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, flagellum basal body
CC {ECO:0000269|PubMed:29167384}. Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:29167384}. Cytoplasm, cytoskeleton, flagellum
CC axoneme {ECO:0000269|PubMed:23427265, ECO:0000269|PubMed:25411337}.
CC -!- PTM: Asymmetrically dimethylated at Arg-96 and Arg-142 during flagellum
CC resorption. Probably methylated by PRMT1.
CC {ECO:0000269|PubMed:24152136}.
CC -!- DISRUPTION PHENOTYPE: Defects in DRC2 give the ida6 and sup-pf5
CC phenotypes characterized by reduced swimming speed, disruption of the
CC assembly of several other N-DRC subunits and destabilization of the
CC assembly of several closely associated structures such as the inner
CC dynein arms and the radial spokes. {ECO:0000269|PubMed:29167384}.
CC -!- SIMILARITY: Belongs to the DRC2 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDO98958.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS496151; EDO98958.1; ALT_SEQ; Genomic_DNA.
DR PDB; 7JU4; EM; 3.40 A; 2=1-573.
DR PDBsum; 7JU4; -.
DR AlphaFoldDB; A8JB22; -.
DR SMR; A8JB22; -.
DR iPTMnet; A8JB22; -.
DR PaxDb; A8JB22; -.
DR EnsemblPlants; PNW74416; PNW74416; CHLRE_13g607750v5.
DR Gramene; PNW74416; PNW74416; CHLRE_13g607750v5.
DR eggNOG; ENOG502QQDD; Eukaryota.
DR HOGENOM; CLU_026536_1_0_1; -.
DR InParanoid; A8JB22; -.
DR OMA; QNHERDV; -.
DR OrthoDB; 815240at2759; -.
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-SubCell.
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; Flagellum; Methylation.
FT CHAIN 1..573
FT /note="Dynein regulatory complex subunit 2"
FT /id="PRO_0000431954"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 15..231
FT /evidence="ECO:0000255"
FT COILED 258..359
FT /evidence="ECO:0000255"
FT COILED 470..501
FT /evidence="ECO:0000255"
FT MOD_RES 96
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:24152136"
FT MOD_RES 142
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:24152136"
SQ SEQUENCE 573 AA; 64885 MW; 59BC1F8AD000484A CRC64;
MVKAGKKVKG ASKVRENETE EEKKIRLEME ALAADEAERK AQEAARVALR ERQLREQRYA
HLNGIKIHNQ WRKIMRMAKV EELRREIEIL SQNHEREVDR KDAIMQMLDR DLEEAEEQYS
LAVRSHMLVV DNLLDLQYQR MRALEAEFAA DLKALEDEFE TERTEIVNAH TRQRKDMGDM
IAAMEGEFAD AEAELRQEYE AQREEIKNRN SEEYNVLKIQ LEGIIEELEK SFELAHRAYL
ESTEHRTNTF RTLTKDDAKA ALKIERQMRK LVRLQEALQH WRTKIATNGR EWEERNRALR
NEKEIMARHY AKLKSSMDAF RAGQAERLKQ LSLASSGAME TLRGKLAVAE NVLKLAELAR
KYETEQEKVL PFWNPAQAVP SGEQGDEEAA AQAEAEAAAL EPSAAELGEL GLRASMPEDS
SKEAPGPSKS SAGPGKPKFS SYGLDPSSGS EVDEWDYLNC FFRRYNKALL DKTAIDKEKS
RLERENADLR SILKQYLDGI SVNDDVLNNP VNPLLVVNNR LQITLTERNK ARAAAMAQRA
AAATGAGLSV TGQGAGGGGQ KQLVEVQVVS RVS
