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P51807 (DYLT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dynein light chain Tctex-type 1
Alternative name(s):
Activator of G-protein signaling 2
Short name=AGS2
T-complex testis-specific protein 1
TCTEX-1
Gene names
Name:Dynlt1
Synonyms:Tctel1, Tctex-1, Tctex1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length113 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Binds to transport cargos and is involved in apical cargo transport such as rhodopsin-bearing vesicles in polarized epithelia. Is involved in intracellular targeting of D-type retrovirus gag polyproteins to the cytoplasmic assembly site By similarity. May also be a accessory component of axonemal dynein. Plays an important role in male germ cell development and function. Candidate for involvement in male sterility. Ref.4 Ref.5 Ref.8

Plays a role in neuronal morphogenesis; the function is independent of cytoplasmic dynein and seems to be coupled to regulation of the actin cytoskeleton by enhancing Rac1 activity. The function in neurogenesis may be regulated by association with a G-protein beta-gamma dimer. May function as a receptor-independent activator of heterotrimeric G-protein signaling; the activation appears to be independent of a nucleotide exchange. Plays a role in regulating neurogenesis; inhibits the genesis of neurons from precursor cells during cortical development presumably by antagonizing ARHGEF2. Involved in the regulation of mitotic spindle orientation. Ref.4 Ref.5 Ref.8

Subunit structure

Homodimer Probable. 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. DYNLT1 and DYNLT3 compete for association with dynein IC (DYNC1I1 or DYNC1I2). Self-associates. Interacts with RHO By similarity. Interacts with DYNC1I1 and DYNC1I2. Interacts with DOC2A, DOC2B and SCN10A. Interacts with PVR. Interacts with SVIL isoform 2 Interacts with GNB1; the interaction occurs in presence of guanine nucleotide-binding protein G(T) subunit gamma; the interaction diminishes the association of DYNLT1 with dynein IC (DYNC1I1 or DYNC1I2). Interacts with GNB2, GNB3 and GNB5; the interactions occur in presence of guanine nucleotide-binding protein G(T) subunit gamma By similarity. Ref.6

Subcellular location

Golgi apparatus By similarity. Cytoplasm By similarity. Cytoplasmcytoskeletonspindle By similarity. Note: Localizes to mitotic spindles By similarity.

Tissue specificity

High level in testis (germ cell-specific). Expressed in sperm (at protein level). 200-fold lower in liver, brain, heart, spleen, and kidney. Levels in thymus and two embryonal carcinoma cell lines were several-fold higher than this low constitutive level. Ref.4

Developmental stage

First abundantly expressed at the pachytene stage of meiosis and persists throughout spermatogenesis.

Post-translational modification

Phosphorylated by BMPR2. The phosphorylation status is proposed to regulate the association with the cytoplasmic dynein complex and may have role in cytoplasmic dynein cargo release By similarity.

Sequence similarities

Belongs to the dynein light chain Tctex-type family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FynP396883EBI-642797,EBI-524514
SVILO463854EBI-642797,EBI-6995105From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 113113Dynein light chain Tctex-type 1
PRO_0000195153

Regions

Region41 – 11373Interaction with GNB1 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Natural variations

Natural variant211V → A.

Sequences

Sequence LengthMass (Da)Tools
P51807 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 92DF96F933DB7AF1

FASTA11312,483
        10         20         30         40         50         60 
MEDFQASEET AFVVDEVSSI VKEAIESAIG GNAYQHSKVN QWTTNVLEQT LSQLTKLGRP 

        70         80         90        100        110 
FKYIVTCVIM QKNGAGLHSA SSCFWDSSTD GSCTVRWENK TMYCIVSTFG LSI 

« Hide

References

« Hide 'large scale' references
[1]"tctex-1: a candidate gene family for a mouse t complex sterility locus."
Lader E., Ha H.-S., O'Neill M., Artzt K., Bennett D.
Cell 58:969-979(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"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. expand/collapse author list , 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 and NOD.
Tissue: Liver and Thymus.
[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].
Strain: C57BL/6.
Tissue: Brain and Testis.
[4]"Identification of the t complex-encoded cytoplasmic dynein light chain tctex1 in inner arm I1 supports the involvement of flagellar dyneins in meiotic drive."
Harrison A., Olds-Clarke P., King S.M.
J. Cell Biol. 140:1137-1147(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, POSSIBLE FUNCTION IN AXONEMAL DYNEIN.
[5]"Receptor-independent activators of heterotrimeric G-protein signaling pathways."
Takesono A., Cismowski M.J., Ribas C., Bernard M., Chung P., Hazard S. III, Duzic E., Lanier S.M.
J. Biol. Chem. 274:33202-33205(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN RECEPTOR-INDEPENDENT ACTIVATION OF G-PROTEIN SIGNALING, ASSOCIATION WITH GBETA-GAMMA.
[6]"Structure of Tctex-1 and its interaction with cytoplasmic dynein intermediate chain."
Mok Y.K., Lo K.W., Zhang M.
J. Biol. Chem. 276:14067-14074(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DYNC1I1, SUBUNIT.
[7]"The Tctex1/Tctex2 class of dynein light chains. Dimerization, differential expression, and interaction with the LC8 protein family."
DiBella L.M., Benashski S.E., Tedford H.W., Harrison A., Patel-King R.S., King S.M.
J. Biol. Chem. 276:14366-14373(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SELF-ASSOCIATION.
[8]"Lfc and Tctex-1 regulate the genesis of neurons from cortical precursor cells."
Gauthier-Fisher A., Lin D.C., Greeve M., Kaplan D.R., Rottapel R., Miller F.D.
Nat. Neurosci. 12:735-744(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NEUROGENESIS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M25825 mRNA. Translation: AAA40408.1.
AK133788 mRNA. Translation: BAE21842.1.
AK153971 mRNA. Translation: BAE32288.1.
AK168478 mRNA. Translation: BAE40367.1.
BC043018 mRNA. Translation: AAH43018.1.
BC087868 mRNA. Translation: AAH87868.1.
CCDSCCDS49936.1.
PIRA32995.
RefSeqNP_001160099.1. NM_001166627.1.
NP_001160101.1. NM_001166629.2.
NP_001160102.1. NM_001166630.1.
NP_033368.1. NM_009342.2.
UniGeneMm.1948.
Mm.381893.
Mm.428775.
Mm.457381.
Mm.457987.
Mm.458102.
Mm.458208.
Mm.463722.

3D structure databases

ProteinModelPortalP51807.
SMRP51807. Positions 12-113.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204082. 2 interactions.
IntActP51807. 9 interactions.
MINTMINT-7901686.

PTM databases

PhosphoSiteP51807.

Proteomic databases

MaxQBP51807.
PaxDbP51807.
PRIDEP51807.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000092966; ENSMUSP00000090644; ENSMUSG00000000579.
ENSMUST00000169415; ENSMUSP00000127990; ENSMUSG00000092074.
ENSMUST00000179554; ENSMUSP00000135978; ENSMUSG00000095677.
ENSMUST00000179569; ENSMUSP00000137171; ENSMUSG00000096255.
GeneID100040531.
100040563.
100310872.
21648.
KEGGmmu:100040531.
mmu:100040563.
mmu:100310872.
mmu:21648.
UCSCuc008agl.2. mouse.

Organism-specific databases

CTD100040531.
100040563.
100310872.
21648.
MGIMGI:98643. Dynlt1.

Phylogenomic databases

eggNOGNOG278055.
GeneTreeENSGT00390000013998.
HOGENOMHOG000255148.
HOVERGENHBG001217.
InParanoidQ5M8S6.
KOK10420.
OMASCFWDNS.
OrthoDBEOG7PK918.
PhylomeDBP51807.
TreeFamTF313904.

Gene expression databases

BgeeP51807.
CleanExMM_DYNLT1.
GenevestigatorP51807.

Family and domain databases

InterProIPR005334. Tctex.
[Graphical view]
PANTHERPTHR21255. PTHR21255. 1 hit.
PfamPF03645. Tctex-1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio300916.
PROP51807.
SOURCESearch...

Entry information

Entry nameDYLT1_MOUSE
AccessionPrimary (citable) accession number: P51807
Secondary accession number(s): Q5M8S6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot