P62627 (DLRB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dynein light chain roadblock-type 1

Alternative name(s):
Dynein light chain 2A, cytoplasmic

Gene names

Name:	Dynlrb1
Synonyms:	Dncl2a, Dnlc2a

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	96 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.
Subunit structure	Homodimer. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Interacts with DYNC1I1 and DYNC1I2. Self-associates. Interacts with DYNLRB2. Interacts with RAB6A; the interaction is direct. Interacts with RAB6B (GDP-bound) By similarity. Ref.4 Ref.5
Subcellular location	Cytoplasm › cytoskeleton.
Sequence similarities	Belongs to the GAMAD family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm Cytoskeleton Dynein Microtubule
Molecular function	Motor protein
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	transport Inferred from electronic annotation. Source: UniProtKB-KW visual behavior Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	centrosome Inferred from electronic annotation. Source: Compara cytoplasmic dynein complex Inferred from direct assay Ref.4. Source: UniProtKB microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	motor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 96

95

Dynein light chain roadblock-type 1

PRO_0000220956

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Experimental info

Sequence conflict

3

1

E → D in BAB25768. Ref.1

Secondary structure

1

.

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96

Helix Strand Turn

Details...

Helix

2 – 13

12

Beta strand

17 – 24

8

Turn

25 – 27

3

Beta strand

28 – 34

7

Helix

36 – 60

25

Beta strand

66 – 75

10

Beta strand

77 – 82

6

Beta strand

84 – 92

9

Sequences

	Sequence		Length	Mass (Da)
	P62627 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 666734B413AFE7D0	FASTA	96	10,990
	10 20 30 40 50 60 MAEVEETLKR LQSQKGVQGI IVVNTEGIPI KSTMDNPTTT QYANLMHNFI LKARSTVREI 70 80 90 DPQNDLTFLR IRSKKNEIMV APDKDYFLIV IQNPTE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryo, Kidney and Small intestine.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Oocyte.
[4]	"The Roadblock light chains are ubiquitous components of cytoplasmic dynein that form homo- and heterodimers." Nikulina K., Patel-King R.S., Takebe S., Pfister K.K., King S.M. Cell Motil. Cytoskeleton 57:233-245(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SELF-ASSOCIATION, INTERACTION WITH DYNLRB2, IDENTIFICATION IN THE CYTOPLASMIC DYNEIN I COMPLEX.
[5]	"Solution structure of isoform 1 of Roadblock/LC7, a light chain in the dynein complex." Song J., Tyler R.C., Lee M.S., Tyler E.M., Markley J.L. J. Mol. Biol. 354:1043-1051(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 2-96, SUBUNIT, INTERACTION WITH DYNC1I1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK002359 mRNA. Translation: BAB22038.1.
AK003435 mRNA. Translation: BAB22788.1.
AK008595 mRNA. Translation: BAB25768.1.
AK166685 mRNA. Translation: BAE38944.1.
AL929588 Genomic DNA. Translation: CAM27181.1.
BC099423 mRNA. Translation: AAH99423.1.
BC125610 mRNA. Translation: AAI25611.1.
BC125648 mRNA. Translation: AAI25649.1.

IPI

IPI00315225.

RefSeq

NP_080223.2. NM_025947.3.

UniGene

Mm.23693.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Y4O	NMR	-	A/B	2-96	[»]

ProteinModelPortal

P62627.

SMR

P62627. Positions 2-95.

ModBase

Search...

Protein-protein interaction databases

STRING

10090.ENSMUSP00000114928.

PTM databases

PhosphoSite

P62627.

2D gel databases

UCD-2DPAGE

P62627.

Proteomic databases

PaxDb

P62627.

PRIDE

P62627.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000109682; ENSMUSP00000105304; ENSMUSG00000047459.

GeneID

67068.

KEGG

mmu:67068.

UCSC

uc008nkg.2. mouse.

Organism-specific databases

CTD

83658.

MGI

MGI:1914318. Dynlrb1.

Phylogenomic databases

eggNOG

NOG309619.

GeneTree

ENSGT00390000011067.

HOGENOM

HOG000232033.

HOVERGEN

HBG058598.

KO

K10419.

OrthoDB

EOG47PX7H.

Gene expression databases

ArrayExpress

P62627.

Bgee

P62627.

CleanEx

MM_DYNLRB1.

Genevestigator

P62627.

GermOnline

ENSMUSG00000047459. Mus musculus.

Family and domain databases

InterPro

IPR004942. Dynein_light-rel.
IPR016561. Dynein_light_roadblock-type.
[Graphical view]

Pfam

PF03259. Robl_LC7. 1 hit.
[Graphical view]

PIRSF

PIRSF009998. DLC7. 1 hit.

SMART

SM00960. Robl_LC7. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

DYNLRB1. mouse.

EvolutionaryTrace

P62627.

NextBio

323476.

SOURCE

Search...

Entry information

Entry name

DLRB1_MOUSE

Accession

Primary (citable) accession number: P62627
Secondary accession number(s): A2AVR8 , O88567, Q4FZJ8, Q9D812

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 77 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program