DYLT1_BOVIN
ID DYLT1_BOVIN Reviewed; 113 AA.
AC P63171; Q15763; Q32PD4;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Dynein light chain Tctex-type 1;
DE AltName: Full=T-complex testis-specific protein 1 homolog;
GN Name=DYNLT1; Synonyms=TCTEL, TCTEX-1, TCTEX1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Retina;
RX PubMed=9677391; DOI=10.1074/jbc.273.31.19639;
RA Tai A.W., Chuang J.-Z., Sung C.-H.;
RT "Localization of Tctex-1, a cytoplasmic dynein light chain, to the Golgi
RT apparatus and evidence for dynein complex heterogeneity.";
RL J. Biol. Chem. 273:19639-19649(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION IN CYTOPLASMIC DYNEIN 1, AND SUBUNIT.
RX PubMed=11425878; DOI=10.1083/jcb.153.7.1499;
RA Tai A.W., Chuang J.Z., Sung C.H.;
RT "Cytoplasmic dynein regulation by subunit heterogeneity and its role in
RT apical transport.";
RL J. Cell Biol. 153:1499-1509(2001).
RN [4]
RP SUBUNIT, AND IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 1 COMPLEX.
RX PubMed=11967380; DOI=10.1110/ps.2520102;
RA King S.J., Bonilla M., Rodgers M.E., Schroer T.A.;
RT "Subunit organization in cytoplasmic dynein subcomplexes.";
RL Protein Sci. 11:1239-1250(2002).
RN [5]
RP INTERACTION WITH RHO, MUTAGENESIS OF SER-82, AND FUNCTION IN CYTOPLASMIC
RP DYNEIN 1.
RX PubMed=16956385; DOI=10.1111/j.1600-0854.2006.00482.x;
RA Yeh T.Y., Peretti D., Chuang J.Z., Rodriguez-Boulan E., Sung C.H.;
RT "Regulatory dissociation of Tctex-1 light chain from dynein complex is
RT essential for the apical delivery of rhodopsin.";
RL Traffic 7:1495-1502(2006).
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 (By similarity).
CC {ECO:0000250}.
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. Unrelated to
CC the role in retrograde microtubule-associated movement may play a role
CC in the dimerization of cytoplasmic proteins/domains such as for ACVR2B.
CC Binds to the cytoplasmic domain of ACVR2B and, in vitro, inhibits
CC ACVR2B signaling (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P63172}.
CC -!- SUBUNIT: Homodimer (By similarity). 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 non-catalytic subunits. The ICs and LICs bind directly
CC to the HC dimer and the LCs assemble on the IC dimer. DYNLT1 and DYNLT3
CC compete for association with dynein IC (DYNC1I1 or DYNC1I2). Self-
CC associates. Interacts with RHO. Interacts with DYNC1I1 and DYNC1I2.
CC Interacts with DOC2A, DOC2B and SCN10A. Interacts with PVR. Interacts
CC with SVIL isoform 2. Interacts with GNB1; the interaction occurs in
CC presence of guanine nucleotide-binding protein G(T) subunit gamma; the
CC interaction diminishes the association of DYNLT1 with dynein IC
CC (DYNC1I1 or DYNC1I2). Interacts with GNB2, GNB3 and GNB5; the
CC interactions occur in presence of guanine nucleotide-binding protein
CC G(T) subunit gamma. Interacts with ACVR2B and ARHGEF2 (By similarity).
CC Interacts with DNAI4 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P51807, ECO:0000250|UniProtKB:P63172}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:9677391}.
CC Cytoplasm {ECO:0000269|PubMed:9677391}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000269|PubMed:9677391}. Note=Localizes to mitotic
CC spindles.
CC -!- PTM: Phosphorylated by BMPR2 (By similarity). The phosphorylation
CC status is proposed to regulate the association with the cytoplasmic
CC dynein complex and may have role in cytoplasmic dynein cargo release.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dynein light chain Tctex-type family.
CC {ECO:0000305}.
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DR EMBL; AF067370; AAC39268.1; -; mRNA.
DR EMBL; BC108160; AAI08161.1; -; mRNA.
DR RefSeq; NP_777045.1; NM_174620.2.
DR AlphaFoldDB; P63171; -.
DR SMR; P63171; -.
DR STRING; 9913.ENSBTAP00000005869; -.
DR iPTMnet; P63171; -.
DR PaxDb; P63171; -.
DR PRIDE; P63171; -.
DR GeneID; 282380; -.
DR KEGG; bta:282380; -.
DR CTD; 6993; -.
DR eggNOG; KOG4081; Eukaryota.
DR HOGENOM; CLU_097204_7_2_1; -.
DR InParanoid; P63171; -.
DR OrthoDB; 1474572at2759; -.
DR TreeFam; TF313904; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
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:0043001; P:Golgi to plasma membrane protein transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; TAS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
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 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 Acetylation; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Dynein;
KW Golgi apparatus; Microtubule; Mitosis; Motor protein; Neurogenesis;
KW Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..113
FT /note="Dynein light chain Tctex-type 1"
FT /id="PRO_0000195151"
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 MUTAGEN 82
FT /note="S->A: No effect on interaction with dynein
FT intermediate chain (DYNC1I1 or DYNC1I2). No effect in
FT interaction with RHO. Mislocation of rhodopsin to
FT basolateral surface of polarized epithelial cells."
FT /evidence="ECO:0000269|PubMed:16956385"
FT MUTAGEN 82
FT /note="S->E: Impairs interaction with dynein intermediate
FT chain (DYNC1I1 or DYNC1I2). No effect in interaction with
FT RHO. Mislocation of rhodopsin to apical and lateral
FT surfaces of polarized epithelial cells."
FT /evidence="ECO:0000269|PubMed:16956385"
SQ SEQUENCE 113 AA; 12452 MW; A6BAD1D0744D1AA6 CRC64;
MEDYQAAEET AFVVDEVSNI VKEAIESAIG GNAYQHSKVN QWTTNVVEQT LSQLTKLGKP
FKYIVTCVIM QKNGAGLHTA SSCFWDSSTD GSCTVRWENK TMYCIVSAFG LSI
