ID   DYLT3_PONAB             Reviewed;         116 AA.
AC   Q5NVF5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Dynein light chain Tctex-type 3;
GN   Name=DYNLT3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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       Probably binds BUB3 as part of transport cargo. Required for the
CC       efficient progression through mitosis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of two
CC       catalytic heavy chains (HCs) and a number of non-catalytic subunits
CC       presented by intermediate chains (ICs), light intermediate chains
CC       (LICs) and light chains (LCs); the composition seems to vary in respect
CC       to the IC, LIC and LC composition. The heavy chain homodimer serves as
CC       a scaffold for the probable homodimeric assembly of the respective non-
CC       catalytic subunits. The ICs and LICs bind directly to the HC dimer and
CC       the LCs assemble on the IC dimer. DYNLT1 and DYNLT3 compete for
CC       association with dynein IC (DYNC1I1 or DYNC1I2). Self-associates.
CC       Interacts with DYNC1I1 and DYNC1I2. Interacts with BUB3. Interacts with
CC       SATB1 in nucleus to form complex with matrix attachment regions (MARs)
CC       of DNA (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton
CC       {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dynein light chain Tctex-type family.
CC       {ECO:0000305}.
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DR   EMBL; CR926081; CAI29708.1; -; mRNA.
DR   RefSeq; NP_001127114.1; NM_001133642.1.
DR   AlphaFoldDB; Q5NVF5; -.
DR   SMR; Q5NVF5; -.
DR   STRING; 9601.ENSPPYP00000022651; -.
DR   Ensembl; ENSPPYT00000042772; ENSPPYP00000025038; ENSPPYG00000020241.
DR   GeneID; 100174155; -.
DR   KEGG; pon:100174155; -.
DR   CTD; 6990; -.
DR   eggNOG; KOG4081; Eukaryota.
DR   GeneTree; ENSGT00940000155009; -.
DR   HOGENOM; CLU_097204_7_0_1; -.
DR   InParanoid; Q5NVF5; -.
DR   OMA; LWENSTI; -.
DR   OrthoDB; 1474572at2759; -.
DR   TreeFam; TF313904; -.
DR   Proteomes; UP000001595; Chromosome X.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; 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   3: Inferred from homology;
KW   Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW   Dynein; Kinetochore; Microtubule; Mitosis; Motor protein; Nitration;
KW   Nucleus; Reference proteome; Transport.
FT   CHAIN           1..116
FT                   /note="Dynein light chain Tctex-type 3"
FT                   /id="PRO_0000244525"
FT   MOD_RES         4
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P56387"
SQ   SEQUENCE   116 AA;  13062 MW;  7DEB2A8B9D989632 CRC64;
     MEEYHRHCDE VGFNAEEAHN IVKECVDGVL GGEDYNHNNI NQWTASIVEQ SLTHLVKLGK
     AYKYIVTCAV VQKSAYGFHT ASSCFWDTTS DGTCTVRWEN RTMNCIVNVF AIAIVL