ID   DC1L2_PONAB             Reviewed;         492 AA.
AC   Q5RE09;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Cytoplasmic dynein 1 light intermediate chain 2;
DE   AltName: Full=Dynein light intermediate chain 2, cytosolic;
GN   Name=DYNC1LI2; Synonyms=DNCLI2;
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=Kidney;
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. May
CC       play a role in binding dynein to membranous organelles or chromosomes.
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 respective non-catalytic subunits. The ICs and LICs
CC       bind directly to the HC dimer and the LCs assemble on the IC dimer.
CC       Self-associates. Interacts with DYNC1H1; DYNC1LI1 and DYNC1LI2 bind
CC       mutually exclusive to DYNC1H1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dynein light intermediate chain family.
CC       {ECO:0000305}.
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DR   EMBL; CR857730; CAH89998.1; -; mRNA.
DR   RefSeq; NP_001124948.1; NM_001131476.1.
DR   AlphaFoldDB; Q5RE09; -.
DR   SMR; Q5RE09; -.
DR   STRING; 9601.ENSPPYP00000008390; -.
DR   GeneID; 100171820; -.
DR   KEGG; pon:100171820; -.
DR   CTD; 1783; -.
DR   eggNOG; KOG3905; Eukaryota.
DR   InParanoid; Q5RE09; -.
DR   OrthoDB; 1299592at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005868; C:cytoplasmic dynein complex; IEA:InterPro.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR008467; Dynein1_light_intermed_chain.
DR   InterPro; IPR022780; Dynein_light_int_chain.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12688; PTHR12688; 1.
DR   Pfam; PF05783; DLIC; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Dynein; Methylation; Microtubule;
KW   Motor protein; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Transport.
FT   CHAIN           1..492
FT                   /note="Cytoplasmic dynein 1 light intermediate chain 2"
FT                   /id="PRO_0000114673"
FT   REGION          187..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..470
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         61..68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         194
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43237"
FT   MOD_RES         383
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43237"
FT   MOD_RES         391
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43237"
FT   MOD_RES         397
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O43237"
FT   MOD_RES         441
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O43237"
FT   MOD_RES         443
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43237"
FT   MOD_RES         446
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43237"
SQ   SEQUENCE   492 AA;  54060 MW;  BF9018C1278B5506 CRC64;
     MAPVGVEKKL LLGPNGPAVA AAGDLTSEEE EGQSLWSSIL SEVSTRAGSK LPSGKNILVF
     GEDGSGKTTL MTKLQGAEHG KKGRGLEYLY LSVHDEDRDD HTRCNVWILD GDLYHKGLLK
     FAVSAESLPE TLVIFVADMS RPWTVMESLQ KWASVLREHI DKMKIPPEKM RELERKFVKD
     FQDYMEPEEG CQGSPQRRGP LTSGSDEENV ALPLGDNVLT HNLGIPVLVV CTKCDAVSVL
     EKEHDYRDEH LDFIQSHLRR FCLQYGAALI YTSVKEEKNL DLLYKYIVHK TYGFHFTTPA
     LVVEKDAVFI PAGWDNEKKI AILHENFTTV KPEDAYEDFI VKPPVRKLVH DKELAAEDEQ
     VFLMKQQSLL AKQPATPTRA SESPARGPSG SPRTQGRGGP ASVPSSFPGT SVKKPDPNIK
     NNAASEGVLA SFFNSLLSKK TGSPGSPGAG GVQSTAKKSG QKTVLSNVQE ELDRMTRKPD
     SMVTNSSTEN EA