ID A0A016T3C5_9BILA Unreviewed; 449 AA.
AC A0A016T3C5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 28-JUN-2023, entry version 26.
DE RecName: Full=Dynein light intermediate chain {ECO:0000256|RuleBase:RU366047};
GN Name=Acey_s0143.g2364 {ECO:0000313|EMBL:EYB97059.1};
GN Synonyms=Acey-dli-1 {ECO:0000313|EMBL:EYB97059.1};
GN ORFNames=Y032_0143g2364 {ECO:0000313|EMBL:EYB97059.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB97059.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYB97059.1}.
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DR EMBL; JARK01001479; EYB97059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016T3C5; -.
DR STRING; 53326.A0A016T3C5; -.
DR Proteomes; UP000024635; 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; 2.
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};
KW Dynein {ECO:0000256|ARBA:ARBA00023017, 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:UP000024635};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366047}.
SQ SEQUENCE 449 AA; 48918 MW; A8BC74BA39C101FB CRC64;
MVASELTAGF SLPTTGSSAA LSSMHPQEDE KLWTRILSEV SSKSSSTFQG GTLIILGENQ
SGKSSLLARL EKNESQGERS ALEYHFLNVQ NDFRDGSYAY QLGTAGGLGP AENFSLPVGS
TVYSAESFSL AVWMLDGEEC FAPLIQYALP LPSPAKTVVL LVAALDNPSL IHSIRRWANV
ITQQVIQKYD KNTITEARKM QERFWQEYVE PVESSMTSSM APGALDDAGL LPLEQGVLTE
NCGVSFVVVI TKSDLCNDLT DQQADRILVQ VRRLCLQLGA ALVYTSAKNV KNIQVLYKYV
VHRAYGFPFT STAQLIERDS VFVPAGWDGE KKIEIVKEGL SDVDSVLEPT REKPTIIREQ
LVEAEDEQVF LQRLAAAESA APAAQKKSSL LDDAADNKTP LSSFFSNLLK DKPNVVKTSA
PPPDTAVQLD RILKSATGQQ SQTNTDSSA
//