DYLT1_MOUSE
ID DYLT1_MOUSE Reviewed; 113 AA.
AC P51807; Q5M8S6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Dynein light chain Tctex-type 1;
DE AltName: Full=Activator of G-protein signaling 2;
DE Short=AGS2;
DE AltName: Full=T-complex testis-specific protein 1;
DE AltName: Full=TCTEX-1;
GN Name=Dynlt1; Synonyms=Tctel1, Tctex-1, Tctex1;
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 [MRNA].
RC TISSUE=Testis;
RX PubMed=2570638; DOI=10.1016/0092-8674(89)90948-3;
RA Lader E., Ha H.-S., O'Neill M., Artzt K., Bennett D.;
RT "tctex-1: a candidate gene family for a mouse t complex sterility locus.";
RL Cell 58:969-979(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and 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 [4]
RP TISSUE SPECIFICITY, AND POSSIBLE FUNCTION IN AXONEMAL DYNEIN.
RX PubMed=9490726; DOI=10.1083/jcb.140.5.1137;
RA Harrison A., Olds-Clarke P., King S.M.;
RT "Identification of the t complex-encoded cytoplasmic dynein light chain
RT tctex1 in inner arm I1 supports the involvement of flagellar dyneins in
RT meiotic drive.";
RL J. Cell Biol. 140:1137-1147(1998).
RN [5]
RP FUNCTION IN RECEPTOR-INDEPENDENT ACTIVATION OF G-PROTEIN SIGNALING, AND
RP ASSOCIATION WITH GBETA-GAMMA.
RX PubMed=10559191; DOI=10.1074/jbc.274.47.33202;
RA Takesono A., Cismowski M.J., Ribas C., Bernard M., Chung P., Hazard S. III,
RA Duzic E., Lanier S.M.;
RT "Receptor-independent activators of heterotrimeric G-protein signaling
RT pathways.";
RL J. Biol. Chem. 274:33202-33205(1999).
RN [6]
RP INTERACTION WITH DYNC1I1, AND SUBUNIT.
RX PubMed=11148215; DOI=10.1074/jbc.m011358200;
RA Mok Y.K., Lo K.W., Zhang M.;
RT "Structure of Tctex-1 and its interaction with cytoplasmic dynein
RT intermediate chain.";
RL J. Biol. Chem. 276:14067-14074(2001).
RN [7]
RP SELF-ASSOCIATION.
RX PubMed=11278908; DOI=10.1074/jbc.m011456200;
RA DiBella L.M., Benashski S.E., Tedford H.W., Harrison A., Patel-King R.S.,
RA King S.M.;
RT "The Tctex1/Tctex2 class of dynein light chains. Dimerization, differential
RT expression, and interaction with the LC8 protein family.";
RL J. Biol. Chem. 276:14366-14373(2001).
RN [8]
RP FUNCTION IN NEUROGENESIS.
RX PubMed=19448628; DOI=10.1038/nn.2339;
RA Gauthier-Fisher A., Lin D.C., Greeve M., Kaplan D.R., Rottapel R.,
RA Miller F.D.;
RT "Lfc and Tctex-1 regulate the genesis of neurons from cortical precursor
RT cells.";
RL Nat. Neurosci. 12:735-744(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [10]
RP INTERACTION WITH DYNC1I2 AND DYNC1I2.
RX PubMed=27502274; DOI=10.1074/jbc.m116.736884;
RA Merino-Gracia J., Zamora-Carreras H., Bruix M., Rodriguez-Crespo I.;
RT "Molecular basis for the protein recognition specificity of the dynein
RT light chain DYNLT1/Tctex1: characterization of the interaction with activin
RT receptor IIB.";
RL J. Biol. Chem. 291:20962-20975(2016).
RN [11]
RP INTERACTION WITH DNAI4.
RX PubMed=30060180; DOI=10.1093/jmcb/mjy043;
RA Zhang Y., Chen Y., Zheng J., Wang J., Duan S., Zhang W., Yan X., Zhu X.;
RT "Vertebrate Dynein-f depends on Wdr78 for axonemal localization and is
RT essential for ciliary beat.";
RL J. Mol. Cell Biol. 11:383-394(2019).
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 Binds to transport cargos and is involved in apical cargo transport
CC such as rhodopsin-bearing vesicles in polarized epithelia (By
CC similarity). May also be a accessory component of axonemal dynein.
CC Plays an important role in male germ cell development and function.
CC Candidate for involvement in male sterility. {ECO:0000250,
CC ECO:0000269|PubMed:9490726}.
CC -!- FUNCTION: Plays a role in neuronal morphogenesis; the function is
CC independent of cytoplasmic dynein and seems to be coupled to regulation
CC of the actin cytoskeleton by enhancing Rac1 activity. The function in
CC neurogenesis may be regulated by association with a G-protein beta-
CC gamma dimer. May function as a receptor-independent activator of
CC heterotrimeric G-protein signaling; the activation appears to be
CC independent of a nucleotide exchange. Plays a role in regulating
CC neurogenesis; inhibits the genesis of neurons from precursor cells
CC during cortical development presumably by antagonizing ARHGEF2.
CC Unrelated to the role in retrograde microtubule-associated movement may
CC play a role in the dimerization of cytoplasmic proteins/domains such as
CC for ACVR2B. Binds to the cytoplasmic domain of ACVR2B and, in vitro,
CC inhibits ACVR2B signaling. Involved in the regulation of mitotic
CC spindle orientation. {ECO:0000269|PubMed:10559191,
CC ECO:0000269|PubMed:19448628}.
CC -!- SUBUNIT: Homodimer (Probable). The cytoplasmic dynein 1 complex
CC consists of two catalytic heavy chains (HCs) and a number of non-
CC catalytic subunits presented by intermediate chains (ICs), light
CC intermediate chains (LICs) and light chains (LCs); the composition
CC seems to vary in respect to the IC, LIC and LC composition. The heavy
CC chain homodimer serves as a scaffold for the probable homodimeric
CC assembly of the respective non-catalytic subunits. The ICs and LICs
CC bind directly to the HC dimer and the LCs assemble on the IC dimer.
CC DYNLT1 and DYNLT3 compete for association with dynein IC (DYNC1I1 or
CC DYNC1I2). Self-associates. Interacts with RHO (By similarity).
CC Interacts with DYNC1I1 and DYNC1I2. Interacts with DOC2A, DOC2B and
CC SCN10A. Interacts with PVR. Interacts with SVIL isoform 2. Interacts
CC with GNB1; the interaction occurs in presence of guanine nucleotide-
CC binding protein G(T) subunit gamma; the interaction diminishes the
CC association of DYNLT1 with dynein IC (DYNC1I1 or DYNC1I2). Interacts
CC with GNB2, GNB3 and GNB5; the interactions occur in presence of guanine
CC nucleotide-binding protein G(T) subunit gamma. Interacts with ACVR2B
CC and ARHGEF2 (By similarity). Interacts with DNAI4 (PubMed:30060180).
CC {ECO:0000250, ECO:0000250|UniProtKB:P63172,
CC ECO:0000269|PubMed:27502274, ECO:0000269|PubMed:30060180, ECO:0000305}.
CC -!- INTERACTION:
CC P51807; P39688: Fyn; NbExp=3; IntAct=EBI-642797, EBI-524514;
CC P51807; O46385: SVIL; Xeno; NbExp=4; IntAct=EBI-642797, EBI-6995105;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC Note=Localizes to mitotic spindles. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: High level in testis (germ cell-specific).
CC Expressed in sperm (at protein level). 200-fold lower in liver, brain,
CC heart, spleen, and kidney. Levels in thymus and two embryonal carcinoma
CC cell lines were several-fold higher than this low constitutive level.
CC {ECO:0000269|PubMed:9490726}.
CC -!- DEVELOPMENTAL STAGE: First abundantly expressed at the pachytene stage
CC of meiosis and persists throughout spermatogenesis.
CC -!- PTM: Phosphorylated by BMPR2. The phosphorylation status is proposed to
CC regulate the association with the cytoplasmic dynein complex and may
CC have role in cytoplasmic dynein cargo release (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dynein light chain Tctex-type family.
CC {ECO:0000305}.
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DR EMBL; M25825; AAA40408.1; -; mRNA.
DR EMBL; AK133788; BAE21842.1; -; mRNA.
DR EMBL; AK153971; BAE32288.1; -; mRNA.
DR EMBL; AK168478; BAE40367.1; -; mRNA.
DR EMBL; BC043018; AAH43018.1; -; mRNA.
DR EMBL; BC087868; AAH87868.1; -; mRNA.
DR CCDS; CCDS49936.1; -.
DR PIR; A32995; A32995.
DR RefSeq; NP_001160099.1; NM_001166627.1.
DR RefSeq; NP_001160101.1; NM_001166629.2.
DR RefSeq; NP_001160102.1; NM_001166630.1.
DR RefSeq; NP_033368.1; NM_009342.2.
DR RefSeq; XP_017172676.1; XM_017317187.1.
DR PDB; 5WI4; X-ray; 2.00 A; A/B/C=1-113.
DR PDBsum; 5WI4; -.
DR AlphaFoldDB; P51807; -.
DR SMR; P51807; -.
DR BioGRID; 204082; 27.
DR ComplexPortal; CPX-5699; Cytoplasmic dynein complex, variant 1.
DR IntAct; P51807; 10.
DR MINT; P51807; -.
DR STRING; 10090.ENSMUSP00000090644; -.
DR iPTMnet; P51807; -.
DR PhosphoSitePlus; P51807; -.
DR EPD; P51807; -.
DR MaxQB; P51807; -.
DR PaxDb; P51807; -.
DR PRIDE; P51807; -.
DR ProteomicsDB; 277618; -.
DR DNASU; 21648; -.
DR Ensembl; ENSMUST00000092966; ENSMUSP00000090644; ENSMUSG00000000579.
DR Ensembl; ENSMUST00000169415; ENSMUSP00000127990; ENSMUSG00000092074.
DR Ensembl; ENSMUST00000179554; ENSMUSP00000135978; ENSMUSG00000095677.
DR Ensembl; ENSMUST00000179569; ENSMUSP00000137171; ENSMUSG00000096255.
DR GeneID; 100040531; -.
DR GeneID; 100040563; -.
DR GeneID; 100310872; -.
DR GeneID; 21648; -.
DR KEGG; mmu:100040531; -.
DR KEGG; mmu:100040563; -.
DR KEGG; mmu:100310872; -.
DR KEGG; mmu:21648; -.
DR UCSC; uc008agl.3; mouse.
DR CTD; 100040531; -.
DR CTD; 100040563; -.
DR CTD; 100310872; -.
DR CTD; 21648; -.
DR MGI; MGI:98643; Dynlt1.
DR VEuPathDB; HostDB:ENSMUSG00000000579; -.
DR VEuPathDB; HostDB:ENSMUSG00000092074; -.
DR VEuPathDB; HostDB:ENSMUSG00000095677; -.
DR VEuPathDB; HostDB:ENSMUSG00000096255; -.
DR eggNOG; KOG4081; Eukaryota.
DR GeneTree; ENSGT00940000154531; -.
DR HOGENOM; CLU_097204_7_2_1; -.
DR InParanoid; P51807; -.
DR OMA; TSDACYV; -.
DR OrthoDB; 1474572at2759; -.
DR PhylomeDB; P51807; -.
DR TreeFam; TF313904; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 100040531; 8 hits in 32 CRISPR screens.
DR BioGRID-ORCS; 100040563; 7 hits in 32 CRISPR screens.
DR BioGRID-ORCS; 100310872; 7 hits in 30 CRISPR screens.
DR BioGRID-ORCS; 21648; 5 hits in 31 CRISPR screens.
DR ChiTaRS; Dynlt1c; mouse.
DR PRO; PR:P51807; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P51807; protein.
DR Bgee; ENSMUSG00000000579; Expressed in hypothalamus and 62 other tissues.
DR ExpressionAtlas; P51807; baseline and differential.
DR Genevisible; P51807; MM.
DR GO; GO:0044295; C:axonal growth cone; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR GO; GO:0030286; C:dynein complex; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0043657; C:host cell; IEA:GOC.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0099503; C:secretory vesicle; ISO:MGI.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IDA:MGI.
DR GO; GO:0030742; F:GTP-dependent protein binding; IPI:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0061564; P:axon development; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016358; P:dendrite development; ISO:MGI.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR GO; GO:0019060; P:intracellular transport of viral protein in host cell; ISO:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:MGI.
DR GO; GO:0035795; P:negative regulation of mitochondrial membrane permeability; ISO:MGI.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IMP:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:MGI.
DR GO; GO:0035022; P:positive regulation of Rac protein signal transduction; ISO:MGI.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; ISO:MGI.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISO:MGI.
DR Gene3D; 3.30.1140.40; -; 1.
DR InterPro; IPR005334; Tctex-1-like.
DR InterPro; IPR038586; Tctex-1-like_sf.
DR PANTHER; PTHR21255; PTHR21255; 1.
DR Pfam; PF03645; Tctex-1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Dynein; Golgi apparatus; Microtubule; Mitosis; Motor protein;
KW Neurogenesis; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..113
FT /note="Dynein light chain Tctex-type 1"
FT /id="PRO_0000195153"
FT REGION 41..113
FT /note="Interaction with GNB1"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P63172"
FT VARIANT 21
FT /note="V -> A"
FT HELIX 14..29
FT /evidence="ECO:0007829|PDB:5WI4"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:5WI4"
FT HELIX 39..55
FT /evidence="ECO:0007829|PDB:5WI4"
FT STRAND 60..71
FT /evidence="ECO:0007829|PDB:5WI4"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:5WI4"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:5WI4"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:5WI4"
FT STRAND 100..112
FT /evidence="ECO:0007829|PDB:5WI4"
SQ SEQUENCE 113 AA; 12483 MW; 92DF96F933DB7AF1 CRC64;
MEDFQASEET AFVVDEVSSI VKEAIESAIG GNAYQHSKVN QWTTNVLEQT LSQLTKLGRP
FKYIVTCVIM QKNGAGLHSA SSCFWDSSTD GSCTVRWENK TMYCIVSTFG LSI
