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Database: UniProt
Entry: K7GIP8_PELSI
LinkDB: K7GIP8_PELSI
Original site: K7GIP8_PELSI 
ID   K7GIP8_PELSI            Unreviewed;       470 AA.
AC   K7GIP8;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Dynein light intermediate chain {ECO:0000256|RuleBase:RU366047};
GN   Name=DYNC1LI2 {ECO:0000313|Ensembl:ENSPSIP00000020159.1};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000020159.1, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000020159.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00037133, 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|ARBA:ARBA00004245, 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; AGCU01136395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01136396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01136397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01136398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01136399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01136400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01136401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01136402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_014432699.1; XM_014577213.1.
DR   AlphaFoldDB; K7GIP8; -.
DR   STRING; 13735.ENSPSIP00000020159; -.
DR   Ensembl; ENSPSIT00000020254.1; ENSPSIP00000020159.1; ENSPSIG00000017826.1.
DR   GeneID; 102459174; -.
DR   CTD; 1783; -.
DR   eggNOG; KOG3905; Eukaryota.
DR   GeneTree; ENSGT00390000008295; -.
DR   HOGENOM; CLU_021937_2_1_1; -.
DR   OMA; FKHNVID; -.
DR   OrthoDB; 179830at2759; -.
DR   TreeFam; TF352602; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
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:0051642; P:centrosome localization; IEA:Ensembl.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
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:SF1; CYTOPLASMIC DYNEIN 1 LIGHT INTERMEDIATE CHAIN 2; 1.
DR   PANTHER; PTHR12688; 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   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   Methylation {ECO:0000256|ARBA:ARBA00022481};
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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366047}.
FT   REGION          165..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..399
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   470 AA;  52473 MW;  008C5F50B6C9362A CRC64;
     MLILPKNTTS YRLRSSILSE VSTRSRSKLP SGKNILVFGD DGSGKTTLMA KVQGAEYSKK
     GRGLEYLYLN IHDEDRDDHT RCNVWILDGD LYHKGLLKFA VSAENVQETL VVFVADMSRP
     WTVMESLQKW ASVLREHIDK LKIPPEEMRD MEQKFIKEFQ EYVEPEEGYQ GSPQRRGPSS
     GQEDENVTLP LGENVLTHNL GIPVLVVCTK CDAVSVLEKE HDYREEHFDF IQSHIRRFCL
     QYGAALIYTS VKEEKNLDLL YKYIVHKTYG FHFTTPALVV EKDAVFIPAG WDNEKKIAIL
     HENFTTVKPE DAYEDFIVKP PVRKLVHEKE LAAEDEQVFL MKQQSLLAKQ PATPTRASES
     PARGPAGSPR TQGRAGPVNV PSASPITSVK KPDPNIKNNA ASEGVLASFF NSLLSKKTGP
     PGSPGAGGVQ STAKKSGQKT VLTNVQEELD RMTRKPDSMV TANSPTENEA
//
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