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Database: UniProt
Entry: A0A085M6V5_9BILA
LinkDB: A0A085M6V5_9BILA
Original site: A0A085M6V5_9BILA 
ID   A0A085M6V5_9BILA        Unreviewed;       478 AA.
AC   A0A085M6V5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Dynein light intermediate chain {ECO:0000256|RuleBase:RU366047};
GN   ORFNames=M513_06261 {ECO:0000313|EMBL:KFD52951.1}, M514_06261
GN   {ECO:0000313|EMBL:KFD68007.1};
OS   Trichuris suis (pig whipworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD52951.1, ECO:0000313|Proteomes:UP000030764};
RN   [1] {ECO:0000313|EMBL:KFD52951.1, ECO:0000313|Proteomes:UP000030764}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD68007.1}, and DCEP-RM93M
RC   {ECO:0000313|EMBL:KFD52951.1};
RX   PubMed=24929829; DOI=10.1038/ng.3012;
RA   Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA   Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA   Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT   "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL   Nat. Genet. 46:701-706(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; KL363222; KFD52951.1; -; Genomic_DNA.
DR   EMBL; KL367509; KFD68007.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A085M6V5; -.
DR   Proteomes; UP000030758; Unassembled WGS sequence.
DR   Proteomes; UP000030764; 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   CDD; cd00882; Ras_like_GTPase; 1.
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   PRINTS; PR00449; RASTRNSFRMNG.
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   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   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366047}.
FT   REGION          360..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   478 AA;  53014 MW;  6C3E0071C924D3D5 CRC64;
     MAVMAPDDDL WSKLLHDVQY RSMNNLPNGS VLVLGDNNCG KTSLLARLQG IDDPKKGAGL
     EYHVLEINPD YKNGSYAYQL SNALPDVSPG ESLRLGVWVL DGDPFYSPLI SLALTPETLK
     HSVAVICCSM AEPWNIMETL SRWAKVLAEH LTSSSMYDND VLSECKEQLV RFWQEYVEPL
     DSSSHSDLGN KVPSMETDQF LLPLSESILS NNIGVPLIVV LTKCDMISSL EKDYDLRDEH
     FDFLQAHVRR FCLNYGAAIV YTNAKEGRNC DTLYKYILHR IYGFPFTQAA SVLERDSVFV
     PAGWDTINKI KILEEAFISV SSTESFEKCI RKPAARRTSQ KEVVVRVEDE NRFLNKVQTT
     LSAHAPNNSS ASHRGQDPAL NISSSKGAER KLTSTPSNGL LTPSGPAKKV DTQSKSVSQV
     PQPEGALAQF FNNLLIKKAG LSQIPTQPGR PPSPKQCVPS EALKELRDKA TDETSFEE
//
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