DC2L1_MOUSE
ID DC2L1_MOUSE Reviewed; 351 AA.
AC Q8K0T2; Q3TVA2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Cytoplasmic dynein 2 light intermediate chain 1;
DE Short=mD2LIC;
GN Name=Dync2li1; Synonyms=D2lic;
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=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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Mammary tumor;
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 TISSUE SPECIFICITY.
RX PubMed=12432068; DOI=10.1242/jcs.00168;
RA Mikami A., Tynan S.H., Hama T., Luby-Phelps K., Saito T., Crandall J.E.,
RA Besharse J.C., Vallee R.B.;
RT "Molecular structure of cytoplasmic dynein 2 and its distribution in
RT neuronal and ciliated cells.";
RL J. Cell Sci. 115:4801-4808(2002).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11907264; DOI=10.1091/mbc.01-08-0402;
RA Grissom P.M., Vaisberg E.A., McIntosh J.R.;
RT "Identification of a novel light intermediate chain (D2LIC) for mammalian
RT cytoplasmic dynein 2.";
RL Mol. Biol. Cell 13:817-829(2002).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12802074; DOI=10.1091/mbc.e02-10-0682;
RA Perrone C.A., Tritschler D., Taulman P., Bower R., Yoder B.K., Porter M.E.;
RT "A novel dynein light intermediate chain colocalizes with the retrograde
RT motor for intraflagellar transport at sites of axoneme assembly in
RT chlamydomonas and mammalian cells.";
RL Mol. Biol. Cell 14:2041-2056(2003).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15371312; DOI=10.1242/dev.01389;
RA Rana A.A., Barbera J.P.M., Rodriguez T.A., Lynch D., Hirst E., Smith J.C.,
RA Beddington R.S.P.;
RT "Targeted deletion of the novel cytoplasmic dynein mD2LIC disrupts the
RT embryonic organiser, formation of the body axes and specification of
RT ventral cell fates.";
RL Development 131:4999-5007(2004).
RN [7]
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, facilitating the assembly of these organelles (By similarity)
CC (PubMed:15371312). Involved in the regulation of ciliary length (By
CC similarity). {ECO:0000250|UniProtKB:Q8TCX1,
CC ECO:0000269|PubMed:15371312}.
CC -!- SUBUNIT: Light intermediate chain of the cytoplasmic dynein complex 2,
CC a 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 dynein-2 complex, but a subset of light
CC chains are also shared by dynein-1 and dynein-2 complexes. Dynein-2
CC complex is built around two copies of cytoplasmic dynein 2 heavy chain
CC 1 (DYNC2H1). The C-terminal region forms the motor domain, which
CC converts the energy from ATP hydrolysis into movement. Its N-terminal
CC region forms the tail, an extended structure that binds the other
CC subunits and holds the two heavy chains in a homodimer. Interacts with
CC DYNC2H1 (via N-terminus); this interaction stabilizes the dynein-2
CC complex structure. {ECO:0000250|UniProtKB:Q8TCX1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12802074}. Cell
CC projection, cilium {ECO:0000250|UniProtKB:Q8TCX1}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8TCX1}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:12802074}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q8TCX1}. Note=Localizes to the apical cytoplasm.
CC {ECO:0000269|PubMed:12802074}.
CC -!- TISSUE SPECIFICITY: Specifically expressed by ciliated cells in brain,
CC lung, spleen, testis and kidney (at protein level). Enriched in the
CC ependymal layer lining the lateral ventricles (at protein level).
CC {ECO:0000269|PubMed:11907264, ECO:0000269|PubMed:12432068,
CC ECO:0000269|PubMed:12802074, ECO:0000269|PubMed:15371312}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed by monociliated cells of
CC the ventral node from the late streak to early somite stage.
CC {ECO:0000269|PubMed:15371312}.
CC -!- DISRUPTION PHENOTYPE: Death before 11.5 dpc with defects in notochord
CC and floor plate formation and a reduction of definitive endoderm. Mice
CC also display anterior truncations of the forebrain, defects in the
CC ventral body wall, in closure of the neural tube, and either an arrest
CC of embryonic turning and heart looping or a randomization in their
CC direction. {ECO:0000269|PubMed:15371312}.
CC -!- SIMILARITY: Belongs to the dynein light intermediate chain family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE35717.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK160259; BAE35717.1; ALT_FRAME; mRNA.
DR EMBL; BC030450; AAH30450.1; -; mRNA.
DR EMBL; BC039070; AAH39070.1; -; mRNA.
DR CCDS; CCDS29000.1; -.
DR RefSeq; NP_758460.1; NM_172256.1.
DR AlphaFoldDB; Q8K0T2; -.
DR SMR; Q8K0T2; -.
DR STRING; 10090.ENSMUSP00000025101; -.
DR iPTMnet; Q8K0T2; -.
DR PhosphoSitePlus; Q8K0T2; -.
DR MaxQB; Q8K0T2; -.
DR PaxDb; Q8K0T2; -.
DR PRIDE; Q8K0T2; -.
DR ProteomicsDB; 279159; -.
DR Antibodypedia; 47397; 96 antibodies from 21 providers.
DR DNASU; 213575; -.
DR Ensembl; ENSMUST00000025101; ENSMUSP00000025101; ENSMUSG00000024253.
DR GeneID; 213575; -.
DR KEGG; mmu:213575; -.
DR UCSC; uc008dsy.1; mouse.
DR CTD; 51626; -.
DR MGI; MGI:1913996; Dync2li1.
DR VEuPathDB; HostDB:ENSMUSG00000024253; -.
DR eggNOG; KOG3929; Eukaryota.
DR GeneTree; ENSGT00390000010498; -.
DR HOGENOM; CLU_049395_0_0_1; -.
DR InParanoid; Q8K0T2; -.
DR OMA; IRKHTCR; -.
DR OrthoDB; 910690at2759; -.
DR PhylomeDB; Q8K0T2; -.
DR TreeFam; TF314138; -.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR BioGRID-ORCS; 213575; 2 hits in 57 CRISPR screens.
DR ChiTaRS; Dync2li1; mouse.
DR PRO; PR:Q8K0T2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8K0T2; protein.
DR Bgee; ENSMUSG00000024253; Expressed in otolith organ and 222 other tissues.
DR Genevisible; Q8K0T2; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:BHF-UCL.
DR GO; GO:0005930; C:axoneme; IDA:BHF-UCL.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0035869; C:ciliary transition zone; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IDA:BHF-UCL.
DR GO; GO:0045504; F:dynein heavy chain binding; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0035721; P:intraciliary retrograde transport; IBA:GO_Central.
DR GO; GO:0035735; P:intraciliary transport involved in cilium assembly; ISS:UniProtKB.
DR GO; GO:1902017; P:regulation of cilium assembly; ISS:UniProtKB.
DR InterPro; IPR040045; DYNC2LI1.
DR InterPro; IPR022780; Dynein_light_int_chain.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13236; PTHR13236; 1.
DR Pfam; PF05783; DLIC; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Developmental protein; Dynein; Microtubule; Motor protein;
KW Reference proteome.
FT CHAIN 1..351
FT /note="Cytoplasmic dynein 2 light intermediate chain 1"
FT /id="PRO_0000318751"
FT REGION 303..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 15
FT /note="E -> Q (in Ref. 1; BAE35717)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="V -> L (in Ref. 1; BAE35717)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="L -> H (in Ref. 1; BAE35717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 39469 MW; 140D6C96B7188C2F CRC64;
MPSETLWEIA KAEVEKRRSH GSEGDGAEIG EKSVFFIGSK NGGKTTIILR CLDRDESAKP
TLALEYTYGR KTKGHNTPKD IAHFWELGGG TSLLDLISIP ITVDTLRTFS IVLVLDLSKP
NDLWSTMENL LQATKSHVDK VIMKLGKTSS KASAEMRQRM WSVVQKDHPD RELIDPFPIP
LVIIGSKYDI FQDFDPEKRK VICKTLRFVA HYYGASLMFT SKSEALLLKI RGVINQLAFG
IDKSKSICVD QNKPLFITAG LDSLCQIGSP PVPDSDIGKL QAHSPMELWK KVYDKLFPPK
STGTLKAVQD PARDPQYAES EVDEMRVQKD QELEHYKRSS SKTWKQIELD S
