DYLT1_HUMAN
ID DYLT1_HUMAN Reviewed; 113 AA.
AC P63172; Q15763; Q5VTU4;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Dynein light chain Tctex-type 1;
DE AltName: Full=Protein CW-1;
DE AltName: Full=T-complex testis-specific protein 1 homolog;
GN Name=DYNLT1; Synonyms=TCTEL1, TCTEX-1, TCTEX1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cao X.M., Solecki D.J., Wimmer E.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RX PubMed=8646886; DOI=10.1159/000134329;
RA Watanabe T.K., Fujiwara T., Shimizu F., Okuno S., Suzuki M., Takahashi E.,
RA Nakamura Y., Hirai Y.;
RT "Cloning, expression, and mapping of TCTEL1, a putative human homologue of
RT murine Tcte1, to 6q.";
RL Cytogenet. Cell Genet. 73:153-156(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Indu S., Laloraya M., Kumar P.G.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [9]
RP INTERACTION WITH PVR.
RX PubMed=11751937; DOI=10.1074/jbc.m111937200;
RA Mueller S., Cao X., Welker R., Wimmer E.;
RT "Interaction of the poliovirus receptor CD155 with the dynein light chain
RT Tctex-1 and its implication for poliovirus pathogenesis.";
RL J. Biol. Chem. 277:7897-7904(2002).
RN [10]
RP INTERACTION WITH BMPR2, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX PubMed=14583445; DOI=10.1093/hmg/ddg365;
RA Machado R.D., Rudarakanchana N., Atkinson C., Flanagan J.A., Harrison R.,
RA Morrell N.W., Trembath R.C.;
RT "Functional interaction between BMPR-II and Tctex-1, a light chain of
RT Dynein, is isoform-specific and disrupted by mutations underlying primary
RT pulmonary hypertension.";
RL Hum. Mol. Genet. 12:3277-3286(2003).
RN [11]
RP INTERACTION WITH PVR.
RX PubMed=15194795; DOI=10.1128/jvi.78.13.7186-7198.2004;
RA Ohka S., Matsuda N., Tohyama K., Oda T., Morikawa M., Kuge S., Nomoto A.;
RT "Receptor (CD155)-dependent endocytosis of poliovirus and retrograde axonal
RT transport of the endosome.";
RL J. Virol. 78:7186-7198(2004).
RN [12]
RP INTERACTION WITH SVIL.
RX PubMed=16880273; DOI=10.1083/jcb.200512051;
RA Takizawa N., Smith T.C., Nebl T., Crowley J.L., Palmieri S.J.,
RA Lifshitz L.M., Ehrhardt A.G., Hoffman L.M., Beckerle M.C., Luna E.J.;
RT "Supervillin modulation of focal adhesions involving TRIP6/ZRP-1.";
RL J. Cell Biol. 174:447-458(2006).
RN [13]
RP SELF-ASSOCIATION, INTERACTION WITH DYNC1I1 AND DYNC1I2, AND SUBUNIT.
RX PubMed=17965411; DOI=10.1074/jbc.m705991200;
RA Lo K.W., Kogoy J.M., Rasoul B.A., King S.M., Pfister K.K.;
RT "Interaction of the DYNLT (TCTEX1/RP3) light chains and the intermediate
RT chains reveals novel intersubunit regulation during assembly of the dynein
RT complex.";
RL J. Biol. Chem. 282:36871-36878(2007).
RN [14]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH MASON-PFIZER MONKEY
RP VIRUS PROTEIN GAG (MICROBIAL INFECTION).
RX PubMed=18647839; DOI=10.1073/pnas.0801765105;
RA Vlach J., Lipov J., Rumlova M., Veverka V., Lang J., Srb P., Knejzlik Z.,
RA Pichova I., Hunter E., Hrabal R., Ruml T.;
RT "D-retrovirus morphogenetic switch driven by the targeting signal
RT accessibility to Tctex-1 of dynein.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10565-10570(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP INTERACTION WITH HUMAN PAPILLOMAVIRUS 16 L2 PROTEIN (MICROBIAL INFECTION).
RX PubMed=21166973; DOI=10.1111/j.1462-5822.2010.01515.x;
RA Schneider M.A., Spoden G.A., Florin L., Lambert C.;
RT "Identification of the dynein light chains required for human
RT papillomavirus infection.";
RL Cell. Microbiol. 13:32-46(2011).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP STRUCTURE BY NMR IN COMPLEX WITH DYNC1I2, INTERACTION WITH ACVR2B AND
RP ARHGEF2, AND FUNCTION.
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).
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. May also be
CC a accessory component of axonemal dynein.
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 Involved in the regulation of mitotic spindle orientation (By
CC similarity). Unrelated to the role in retrograde microtubule-associated
CC movement may play a role in the dimerization of cytoplasmic
CC proteins/domains such as for ACVR2B. Binds to the cytoplasmic domain of
CC ACVR2B and, in vitro, inhibits ACVR2B signaling (PubMed:27502274).
CC {ECO:0000250, ECO:0000269|PubMed:27502274}.
CC -!- FUNCTION: (Microbial infection) Is involved in intracellular targeting
CC of D-type retrovirus gag polyproteins to the cytoplasmic assembly site.
CC {ECO:0000269|PubMed:18647839}.
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 DYNC1I1 and DYNC1I2.
CC Interacts with RHO. Interacts with DOC2A, DOC2B and SCN10A. Interacts
CC with PVR. Interacts with SVIL isoform 2. Interacts with BMPR2.
CC Interacts with GNB1; the interaction occurs in presence of guanine
CC nucleotide-binding protein G(T) subunit gamma; the interaction
CC diminishes the association of DYNLT1 with dynein IC (DYNC1I1 or
CC DYNC1I2). Interacts with GNB2, GNB3 and GNB5; the interactions occur in
CC presence of guanine nucleotide-binding protein G(T) subunit gamma (By
CC similarity). Interacts with ACVR2B and ARHGEF2. Interacts with DNAI4
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P51807,
CC ECO:0000269|PubMed:11751937, ECO:0000269|PubMed:14583445,
CC ECO:0000269|PubMed:15194795, ECO:0000269|PubMed:16880273,
CC ECO:0000269|PubMed:17965411, ECO:0000269|PubMed:27502274, ECO:0000305}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human papillomavirus 16
CC L2 protein; this interaction is essential for virus intracellular
CC transport during entry. {ECO:0000269|PubMed:21166973}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Mason-Pfizer monkey virus
CC protein Gag. {ECO:0000269|PubMed:18647839}.
CC -!- INTERACTION:
CC P63172; Q9BTE6-2: AARSD1; NbExp=3; IntAct=EBI-1176455, EBI-9357295;
CC P63172; Q99424: ACOX2; NbExp=3; IntAct=EBI-1176455, EBI-12026476;
CC P63172; P12814: ACTN1; NbExp=3; IntAct=EBI-1176455, EBI-351710;
CC P63172; Q4LE39-3: ARID4B; NbExp=3; IntAct=EBI-1176455, EBI-11957452;
CC P63172; Q9H2F9: CCDC68; NbExp=3; IntAct=EBI-1176455, EBI-2813327;
CC P63172; O60884: DNAJA2; NbExp=3; IntAct=EBI-1176455, EBI-352957;
CC P63172; Q13409-3: DYNC1I2; NbExp=3; IntAct=EBI-1176455, EBI-12094038;
CC P63172; Q8WW35: DYNLT2B; NbExp=5; IntAct=EBI-1176455, EBI-2692044;
CC P63172; P51808: DYNLT3; NbExp=4; IntAct=EBI-1176455, EBI-743027;
CC P63172; Q9UBY9: HSPB7; NbExp=3; IntAct=EBI-1176455, EBI-739361;
CC P63172; Q9BQS6: HSPB9; NbExp=5; IntAct=EBI-1176455, EBI-1176448;
CC P63172; Q9H2R5: KLK15; NbExp=3; IntAct=EBI-1176455, EBI-8645371;
CC P63172; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-1176455, EBI-739832;
CC P63172; Q9P0L2: MARK1; NbExp=3; IntAct=EBI-1176455, EBI-968587;
CC P63172; P07196: NEFL; NbExp=3; IntAct=EBI-1176455, EBI-475646;
CC P63172; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-1176455, EBI-2859639;
CC P63172; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-1176455, EBI-741158;
CC P63172; Q96PB7-3: OLFM3; NbExp=3; IntAct=EBI-1176455, EBI-12005356;
CC P63172; Q9BRX2: PELO; NbExp=3; IntAct=EBI-1176455, EBI-1043580;
CC P63172; Q99697-2: PITX2; NbExp=3; IntAct=EBI-1176455, EBI-12138495;
CC P63172; P25786: PSMA1; NbExp=3; IntAct=EBI-1176455, EBI-359352;
CC P63172; P49190: PTH2R; NbExp=3; IntAct=EBI-1176455, EBI-1045772;
CC P63172; Q7L523: RRAGA; NbExp=3; IntAct=EBI-1176455, EBI-752376;
CC P63172; O00560: SDCBP; NbExp=3; IntAct=EBI-1176455, EBI-727004;
CC P63172; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-1176455, EBI-11955057;
CC P63172; Q9UBK9: UXT; NbExp=3; IntAct=EBI-1176455, EBI-357355;
CC P63172; O76024: WFS1; NbExp=3; IntAct=EBI-1176455, EBI-720609;
CC P63172; A0A0H3MBG2: CTL0223; Xeno; NbExp=5; IntAct=EBI-1176455, EBI-26359442;
CC P63172; P07567: gag; Xeno; NbExp=2; IntAct=EBI-1176455, EBI-15717123;
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: Expressed in heart, placenta, skeletal muscle
CC kidney, pancreas, spleen, prostate, testis, ovary, ileum and colon.
CC Expressed in lung endothelial and smooth muscle cells (at protein
CC level). {ECO:0000269|PubMed:14583445}.
CC -!- PTM: Phosphorylated by BMPR2; the phosphorylation is abolished by BMPR2
CC mutations in exon 12 which lead to truncated forms of BMPR2 and which
CC are linked to primary pulmonary hypertension (PPH1) [MIM:178600]. The
CC phosphorylation status is proposed to regulate the association with the
CC cytoplasmic dynein complex and may have role in cytoplasmic dynein
CC cargo release (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dynein light chain Tctex-type family.
CC {ECO:0000305}.
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DR EMBL; U56255; AAB03318.1; -; mRNA.
DR EMBL; D50663; BAA09317.1; -; mRNA.
DR EMBL; EU862237; ACF74976.1; -; mRNA.
DR EMBL; AK315601; BAG37971.1; -; mRNA.
DR EMBL; CR456931; CAG33212.1; -; mRNA.
DR EMBL; AL591025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47657.1; -; Genomic_DNA.
DR EMBL; BC029412; AAH29412.1; -; mRNA.
DR EMBL; BC105588; AAI05589.1; -; mRNA.
DR CCDS; CCDS5257.1; -.
DR RefSeq; NP_006510.1; NM_006519.3.
DR PDB; 5JPW; NMR; -; A/B=1-113.
DR PDBsum; 5JPW; -.
DR AlphaFoldDB; P63172; -.
DR SMR; P63172; -.
DR BioGRID; 112853; 223.
DR ComplexPortal; CPX-5025; Cytoplasmic dynein complex, variant 1.
DR CORUM; P63172; -.
DR DIP; DIP-35251N; -.
DR IntAct; P63172; 62.
DR MINT; P63172; -.
DR STRING; 9606.ENSP00000356056; -.
DR GlyGen; P63172; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P63172; -.
DR PhosphoSitePlus; P63172; -.
DR SwissPalm; P63172; -.
DR BioMuta; DYNLT1; -.
DR DMDM; 52783582; -.
DR EPD; P63172; -.
DR jPOST; P63172; -.
DR MassIVE; P63172; -.
DR PaxDb; P63172; -.
DR PeptideAtlas; P63172; -.
DR PRIDE; P63172; -.
DR ProteomicsDB; 57502; -.
DR TopDownProteomics; P63172; -.
DR ABCD; P63172; 1 sequenced antibody.
DR Antibodypedia; 33440; 80 antibodies from 23 providers.
DR DNASU; 6993; -.
DR Ensembl; ENST00000367089.8; ENSP00000356056.3; ENSG00000146425.11.
DR GeneID; 6993; -.
DR KEGG; hsa:6993; -.
DR MANE-Select; ENST00000367089.8; ENSP00000356056.3; NM_006519.4; NP_006510.1.
DR UCSC; uc003qrn.3; human.
DR CTD; 6993; -.
DR DisGeNET; 6993; -.
DR GeneCards; DYNLT1; -.
DR HGNC; HGNC:11697; DYNLT1.
DR HPA; ENSG00000146425; Low tissue specificity.
DR MIM; 601554; gene.
DR neXtProt; NX_P63172; -.
DR OpenTargets; ENSG00000146425; -.
DR PharmGKB; PA36416; -.
DR VEuPathDB; HostDB:ENSG00000146425; -.
DR eggNOG; KOG4081; Eukaryota.
DR GeneTree; ENSGT00940000154531; -.
DR HOGENOM; CLU_097204_7_2_1; -.
DR InParanoid; P63172; -.
DR OMA; TSDACYV; -.
DR OrthoDB; 1474572at2759; -.
DR PhylomeDB; P63172; -.
DR TreeFam; TF313904; -.
DR PathwayCommons; P63172; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P63172; -.
DR BioGRID-ORCS; 6993; 22 hits in 1080 CRISPR screens.
DR ChiTaRS; DYNLT1; human.
DR GeneWiki; DYNLT1; -.
DR GenomeRNAi; 6993; -.
DR Pharos; P63172; Tbio.
DR PRO; PR:P63172; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P63172; protein.
DR Bgee; ENSG00000146425; Expressed in bronchial epithelial cell and 209 other tissues.
DR Genevisible; P63172; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:GO_Central.
DR GO; GO:0030286; C:dynein complex; IPI:ComplexPortal.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043657; C:host cell; IEA:GOC.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0099503; C:secretory vesicle; IDA:GO_Central.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR GO; GO:0019060; P:intracellular transport of viral protein in host cell; IMP:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-KW.
DR GO; GO:0050768; P:negative regulation of neurogenesis; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
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 Cytoplasmic inwards viral transport; Cytoskeleton; Dynein; Golgi apparatus;
KW Host-virus interaction; Microtubular inwards viral transport; Microtubule;
KW Mitosis; Motor protein; Neurogenesis; Phosphoprotein; Reference proteome;
KW Transport; Virus entry into host cell.
FT CHAIN 1..113
FT /note="Dynein light chain Tctex-type 1"
FT /id="PRO_0000195152"
FT REGION 41..113
FT /note="Interaction with GNB1"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT HELIX 1..3
FT /evidence="ECO:0007829|PDB:5JPW"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:5JPW"
FT HELIX 14..29
FT /evidence="ECO:0007829|PDB:5JPW"
FT HELIX 38..57
FT /evidence="ECO:0007829|PDB:5JPW"
FT STRAND 62..71
FT /evidence="ECO:0007829|PDB:5JPW"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:5JPW"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:5JPW"
FT STRAND 87..98
FT /evidence="ECO:0007829|PDB:5JPW"
FT STRAND 100..111
FT /evidence="ECO:0007829|PDB:5JPW"
SQ SEQUENCE 113 AA; 12452 MW; A6BAD1D0744D1AA6 CRC64;
MEDYQAAEET AFVVDEVSNI VKEAIESAIG GNAYQHSKVN QWTTNVVEQT LSQLTKLGKP
FKYIVTCVIM QKNGAGLHTA SSCFWDSSTD GSCTVRWENK TMYCIVSAFG LSI
