ID   DRC1_MOUSE              Reviewed;         753 AA.
AC   Q3USS3; B9EKF0;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Dynein regulatory complex protein 1;
DE   AltName: Full=Coiled-coil domain-containing protein 164;
GN   Name=Drc1; Synonyms=Ccdc164, Gm1060;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   DEVELOPMENTAL STAGE.
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).
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 CCDC65/DRC2 to form a central scaffold
CC       needed for assembly of the N-DRC and its attachment to the outer
CC       doublet microtubules. {ECO:0000250|UniProtKB:P0DL09,
CC       ECO:0000250|UniProtKB:Q96MC2}.
CC   -!- SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC).
CC       {ECO:0000250|UniProtKB:P0DL09}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000250|UniProtKB:P0DL09}. Cytoplasm, cytoskeleton, flagellum
CC       axoneme {ECO:0000250|UniProtKB:P0DL09}.
CC   -!- DEVELOPMENTAL STAGE: At 7.5 dpc, expressed in the pit cells of the
CC       node, which carry motile cilia and are involved in left-right axis
CC       development. {ECO:0000269|PubMed:23354437}.
CC   -!- SIMILARITY: Belongs to the DRC1 family. {ECO:0000305}.
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DR   EMBL; AK140154; BAE24258.1; -; mRNA.
DR   EMBL; BC150863; AAI50864.1; -; mRNA.
DR   CCDS; CCDS84857.1; -.
DR   RefSeq; NP_001028632.1; NM_001033460.3.
DR   AlphaFoldDB; Q3USS3; -.
DR   SMR; Q3USS3; -.
DR   BioGRID; 238065; 2.
DR   STRING; 10090.ENSMUSP00000098992; -.
DR   TCDB; 3.A.1.211.8; the atp-binding cassette (abc) superfamily.
DR   iPTMnet; Q3USS3; -.
DR   PhosphoSitePlus; Q3USS3; -.
DR   MaxQB; Q3USS3; -.
DR   PaxDb; Q3USS3; -.
DR   PRIDE; Q3USS3; -.
DR   ProteomicsDB; 279485; -.
DR   Antibodypedia; 55104; 32 antibodies from 4 providers.
DR   Ensembl; ENSMUST00000101448; ENSMUSP00000098992; ENSMUSG00000073102.
DR   GeneID; 381738; -.
DR   KEGG; mmu:381738; -.
DR   UCSC; uc029vgu.1; mouse.
DR   CTD; 92749; -.
DR   MGI; MGI:2685906; Drc1.
DR   VEuPathDB; HostDB:ENSMUSG00000073102; -.
DR   eggNOG; ENOG502QQ2B; Eukaryota.
DR   GeneTree; ENSGT00940000153804; -.
DR   HOGENOM; CLU_012489_1_0_1; -.
DR   InParanoid; Q3USS3; -.
DR   OMA; LEKSECY; -.
DR   OrthoDB; 258073at2759; -.
DR   PhylomeDB; Q3USS3; -.
DR   TreeFam; TF324985; -.
DR   BioGRID-ORCS; 381738; 1 hit in 51 CRISPR screens.
DR   ChiTaRS; Drc1; mouse.
DR   PRO; PR:Q3USS3; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q3USS3; protein.
DR   Bgee; ENSMUSG00000073102; Expressed in spermatid and 108 other tissues.
DR   Genevisible; Q3USS3; MM.
DR   GO; GO:0005858; C:axonemal dynein complex; IEA:InterPro.
DR   GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR   GO; GO:0070286; P:axonemal dynein complex assembly; ISS:UniProtKB.
DR   GO; GO:0060285; P:cilium-dependent cell motility; ISS:UniProtKB.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0003352; P:regulation of cilium movement; IBA:GO_Central.
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   Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Flagellum;
KW   Reference proteome.
FT   CHAIN           1..753
FT                   /note="Dynein regulatory complex protein 1"
FT                   /id="PRO_0000277883"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          55..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          100..388
FT                   /evidence="ECO:0000255"
FT   COILED          703..739
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        612..628
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        571
FT                   /note="V -> M (in Ref. 2; AAI50864)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   753 AA;  88507 MW;  074425DAD6C18C56 CRC64;
     MNPSGTIGVL EQNGEEHLAT PILGPSVHSD NPQERIQARR LRIAARQEAR RREALGEYLD
     GKKESEEEQS KSYKQKEESR LKLTKLLLCG TELVTNIQVA ADVREIHRRV EEEETKRQRL
     EKLENEVKTS QDKFDEITAK WEEGRRKRIP QELWEMLNSQ QVHCAELIED KNKLANELQQ
     ELKIKDDQYV KDLKKQSEDI TLILERMEEQ VKNVMKNFRQ ELIHIEKAFE SERQELLSSN
     KKKWERALQA HNAKELEYLT NRMKKVEDYE KQLNKQRVWD CEEYNTIKIK LEQDVQILEQ
     QLQQMKATYQ LNQEKLEYNF QVLKKRDEES TVIKSQQKRK LNRLHDVVNN LRTKYTKQIR
     QFQDDNQSLT SDYKRLVTQF KDLQKALRHF IIIDEEKFRE IWLMNEAEAK ELAQRAFDVD
     RIIHSQHLGL PWNMPDLWFL NNVGPISLQQ QKSVTQILEE LLLQTEDEAT EAAMSEDEDY
     MDLPNQISAK TTTKVLMLLC DESGFLIESK LLSLLHPLEK SECYLLRLDA IFSALAIEDE
     DDLYKLVNFF LRYRAHRLSS AQASSSIHSN VERTSLMSAL ERLSLMSQTD KGSMVSKSDQ
     EPTEQEDEQE GDNASLSSRE LEEQEDLSSP RFIHPNDVLK ILEAFVTGLK KPKDAQPVLK
     LKKETRDNSK DTEYWESLAA VIPFFKQNLW DALYKALEKY YLVLTERAKL LMENESLEQQ
     NAEMQSLLQQ YLQAKVNTEL QIPPTQGFRM PSK