GenomeNet

Database: UniProt
Entry: W3A5P1_PHYPR
LinkDB: W3A5P1_PHYPR
Original site: W3A5P1_PHYPR 
ID   W3A5P1_PHYPR            Unreviewed;       435 AA.
AC   W3A5P1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Dynein light intermediate chain {ECO:0000256|RuleBase:RU366047};
GN   ORFNames=F442_01309 {ECO:0000313|EMBL:ETP53824.1};
OS   Phytophthora parasitica P10297.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP53824.1, ECO:0000313|Proteomes:UP000018948};
RN   [1] {ECO:0000313|EMBL:ETP53824.1, ECO:0000313|Proteomes:UP000018948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P10297 {ECO:0000313|EMBL:ETP53824.1,
RC   ECO:0000313|Proteomes:UP000018948};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P10297.";
RL   Submitted (NOV-2013) 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       {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:ETP53824.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ANIY01000236; ETP53824.1; -; Genomic_DNA.
DR   AlphaFoldDB; W3A5P1; -.
DR   EnsemblProtists; ETP53824; ETP53824; F442_01309.
DR   Proteomes; UP000018948; 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   Reference proteome {ECO:0000313|Proteomes:UP000018948};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366047}.
FT   REGION          375..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..391
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..435
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   435 AA;  48320 MW;  8FF7182EE7BC1155 CRC64;
     MATGEDLWQQ MLRDCSVRSK LPVANFLLVG DAESGKSALL ARLDEAKSTP SETADETHAV
     DTLLAFKTLD VLDPRAKESG GDASEDVMAH IGTWSLNDLN LKDLIKIAVK PQTLQKTVVA
     IVLDLSRPWT IKSSLEQWLS ALEGQLLEQI NQLAPETRNE LYGAIKQHIL AYEDPSVDHS
     APTPMDTSTN EFMEEGVLSK NLGVPLVIVV AKADLRPENS VKMDYIEYTL RQFAIRYGAS
     VVFTSAKTGS NVDTLRKYIL HRAYPSQFKF TEPPQLVDHN SIFIPSGYDS FELVNQSLVG
     SQARWPTDKP FEKIVPAPTE ETDDAAATLA TDIRVDTHEQ WLEKLEKAAG AGLEELQKQS
     IEASKKAEQA AVARRAAADR RKREEKDVSS KHLQNFFNNL LSRPEKTRSS RSMSDKKKEK
     SDKALGDQEA KRSAV
//
DBGET integrated database retrieval system