DC2L1_RAT
ID DC2L1_RAT Reviewed; 351 AA.
AC Q6AY43;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Cytoplasmic dynein 2 light intermediate chain 1;
GN Name=Dync2li1; Synonyms=Lic3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 INTERACTION WITH DYNC2H1, AND SUBCELLULAR LOCATION.
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 INTERACTION WITH DYNC2H1.
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).
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. Involved in the
CC regulation of ciliary length. {ECO:0000250|UniProtKB:Q8TCX1}.
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 (By similarity).
CC Interacts with DYNC2H1 (via N-terminus); this interaction stabilizes
CC the dynein-2 complex structure (PubMed:11907264).
CC {ECO:0000250|UniProtKB:Q8TCX1, ECO:0000269|PubMed:11907264}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TCX1}. 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:12432068}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q8TCX1}. Note=Localizes to the apical cytoplasm.
CC {ECO:0000250|UniProtKB:Q8K0T2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6AY43-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6AY43-2; Sequence=VSP_031293, VSP_031294;
CC -!- SIMILARITY: Belongs to the dynein light intermediate chain family.
CC {ECO:0000305}.
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DR EMBL; AABR03048845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC079201; AAH79201.1; -; mRNA.
DR RefSeq; NP_001013962.1; NM_001013940.1. [Q6AY43-2]
DR RefSeq; XP_006239757.1; XM_006239695.3. [Q6AY43-1]
DR AlphaFoldDB; Q6AY43; -.
DR SMR; Q6AY43; -.
DR STRING; 10116.ENSRNOP00000006953; -.
DR PaxDb; Q6AY43; -.
DR Ensembl; ENSRNOT00000006953; ENSRNOP00000006953; ENSRNOG00000005151. [Q6AY43-1]
DR Ensembl; ENSRNOT00000068030; ENSRNOP00000063540; ENSRNOG00000005151. [Q6AY43-2]
DR GeneID; 298767; -.
DR KEGG; rno:298767; -.
DR UCSC; RGD:1310286; rat. [Q6AY43-1]
DR CTD; 51626; -.
DR RGD; 1310286; Dync2li1.
DR eggNOG; KOG3929; Eukaryota.
DR GeneTree; ENSGT00390000010498; -.
DR HOGENOM; CLU_049395_0_0_1; -.
DR InParanoid; Q6AY43; -.
DR OMA; IRKHTCR; -.
DR OrthoDB; 910690at2759; -.
DR PhylomeDB; Q6AY43; -.
DR TreeFam; TF314138; -.
DR Reactome; R-RNO-5620924; Intraflagellar transport.
DR PRO; PR:Q6AY43; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000005151; Expressed in testis and 20 other tissues.
DR Genevisible; Q6AY43; RN.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0005930; C:axoneme; ISO:RGD.
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:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; ISO:RGD.
DR GO; GO:0045504; F:dynein heavy chain binding; IPI:WormBase.
DR GO; GO:0060271; P:cilium assembly; ISO:RGD.
DR GO; GO:0007368; P:determination of left/right symmetry; ISO:RGD.
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 Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW 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_0000318752"
FT REGION 304..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 VAR_SEQ 244
FT /note="S -> RYWYIFSNQFPRSRVSCLPPPLSSACDFPLLIFSTCLFWLCPARGLS
FT WLWCCLSQPVLLAHLGHCFYP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031293"
FT VAR_SEQ 245..351
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031294"
SQ SEQUENCE 351 AA; 39670 MW; 2380321063189EB7 CRC64;
MPSETLWEIA KAEVEKRRCH GSDGDGMEIG EKSVFFIGSK NGGKTTIILR CLDRDEPAKP
TLALEYTYGR KTKGHNTPKD IAHFWELGGG TSLLDLISIP ITVDTLRTFS IVLVLDLSKP
NDLWPTMENL LQATKSHVDK VTMKLGKANS KASSEMRQRM WSVMQKDHPD RELIDPFPIP
LVIIGSKYDI FQDFDPEKRK VICKTLRFVA HYYGASLMFT SKSEALLLKM RGVINQLAFG
IDKSKSMCVD QNKPLFITAG LDSLCQIGSP PVPDSDIGKL QAHSPMELWK KVYEKLFPPK
STSTLKAIQD PARDPQYAES EVDEMRVQKD QELEQYKRSS SKTWKQIELD S
