DRC4_CHLRE
ID DRC4_CHLRE Reviewed; 471 AA.
AC Q7XJ96; A8J6Z3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Dynein regulatory complex subunit 4 {ECO:0000303|PubMed:25411337};
DE AltName: Full=Growth arrest-specific protein 8 homolog;
DE AltName: Full=Protein PF2;
GN Name=DRC4 {ECO:0000303|PubMed:25411337}; Synonyms=GAS8, PF2;
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, SUBUNIT, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=12847082; DOI=10.1083/jcb.200303019;
RA Rupp G., Porter M.E.;
RT "A subunit of the dynein regulatory complex in Chlamydomonas is a homologue
RT of a growth arrest-specific gene product.";
RL J. Cell Biol. 162:47-57(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
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 FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION
RP WITH DRC1; DRC2 AND DRC5, VARIANT SUP-PF3A 96-VAL--GLN-151 DEL, VARIANT
RP SUP-PF3B 96-VAL--GLN-127 DEL, 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 [4]
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 [5]
RP MUTAGENESIS OF ASP-198, AND SUBCELLULAR LOCATION.
RX PubMed=27472056; DOI=10.1371/journal.pgen.1006220;
RA Lewis W.R., Malarkey E.B., Tritschler D., Bower R., Pasek R.C.,
RA Porath J.D., Birket S.E., Saunier S., Antignac C., Knowles M.R.,
RA Leigh M.W., Zariwala M.A., Challa A.K., Kesterson R.A., Rowe S.M.,
RA Drummond I.A., Parant J.M., Hildebrandt F., Porter M.E., Yoder B.K.,
RA Berbari N.F.;
RT "Mutation of growth arrest specific 8 reveals a role in motile cilia
RT function and human disease.";
RL PLoS Genet. 12:E1006220-E1006220(2016).
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:12847082, PubMed:23427265,
CC PubMed:25411337). Plays an important role in the assembly of the N-DRC
CC linker (PubMed:23427265). {ECO:0000269|PubMed:12847082,
CC ECO:0000269|PubMed:23427265, ECO:0000269|PubMed:25411337}.
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:25411337, PubMed:12847082,
CC PubMed:23427265). Interacts with DRC1, DRC2 and DRC5 (PubMed:23427265).
CC {ECO:0000269|PubMed:12847082, ECO:0000269|PubMed:23427265,
CC ECO:0000269|PubMed:25411337}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:12847082,
CC ECO:0000269|PubMed:23427265, ECO:0000269|PubMed:25411337,
CC ECO:0000269|PubMed:27472056}. Cytoplasm, cytoskeleton, flagellum basal
CC body {ECO:0000269|PubMed:12847082, ECO:0000269|PubMed:23427265}.
CC -!- DISRUPTION PHENOTYPE: Defects in DRC4 give the pf2 phenotype
CC characterized by disruption of the assembly of several other N-DRC
CC subunits and an altered waveform that results in slow swimming cells.
CC {ECO:0000269|PubMed:12847082, ECO:0000269|PubMed:23427265}.
CC -!- SIMILARITY: Belongs to the DRC4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDP00235.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY309088; AAP57169.1; -; Genomic_DNA.
DR EMBL; AY309087; AAP57169.1; JOINED; Genomic_DNA.
DR EMBL; DS496140; EDP00235.1; ALT_SEQ; Genomic_DNA.
DR PDB; 7JU4; EM; 3.40 A; 0/4=1-471.
DR PDBsum; 7JU4; -.
DR AlphaFoldDB; Q7XJ96; -.
DR SMR; Q7XJ96; -.
DR EnsemblPlants; PNW76803; PNW76803; CHLRE_11g476850v5.
DR Gramene; PNW76803; PNW76803; CHLRE_11g476850v5.
DR eggNOG; ENOG502QQDA; Eukaryota.
DR HOGENOM; CLU_045343_0_0_1; -.
DR OMA; SWEHEVL; -.
DR OrthoDB; 1257437at2759; -.
DR GO; GO:0097729; C:9+2 motile cilium; IMP:GO_Central.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0070286; P:axonemal dynein complex assembly; IMP:UniProtKB.
DR GO; GO:0060294; P:cilium movement involved in cell motility; IMP:GO_Central.
DR GO; GO:0051179; P:localization; IEA:UniProt.
DR InterPro; IPR039308; GAS8.
DR InterPro; IPR025593; GAS8_dom.
DR PANTHER; PTHR31543; PTHR31543; 1.
DR Pfam; PF13851; GAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Flagellum; Microtubule.
FT CHAIN 1..471
FT /note="Dynein regulatory complex subunit 4"
FT /id="PRO_0000306333"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..239
FT /evidence="ECO:0000255"
FT COILED 282..425
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 96..151
FT /note="Missing (in sup-pf3a; reduced swimming speed;
FT defective assembly of N-DRC)"
FT /evidence="ECO:0000269|PubMed:23427265"
FT VARIANT 96..127
FT /note="Missing (in sup-pf3b; reduced swimming speed;
FT defective assembly of N-DRC)"
FT /evidence="ECO:0000269|PubMed:23427265"
FT MUTAGEN 198
FT /note="D->K: Subtle defect in swim velocity."
FT /evidence="ECO:0000269|PubMed:27472056"
SQ SEQUENCE 471 AA; 55108 MW; 6B974D05A69936C5 CRC64;
MAPKKKGTKK ESKKDAVATG DIEGASVEEL NQKIGTLEKE KNKEEEYRNY MQLERDKINA
FWEITKKDLE DRRAELRNKD REMEEMEERH QVEIKVYKQK VKHLLYEHQN NITTLKSDGE
LALKLQQDEY RKREGDLGKD KRNLKLELKE QELAHQDIIR QLKLEHAKEI TKLRQEFEQQ
AKDLQSKYEK KMKMLRDDME LRRKQEIHEI EERKNTHINE LMKKHERAFA EIKNYYNDIT
HNNLDLIKTL KEDVAEMKRR EAANEKLMYE IAQDNKKLSE PLSRALKEVE LLRQQLANYD
KDKLSLAQTK ARLLNAERQI KNLEWENEVL SQRFSKVQTE RDELYGKFEA SIYDVQQKTG
LKSALLEKKV EALGEALEMK EAQLAEVLTA ANLDPGTLAA INQRLEEVLD NKNQIIKALQ
YDVAKVSKAH NDLIRVYEAK LTEFGIPVDE LGFRPLVTNT STGPAGLVVG A
