DRC6_MOUSE
ID DRC6_MOUSE Reviewed; 790 AA.
AC Q8CDU4; Q8CDE9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Dynein regulatory complex subunit 6 {ECO:0000303|PubMed:28630322};
DE AltName: Full=F-box and leucine-rich repeat protein 13;
DE AltName: Full=F-box/LRR-repeat protein 13;
GN Name=Fbxl13; Synonyms=Drc6 {ECO:0000303|PubMed:28630322};
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] (ISOFORMS 1 AND 2).
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 [2]
RP INTERACTION WITH TCTE1.
RX PubMed=28630322; DOI=10.1073/pnas.1621279114;
RA Castaneda J.M., Hua R., Miyata H., Oji A., Guo Y., Cheng Y., Zhou T.,
RA Guo X., Cui Y., Shen B., Wang Z., Hu Z., Zhou Z., Sha J.,
RA Prunskaite-Hyyrylainen R., Yu Z., Ramirez-Solis R., Ikawa M., Matzuk M.M.,
RA Liu M.;
RT "TCTE1 is a conserved component of the dynein regulatory complex and is
RT required for motility and metabolism in mouse spermatozoa.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E5370-E5378(2017).
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. Substrate-recognition component of the SCF
CC (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.
CC {ECO:0000250, ECO:0000250|UniProtKB:A8JHD7}.
CC -!- SUBUNIT: Component of the nexin-dynein regulatory complex (N-DRC).
CC Directly interacts with SKP1 and CUL1 (By similarity). Interacts with
CC TCTE1/DRC5 (PubMed:28630322). {ECO:0000250,
CC ECO:0000250|UniProtKB:A8JHD7, ECO:0000269|PubMed:28630322}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC {ECO:0000250|UniProtKB:A8JHD7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CDU4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CDU4-2; Sequence=VSP_013006, VSP_013007, VSP_013008;
CC -!- SIMILARITY: Belongs to the DRC6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC26515.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC26821.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK029566; BAC26515.1; ALT_FRAME; mRNA.
DR EMBL; AK030172; BAC26821.1; ALT_FRAME; mRNA.
DR CCDS; CCDS51429.1; -. [Q8CDU4-1]
DR RefSeq; NP_796050.2; NM_177076.4. [Q8CDU4-1]
DR AlphaFoldDB; Q8CDU4; -.
DR SMR; Q8CDU4; -.
DR BioGRID; 235772; 1.
DR STRING; 10090.ENSMUSP00000052716; -.
DR PhosphoSitePlus; Q8CDU4; -.
DR PaxDb; Q8CDU4; -.
DR PRIDE; Q8CDU4; -.
DR ProteomicsDB; 267533; -. [Q8CDU4-1]
DR ProteomicsDB; 267534; -. [Q8CDU4-2]
DR Antibodypedia; 31140; 104 antibodies from 21 providers.
DR DNASU; 320118; -.
DR Ensembl; ENSMUST00000051358; ENSMUSP00000052716; ENSMUSG00000048520. [Q8CDU4-1]
DR GeneID; 320118; -.
DR KEGG; mmu:320118; -.
DR UCSC; uc008wop.2; mouse. [Q8CDU4-1]
DR UCSC; uc008woq.1; mouse. [Q8CDU4-2]
DR CTD; 222235; -.
DR MGI; MGI:2443416; Fbxl13.
DR VEuPathDB; HostDB:ENSMUSG00000048520; -.
DR eggNOG; KOG1947; Eukaryota.
DR GeneTree; ENSGT00940000160224; -.
DR InParanoid; Q8CDU4; -.
DR OMA; DKHYPNI; -.
DR OrthoDB; 1282076at2759; -.
DR PhylomeDB; Q8CDU4; -.
DR TreeFam; TF329711; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 320118; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Fbxl13; mouse.
DR PRO; PR:Q8CDU4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8CDU4; protein.
DR Bgee; ENSMUSG00000048520; Expressed in spermatid and 15 other tissues.
DR ExpressionAtlas; Q8CDU4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF13516; LRR_6; 2.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 14.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium; Cytoplasm; Cytoskeleton;
KW Flagellum; Leucine-rich repeat; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..790
FT /note="Dynein regulatory complex subunit 6"
FT /id="PRO_0000119860"
FT DOMAIN 237..283
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 503..525
FT /note="LRR 1"
FT REPEAT 531..552
FT /note="LRR 2"
FT REPEAT 557..579
FT /note="LRR 3"
FT REPEAT 582..602
FT /note="LRR 4"
FT REPEAT 606..628
FT /note="LRR 5"
FT REPEAT 632..657
FT /note="LRR 6"
FT VAR_SEQ 420
FT /note="Q -> QISVQGFRNIASSCTGIVHLTINDMPTLTDNCVK (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013006"
FT VAR_SEQ 670..685
FT /note="ITDAGMEILSARCHYL -> VCMAAGALTGSRQGCT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013007"
FT VAR_SEQ 686..790
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013008"
FT CONFLICT 173
FT /note="L -> W (in Ref. 1; BAC26821)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="R -> K (in Ref. 1; BAC26515)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="R -> E (in Ref. 1; BAC26515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 790 AA; 90657 MW; E4E3C2BA2D680367 CRC64;
MASLRSATPR LRSYFRDKYI PQICEALLCG LLVTCPEDPL KYLEHMILAI IKRGLENLLW
DTCIHPSLKS RVRRLSETYL DELFGLDDQL VTPELMIKAC TFYTGHLVKT HFSGWKKVAI
PRANQEEIMA EKMDKAIAHD NFRCQKYIFN RWFAYTVMSR ERLITTLLRL RHLFYMQRQR
IILAKWKERA RHKSKTREDD LISKHELQLK KWKFKLGKPI SLEGSLSDIA VENRRIAFDI
SVLPEQAILQ IFLYLTFKDM MACSRVNRSW MAMIQRGSLW NSIDFSTVKN IADKCVVTTL
QKWRLNVLRL NFRGCDFRTK TLKAVSHCKN LQELNVSDCQ SFTDESMRHI SEGCPGVLYL
NLSNTTITNR TMRLLPRYFH NLQNLSLAYC RKFTDKGLQY LNLGNGCHKL IYLDLSGCTQ
VLVEKCPRIS SVVLIGSPHI SDSAFKALSS CDLKKIRFEG NKRISDACFK SIDRNYPGIN
HIYMVDCKGL TDSSLKSLSL LKQLTVLNLT NCIRIGDIGL KHFFDGPASI RLRELNLTNC
SLLGDSSVIR LSERCPNLHY LNLRNCEHLT DLAIEYIASM LSLISVDLSG TLISNEGMTI
LSRHRKLREV SVSDCVNITD FGIRAYCKTS LLLEHLDVSY CSQLTDDIIK TIAIFCTRIT
SLNIAGCPKI TDAGMEILSA RCHYLHILDI SGCIQLTDQI IQDLQIGCKQ LRILKMQFCK
SISPAAAQKM SSVVQHQEYN SDNPPHWFGY DSEGNPLDKI HSRVQLRTYS KLIVKEPFSI
DEEDPDSKHQ
