DC2I1_MOUSE
ID DC2I1_MOUSE Reviewed; 999 AA.
AC Q8C761; Q3UNM4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Cytoplasmic dynein 2 intermediate chain 1;
DE AltName: Full=Dynein 2 intermediate chain 1;
DE AltName: Full=WD repeat-containing protein 60;
GN Name=Dync2i1; Synonyms=Wdr60;
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=Kidney, and Lung;
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 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: Acts as one of several non-catalytic accessory components of
CC the cytoplasmic dynein 2 complex (dynein-2 complex), a motor protein
CC complex that drives the movement of cargos along microtubules within
CC cilia and flagella in concert with the intraflagellar transport (IFT)
CC system. DYNC2I1 plays a major role in retrograde ciliary protein
CC trafficking in cilia and flagella. Requires also to maintain a
CC functional transition zone. {ECO:0000250|UniProtKB:Q8WVS4}.
CC -!- SUBUNIT: Intermediate chain of the cytoplasmic dynein complex 2, a
CC multisubunit complex, composed at least of eleven different proteins.
CC The cytoplasmic dynein 2 complex consists of two catalytic heavy chains
CC (HCs) and a number of non-catalytic subunits presented by intermediate
CC chains (ICs), light intermediate chains (LICs) and light chains (LCs).
CC Among them, a heavy chain (DYNC2H1), two intermediate chains (DYNC2I2
CC and DYNC2I1), a light intermediate chain (DYNC2LI1), and a light chain
CC (DYNLT2B) are unique to the cytoplasmic dynein complex 2, but a subset
CC of the light chains are also shared by dynein-1 and dynein-2 complexes.
CC Interacts with DYNC2I2; their C-terminal domains each bind a copy of
CC the heavy chain, and their extended N-terminal regions are held
CC together by an array of light chain dimers. Interacts with DYNLT2B.
CC Interacts (via the N-terminal half) with DYNLT2B-DYNLT1 dimer or with
CC DYNLT2B-DYNLT3 dimer; this interaction is crucial for retrograde
CC trafficking of ciliary proteins. {ECO:0000250|UniProtKB:Q8WVS4}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q8WVS4}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q8WVS4}.
CC Note=Located at the base of the primary cilium in serum-starved
CC fibroblasts. {ECO:0000250|UniProtKB:Q8WVS4}.
CC -!- SIMILARITY: Belongs to the dynein light intermediate chain family.
CC {ECO:0000305}.
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DR EMBL; AK052482; BAC35011.1; -; mRNA.
DR EMBL; AK144138; BAE25723.1; -; mRNA.
DR CCDS; CCDS36575.1; -.
DR RefSeq; NP_666151.3; NM_146039.3.
DR AlphaFoldDB; Q8C761; -.
DR SMR; Q8C761; -.
DR BioGRID; 229980; 1.
DR STRING; 10090.ENSMUSP00000047334; -.
DR iPTMnet; Q8C761; -.
DR PhosphoSitePlus; Q8C761; -.
DR MaxQB; Q8C761; -.
DR PaxDb; Q8C761; -.
DR PeptideAtlas; Q8C761; -.
DR PRIDE; Q8C761; -.
DR ProteomicsDB; 299745; -.
DR Antibodypedia; 10739; 44 antibodies from 11 providers.
DR DNASU; 217935; -.
DR Ensembl; ENSMUST00000039349; ENSMUSP00000047334; ENSMUSG00000042050.
DR GeneID; 217935; -.
DR KEGG; mmu:217935; -.
DR UCSC; uc007phj.1; mouse.
DR CTD; 55112; -.
DR MGI; MGI:2445085; Dync2i1.
DR VEuPathDB; HostDB:ENSMUSG00000042050; -.
DR eggNOG; KOG1587; Eukaryota.
DR GeneTree; ENSGT00390000013743; -.
DR HOGENOM; CLU_010610_0_0_1; -.
DR InParanoid; Q8C761; -.
DR OMA; ILNMWVV; -.
DR OrthoDB; 1158787at2759; -.
DR PhylomeDB; Q8C761; -.
DR TreeFam; TF329081; -.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR BioGRID-ORCS; 217935; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Wdr60; mouse.
DR PRO; PR:Q8C761; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8C761; protein.
DR Bgee; ENSMUSG00000042050; Expressed in retinal neural layer and 169 other tissues.
DR ExpressionAtlas; Q8C761; baseline and differential.
DR Genevisible; Q8C761; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0097546; C:ciliary base; ISO:MGI.
DR GO; GO:0097014; C:ciliary plasm; IBA:GO_Central.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR GO; GO:0031021; C:interphase microtubule organizing center; ISO:MGI.
DR GO; GO:0000242; C:pericentriolar material; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0045504; F:dynein heavy chain binding; IBA:GO_Central.
DR GO; GO:0045503; F:dynein light chain binding; ISO:MGI.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISO:MGI.
DR GO; GO:0035721; P:intraciliary retrograde transport; ISS:UniProtKB.
DR GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR042505; DYNC2I1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR16022; PTHR16022; 2.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..999
FT /note="Cytoplasmic dynein 2 intermediate chain 1"
FT /id="PRO_0000242143"
FT REPEAT 637..677
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 718..764
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 850..890
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 895..935
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REGION 1..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..495
FT /note="Binding to the DYNLT2B-DYNLT1/DYNLT3 dimer"
FT /evidence="ECO:0000250|UniProtKB:Q8WVS4"
FT COMPBIAS 1..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..337
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WVS4"
FT CONFLICT 732
FT /note="Q -> H (in Ref. 1; BAE25723)"
FT /evidence="ECO:0000305"
FT CONFLICT 760
FT /note="P -> S (in Ref. 1; BAE25723)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 999 AA; 115382 MW; D86C469803BD6F5C CRC64;
MEPGKRRTKD DTWKADDLRK HLKVQSGSPK EEKKLREKKA HKDSESAAPE YREHKSRDPD
REARHKEKTA ERDLYTSTEH PRGERDRERH KERRKDAKDR EKDKLKERHR DQEAEKAHSR
GKDREREKDR RARKEEIRQS MAYHDLLSRD MRGRQMAEKV EKKASKIRTE ERERRDEDSE
RIDEDRERRY RERKLQYGDS KEHPLSYWLY KEDGEKKHRK AKDADREKRL REKSSMREKR
ERHAREKGSS LSDREVEDRH REKRHKEGLH YDDERRRSHA DKKERSSKEE HKKRELKELE
KEDNDLEATG PDEYLPNLED DFVDYEDDFE VCDGDDDSNN EHEAREKAEE LPLAQKREIQ
EIQKAISAEN ERVGELSLKM FQKQGWTEYT KEPWTDANDS PSRTPVCGIF VDFATASHRQ
KSRSQALKQK TRSSKLLRLI DLDFSFTFSL LDLPPVNEYD MYIRNFGKKN TKQAYVQYNE
DNVERDIQTE DIETREVWTQ HPGEGTAVSG GSEEKDFSDV TVVPKIDTPR LANFLRAACQ
VVAVLLEEDR LAAGPSWIPR AQDKALNISD SSSQLNTSLP FLQSRKVSCL HASRVQRQTV
VSVHDLPEKA FAPSLDSRHL LCVWDIWQPS GPQKVLICES KVTCCCFSPL KAFLLFAGTV
HGSVVVWDLR EDSRIHHYVR LSNCFWAFRT PTFSTDGILT SVNHRSPLQA IEPVATSAYK
KQSFVLSPFS TQEEMAGLSF HIASLDETGV LNVWVVVELP KADISGSMSD LGLIPGGRIK
LVHSTVIQLG NSLSHKDSEL WGSTQTLSVK FLPSDPNHFV VGTDMGLISH STRQDWRVSP
RVFKPEQHGV RPIKVNVIDF SPFEETVFLA GCSDGSIRLH QLTSERPIMQ WDNSTSGHAV
TSLQWSPTRP AVFLVQDDAS RIYVWDLLEN DLGPVAQQPI SPDKLVAMTI VGEPEKTSGS
FVALVLARTS GTVDVQNLKR RWTTPAVDEH SQLRLLLQK
