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Database: UniProt
Entry: A0A067QP10_ZOONE
LinkDB: A0A067QP10_ZOONE
Original site: A0A067QP10_ZOONE 
ID   A0A067QP10_ZOONE        Unreviewed;       489 AA.
AC   A0A067QP10;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Dynein light intermediate chain {ECO:0000256|RuleBase:RU366047};
GN   ORFNames=L798_14963 {ECO:0000313|EMBL:KDR11321.1};
OS   Zootermopsis nevadensis (Dampwood termite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC   Termopsidae; Zootermopsis.
OX   NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR11321.1, ECO:0000313|Proteomes:UP000027135};
RN   [1] {ECO:0000313|EMBL:KDR11321.1, ECO:0000313|Proteomes:UP000027135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KDR11321.1};
RX   PubMed=24845553; DOI=10.1038/ncomms4636;
RA   Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA   Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA   Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA   Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA   Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA   Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA   Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA   Liebig J.;
RT   "Molecular traces of alternative social organization in a termite genome.";
RL   Nat. Commun. 5:3636-3636(2014).
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       {ECO:0000256|RuleBase:RU366047}.
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).
CC       {ECO:0000256|RuleBase:RU366047}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|RuleBase:RU366047}.
CC   -!- SIMILARITY: Belongs to the dynein light intermediate chain family.
CC       {ECO:0000256|ARBA:ARBA00006831, ECO:0000256|RuleBase:RU366047}.
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DR   EMBL; KK853103; KDR11321.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067QP10; -.
DR   STRING; 136037.A0A067QP10; -.
DR   EnsemblMetazoa; KDR11321; KDR11321; L798_14963.
DR   eggNOG; KOG3905; Eukaryota.
DR   InParanoid; A0A067QP10; -.
DR   OMA; FKHNVID; -.
DR   OrthoDB; 179830at2759; -.
DR   Proteomes; UP000027135; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005868; C:cytoplasmic dynein complex; IEA:UniProtKB-UniRule.
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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR008467; Dynein1_light_intermed_chain.
DR   InterPro; IPR022780; Dynein_light_int_chain.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12688; DYNEIN LIGHT INTERMEDIATE CHAIN; 1.
DR   PANTHER; PTHR12688:SF0; DYNEIN LIGHT INTERMEDIATE CHAIN; 1.
DR   Pfam; PF05783; DLIC; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU366047};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU366047};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW   ECO:0000256|RuleBase:RU366047}; Dynein {ECO:0000256|RuleBase:RU366047};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU366047};
KW   Motor protein {ECO:0000256|RuleBase:RU366047};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU366047};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027135};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366047}.
FT   REGION          366..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          145..172
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        366..399
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..477
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   489 AA;  54767 MW;  F390AA9A8DE7B72C CRC64;
     MAPVIENVGV NGFLSKKKEE ADNKENLWSA ILGDVQTRGN TKLPSYKSVL VLGDNESGKT
     TLIAKLQGVE DPKKGSGLEY AYIDVRDEYR DDHTRLSVWV LDGDPSHAHL LRFALSEESF
     PHTLVMFVVA MTTPWGILDQ LQTWATVLQD HIDRLKINID DLQDARHKYV KKWQDYVEPG
     DELEQGSPMR RTSRNLDEEG GDILPLGDGV LTRNLGLDVV VVVTKTDYMS TLEKDYDYRD
     EHFDFMQQWI RRFCLQYGAA LFYTSAKEDK NCDLLYKYLT HRIYGFPFRT PALVVEKDAV
     LIPSGWDNMK KISILYENMQ SMKPDDYYRD VIVQPVLRKP VTRESETQAE DEQSFLTRQL
     QLLQQGAPSL RQDSSPMRTP AGVQKTGDRR TSGSPGVQGQ LGSPKKIDGS KPGVAGSGEG
     VLANFFNSLL HKKTGAGSPA PKMSADLANE RPHTSVDKAV MRSDAAAELD RLTRGKKSSV
     SPDQSSSDC
//
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