DRC2_MOUSE
ID DRC2_MOUSE Reviewed; 493 AA.
AC Q8VHI7; Q6PAP9;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Dynein regulatory complex subunit 2 {ECO:0000250|UniProtKB:Q8IXS2};
DE AltName: Full=Coiled-coil domain-containing protein 65;
DE AltName: Full=Testis development protein NYD-SP28;
GN Name=Ccdc65; Synonyms=Drc2 {ECO:0000250|UniProtKB:Q8IXS2};
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 [MRNA] (ISOFORM 1).
RC STRAIN=ICR; TISSUE=Brain, and Testis;
RA Li J.M., Sha J.H.;
RT "A new mouse nucleoprotein mNYD-SP28: similar to NYD-SP28.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Olfactory epithelium;
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 [4]
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).
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 DRC1 to form a central scaffold needed
CC for assembly of the N-DRC and its attachment to the outer doublet
CC microtubules. {ECO:0000250|UniProtKB:A8JB22,
CC ECO:0000250|UniProtKB:Q8IXS2}.
CC -!- SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC).
CC {ECO:0000250|UniProtKB:A8JB22}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum basal body
CC {ECO:0000250|UniProtKB:A8JB22}. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:A8JB22}. Cytoplasm, cytoskeleton, flagellum
CC axoneme {ECO:0000250|UniProtKB:A8JB22}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VHI7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VHI7-2; Sequence=VSP_024645;
CC -!- SIMILARITY: Belongs to the DRC2 family.
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; AF454432; AAL51007.1; -; mRNA.
DR EMBL; AK077174; BAC36661.1; -; mRNA.
DR EMBL; BC048073; AAH48073.1; -; mRNA.
DR EMBL; BC056947; AAH56947.1; -; mRNA.
DR EMBL; BC060155; AAH60155.1; -; mRNA.
DR CCDS; CCDS27802.1; -. [Q8VHI7-1]
DR RefSeq; NP_705738.1; NM_153518.1. [Q8VHI7-1]
DR AlphaFoldDB; Q8VHI7; -.
DR SMR; Q8VHI7; -.
DR STRING; 10090.ENSMUSP00000003444; -.
DR PhosphoSitePlus; Q8VHI7; -.
DR MaxQB; Q8VHI7; -.
DR PaxDb; Q8VHI7; -.
DR PRIDE; Q8VHI7; -.
DR ProteomicsDB; 265713; -. [Q8VHI7-1]
DR ProteomicsDB; 265714; -. [Q8VHI7-2]
DR Antibodypedia; 48594; 57 antibodies from 13 providers.
DR DNASU; 105833; -.
DR Ensembl; ENSMUST00000003444; ENSMUSP00000003444; ENSMUSG00000003354. [Q8VHI7-1]
DR GeneID; 105833; -.
DR KEGG; mmu:105833; -.
DR UCSC; uc007xnk.1; mouse. [Q8VHI7-2]
DR UCSC; uc007xnl.1; mouse. [Q8VHI7-1]
DR CTD; 85478; -.
DR MGI; MGI:2146001; Ccdc65.
DR VEuPathDB; HostDB:ENSMUSG00000003354; -.
DR eggNOG; ENOG502QQDD; Eukaryota.
DR GeneTree; ENSGT00940000153804; -.
DR HOGENOM; CLU_026536_1_0_1; -.
DR InParanoid; Q8VHI7; -.
DR OMA; QNHERDV; -.
DR OrthoDB; 815240at2759; -.
DR PhylomeDB; Q8VHI7; -.
DR TreeFam; TF326074; -.
DR BioGRID-ORCS; 105833; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Ccdc65; mouse.
DR PRO; PR:Q8VHI7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8VHI7; protein.
DR Bgee; ENSMUSG00000003354; Expressed in spermatid and 67 other tissues.
DR ExpressionAtlas; Q8VHI7; baseline and differential.
DR Genevisible; Q8VHI7; MM.
DR GO; GO:0005858; C:axonemal dynein complex; IEA:InterPro.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0070286; P:axonemal dynein complex assembly; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR GO; GO:0060285; P:cilium-dependent cell motility; IBA:GO_Central.
DR GO; GO:0003352; P:regulation of cilium movement; ISO:MGI.
DR InterPro; IPR039505; DRC1/2_N.
DR InterPro; IPR039750; DRC1/DRC2.
DR PANTHER; PTHR21625; PTHR21625; 1.
DR Pfam; PF14772; NYD-SP28; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Flagellum; Reference proteome.
FT CHAIN 1..493
FT /note="Dynein regulatory complex subunit 2"
FT /id="PRO_0000284780"
FT COILED 99..163
FT /evidence="ECO:0000255"
FT COILED 253..280
FT /evidence="ECO:0000255"
FT VAR_SEQ 105..493
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024645"
FT CONFLICT 104
FT /note="S -> V (in Ref. 2; AAH56947/AAH60155)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 58170 MW; 2BEE9457E4CB5154 CRC64;
MSKKGKKPKL PKAPLSEEDQ LLIFQQKMLA DEEAAKKKER LLTQFLKDKL AKEEHNSALN
LNKINTQWRT ILREVKTREL HQDIEILSQT FERVVDCKDS VIKSLAKDLT EAEEQYAHAL
RSHLHNIDQL LTLQRRRLGL LEENYNMELE VLTKEFETER KLIIDHHEKE MHYLQDVFMA
MEQNYIDSEY ESKLEFQSMW DDLKNKNLEE KHFLRLQLEN IVEDLWRRFQ DALKNYTDAT
EDRKIAFEYL KVKDEKSSKE IETQMKKIQK LQETIGILKG KIVAHSREGE WQNQCIRNNK
ELVHVQLRKL KVQRTQARTL SQENLVKLTL ESNATLKALK KVVEKGEKIL KLAEICRKFE
TEEEKVLPFY SSVLTPEEQE EAKLQNPEDI TEDLAKIMMD YAGMENFWKR YNKVKLEVLS
LQHRRLQLLD ISSKLREMLK QYLDGISVSD EVLSHLNPLF VVNHRSNLPQ LPPPSAQPVY
NVIEAAHIAS HIL
