DLRB1_MOUSE
ID DLRB1_MOUSE Reviewed; 96 AA.
AC P62627; A2AVR8; O88567; Q4FZJ8; Q9D812;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Dynein light chain roadblock-type 1;
DE AltName: Full=Dynein light chain 2A, cytoplasmic;
GN Name=Dynlrb1; Synonyms=Dncl2a, Dnlc2a;
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=Embryo, Kidney, and Small intestine;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Oocyte;
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 SELF-ASSOCIATION, INTERACTION WITH DYNLRB2, AND IDENTIFICATION IN THE
RP CYTOPLASMIC DYNEIN I COMPLEX.
RX PubMed=14752807; DOI=10.1002/cm.10172;
RA Nikulina K., Patel-King R.S., Takebe S., Pfister K.K., King S.M.;
RT "The Roadblock light chains are ubiquitous components of cytoplasmic dynein
RT that form homo- and heterodimers.";
RL Cell Motil. Cytoskeleton 57:233-245(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, Spleen, and 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).
RN [6]
RP STRUCTURE BY NMR OF 2-96, SUBUNIT, AND INTERACTION WITH DYNC1I1.
RX PubMed=16289575; DOI=10.1016/j.jmb.2005.10.017;
RA Song J., Tyler R.C., Lee M.S., Tyler E.M., Markley J.L.;
RT "Solution structure of isoform 1 of Roadblock/LC7, a light chain in the
RT dynein complex.";
RL J. Mol. Biol. 354:1043-1051(2005).
CC -!- FUNCTION: Acts as one of several non-catalytic accessory components of
CC the cytoplasmic dynein 1 complex that are thought to be involved in
CC linking dynein to cargos and to adapter proteins that regulate dynein
CC function. Cytoplasmic dynein 1 acts as a motor for the intracellular
CC retrograde motility of vesicles and organelles along microtubules.
CC -!- SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of two
CC catalytic heavy chains (HCs) and a number of non-catalytic subunits
CC presented by intermediate chains (ICs), light intermediate chains
CC (LICs) and light chains (LCs); the composition seems to vary in respect
CC to the IC, LIC and LC composition. The heavy chain homodimer serves as
CC a scaffold for the probable homodimeric assembly of the respective non-
CC catalytic subunits. The ICs and LICs bind directly to the HC dimer and
CC the LCs assemble on the IC dimer. Interacts with DYNC1I1 and DYNC1I2.
CC Self-associates. Interacts with DYNLRB2. Interacts with RAB6A; the
CC interaction is direct. Interacts with RAB6B (GDP-bound) (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Belongs to the GAMAD family. {ECO:0000305}.
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; AK002359; BAB22038.1; -; mRNA.
DR EMBL; AK003435; BAB22788.1; -; mRNA.
DR EMBL; AK008595; BAB25768.1; -; mRNA.
DR EMBL; AK166685; BAE38944.1; -; mRNA.
DR EMBL; AL929588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC099423; AAH99423.1; -; mRNA.
DR EMBL; BC125610; AAI25611.1; -; mRNA.
DR EMBL; BC125648; AAI25649.1; -; mRNA.
DR CCDS; CCDS38294.1; -.
DR RefSeq; NP_080223.2; NM_025947.3.
DR PDB; 1Y4O; NMR; -; A/B=2-96.
DR PDBsum; 1Y4O; -.
DR AlphaFoldDB; P62627; -.
DR BMRB; P62627; -.
DR SMR; P62627; -.
DR BioGRID; 211916; 25.
DR ComplexPortal; CPX-5699; Cytoplasmic dynein complex, variant 1.
DR IntAct; P62627; 14.
DR STRING; 10090.ENSMUSP00000105304; -.
DR iPTMnet; P62627; -.
DR PhosphoSitePlus; P62627; -.
DR UCD-2DPAGE; P62627; -.
DR EPD; P62627; -.
DR jPOST; P62627; -.
DR MaxQB; P62627; -.
DR PaxDb; P62627; -.
DR PRIDE; P62627; -.
DR ProteomicsDB; 277469; -.
DR TopDownProteomics; P62627; -.
DR Antibodypedia; 4076; 78 antibodies from 21 providers.
DR Ensembl; ENSMUST00000109682; ENSMUSP00000105304; ENSMUSG00000047459.
DR GeneID; 67068; -.
DR KEGG; mmu:67068; -.
DR UCSC; uc008nkg.2; mouse.
DR CTD; 83658; -.
DR MGI; MGI:1914318; Dynlrb1.
DR VEuPathDB; HostDB:ENSMUSG00000047459; -.
DR eggNOG; KOG4115; Eukaryota.
DR GeneTree; ENSGT00390000011067; -.
DR HOGENOM; CLU_113002_3_2_1; -.
DR InParanoid; P62627; -.
DR OMA; CAMATLL; -.
DR PhylomeDB; P62627; -.
DR TreeFam; TF315165; -.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR BioGRID-ORCS; 67068; 24 hits in 70 CRISPR screens.
DR ChiTaRS; Dynlrb1; mouse.
DR EvolutionaryTrace; P62627; -.
DR PRO; PR:P62627; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P62627; protein.
DR Bgee; ENSMUSG00000047459; Expressed in embryonic brain and 255 other tissues.
DR ExpressionAtlas; P62627; baseline and differential.
DR Genevisible; P62627; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:UniProtKB.
DR GO; GO:0030286; C:dynein complex; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007632; P:visual behavior; ISS:UniProtKB.
DR InterPro; IPR016561; DYNLRB1/2.
DR InterPro; IPR004942; Roadblock/LAMTOR2_dom.
DR Pfam; PF03259; Robl_LC7; 1.
DR PIRSF; PIRSF009998; DLC7; 1.
DR SMART; SM00960; Robl_LC7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoskeleton; Dynein; Microtubule;
KW Motor protein; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62628"
FT CHAIN 2..96
FT /note="Dynein light chain roadblock-type 1"
FT /id="PRO_0000220956"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P62628"
FT CONFLICT 3
FT /note="E -> D (in Ref. 1; BAB25768)"
FT /evidence="ECO:0000305"
FT HELIX 2..13
FT /evidence="ECO:0007829|PDB:1Y4O"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:1Y4O"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1Y4O"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:1Y4O"
FT HELIX 36..60
FT /evidence="ECO:0007829|PDB:1Y4O"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:1Y4O"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1Y4O"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:1Y4O"
SQ SEQUENCE 96 AA; 10990 MW; 666734B413AFE7D0 CRC64;
MAEVEETLKR LQSQKGVQGI IVVNTEGIPI KSTMDNPTTT QYANLMHNFI LKARSTVREI
DPQNDLTFLR IRSKKNEIMV APDKDYFLIV IQNPTE
