ID   DRC7_CHLRE              Reviewed;        1159 AA.
AC   A8JAM0;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Dynein regulatory complex subunit 7;
DE   AltName: Full=Coiled-coil domain-containing protein lobo homolog;
DE   AltName: Full=Flagellar-associated protein 50;
DE   Flags: Fragment;
GN   Name=DRC7; Synonyms=FAP50; ORFNames=CHLREDRAFT_177591;
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;
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   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=21289096; DOI=10.1091/mbc.e10-04-0331;
RA   Yang Y., Cochran D.A., Gargano M.D., King I., Samhat N.K., Burger B.P.,
RA   Sabourin K.R., Hou Y., Awata J., Parry D.A., Marshall W.F., Witman G.B.,
RA   Lu X.;
RT   "Regulation of flagellar motility by the conserved flagellar protein
RT   CG34110/Ccdc135/FAP50.";
RL   Mol. Biol. Cell 22:976-987(2011).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE N-DRC COMPLEX,
RP   SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX   PubMed=21700706; DOI=10.1074/jbc.m111.241760;
RA   Lin J., Tritschler D., Song K., Barber C.F., Cobb J.S., Porter M.E.,
RA   Nicastro D.;
RT   "Building blocks of the nexin-dynein regulatory complex in Chlamydomonas
RT   flagella.";
RL   J. Biol. Chem. 286:29175-29191(2011).
RN   [4]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH DRC5, AND
RP   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).
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). Involved
CC       in the regulation of flagellar motility (PubMed:21289096).
CC       {ECO:0000269|PubMed:21289096, ECO:0000269|PubMed:23427265,
CC       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:23427265). Interacts
CC       with DRC5 (PubMed:23427265). {ECO:0000269|PubMed:23427265,
CC       ECO:0000269|PubMed:25411337}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC       {ECO:0000269|PubMed:21289096}. Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000269|PubMed:21700706}. Cytoplasm, cytoskeleton, flagellum
CC       axoneme {ECO:0000269|PubMed:23427265, ECO:0000269|PubMed:25411337}.
CC       Note=Associated with the outer doublet microtubules (OD).
CC       {ECO:0000269|PubMed:21289096}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:21700706}.
CC   -!- SIMILARITY: Belongs to the DRC7 family. {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; DS496150; EDO99088.1; -; Genomic_DNA.
DR   RefSeq; XP_001699034.1; XM_001698982.1.
DR   AlphaFoldDB; A8JAM0; -.
DR   SMR; A8JAM0; -.
DR   STRING; 3055.EDO99088; -.
DR   PaxDb; A8JAM0; -.
DR   PRIDE; A8JAM0; -.
DR   GeneID; 5724586; -.
DR   eggNOG; KOG0379; Eukaryota.
DR   eggNOG; KOG0619; Eukaryota.
DR   HOGENOM; CLU_275527_0_0_1; -.
DR   InParanoid; A8JAM0; -.
DR   OrthoDB; 131133at2759; -.
DR   GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR   GO; GO:0031514; C:motile cilium; IDA:UniProtKB.
DR   Gene3D; 2.120.10.80; -; 1.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR033551; DRC7/lobo.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   PANTHER; PTHR35249; PTHR35249; 5.
DR   Pfam; PF13516; LRR_6; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   SMART; SM00369; LRR_TYP; 5.
DR   SUPFAM; SSF117281; SSF117281; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS51450; LRR; 6.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Flagellum;
KW   Kelch repeat; Leucine-rich repeat; Repeat.
FT   CHAIN           1..>1159
FT                   /note="Dynein regulatory complex subunit 7"
FT                   /id="PRO_0000415788"
FT   REPEAT          21..46
FT                   /note="LRR 1"
FT   REPEAT          51..74
FT                   /note="LRR 2"
FT   REPEAT          75..97
FT                   /note="LRR 3"
FT   REPEAT          99..120
FT                   /note="LRR 4"
FT   REPEAT          121..143
FT                   /note="LRR 5"
FT   REPEAT          144..166
FT                   /note="LRR 6"
FT   REPEAT          168..189
FT                   /note="LRR 7"
FT   REPEAT          190..212
FT                   /note="LRR 8"
FT   REPEAT          214..235
FT                   /note="LRR 9"
FT   REPEAT          309..360
FT                   /note="Kelch 1"
FT   REPEAT          363..413
FT                   /note="Kelch 2"
FT   REPEAT          415..463
FT                   /note="Kelch 3"
FT   REPEAT          465..513
FT                   /note="Kelch 4"
FT   REPEAT          515..571
FT                   /note="Kelch 5"
FT   REGION          827..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1050..1137
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        827..841
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1159
SQ   SEQUENCE   1159 AA;  132548 MW;  700E90C41F814261 CRC64;
     MAEGIGTFGT LSRDVLEERL MEARRTYRLN MGYAGLKQLP PGFVELVKKY NPHITELELS
     SNDLTDLPDE LEEFRYLRIL RLKYNQLKRI PAVVYRLPQL MVFDASGNRI QKVDDAIGHL
     SLLKELDVSG NEITTLPESL STLPKLEVLQ VENNRLELLP ESLGELPGVI KMDLSTNNLR
     YLPASMGQLK KVQRIDVGNN LLTKVPPSMG HLKTLKEFNL RYNHLDDRYK AKVEEGLSKF
     LAFLREEEER ERLEEIERLK PIGTPVGAYL EYRCKAEVGQ VVKTDMGETT VDNRCWIRTG
     HTLTQVGSML LIFGGQLQKD GSTTNDLFWM TMDRMEWHNQ PCKGEKPPPR YNHAACYDEE
     NNRLVVFGGR TAERKRLNDI YFLDLDSWTW FKPSTEGTAP TPREQAVATF WAGSMVLFGG
     HAIGGRTNDL FLLDLGAWQW SQPAFSGTAP SPRQACALCI GHGNLLFVHG GRNNFVLEDL
     HVMDFVSKNW TEIPCEGRVP PPRHSHRITV HRDQLYLLGG LDELGAQSVA MYRVALPAGQ
     QDTYATSKPK WVEWDSELPY NKNRTATLWN GTISIYQLGS NTLGRVNDDD AEKGLDELRP
     KNAKRMRVQH TINTAGKMPR SFTQHSAHEA RVLQYVQDFQ RIFEELYPYR RPLYLTPRNE
     CGVPKFVCTS LRPSQLVYTE LYDLDGASQF VADFLSYEPL EDPLHPPDTL PSPMSALEWR
     AGDSFDMATV LASMLLGVGY NAFVVLGYAP GPVVQNDQRN TDLAATRTGA GAEEEEESGP
     CKFVHAWVMV LPGKREVTEA MFIEPSAGRK DVSYDLSDPT KWEPVFEDRG MRSRADGNAD
     ESETEGGGGL DDGEGVEAEV VPDIPPSWVP KLTIPRDAFD MRCPRHEIFA RFGDCSRWDG
     MVERLVLYAD EERTVVTEIR ETFTRRRDKL RERRVYPQKD TTIEHFNRGS VFALKDILTV
     KNDRRGRKVI QYYTGRDDRL IYISATYAVD PLAPRPQPSA LLEEYSSLLV AEKDCLQWVR
     DGEWEISEII RTRTNQEQNI TLETPYYDIV RIKAEESEEV REKALKALKD RLIERANIIQ
     ARLDEESAAL AKRQQTFHRD RDQMSAAEEE DYERQTEESM FRIHILERRL RRHEEQALHK
     YYELDAKLRA DGRLAALLN