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DYL1_SCHPO
ID   DYL1_SCHPO              Reviewed;          85 AA.
AC   Q9UR05;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Dynein light chain 1, cytoplasmic;
GN   Name=dlc2; ORFNames=SPAC926.07c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11907273; DOI=10.1091/mbc.01-11-0543;
RA   Miki F., Okazaki K., Shimanuki M., Yamamoto A., Hiraoka Y., Niwa O.;
RT   "The 14-kDa dynein light chain-family protein Dlc1 is required for regular
RT   oscillatory nuclear movement and efficient recombination during meiotic
RT   prophase in fission yeast.";
RL   Mol. Biol. Cell 13:930-946(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Acts as one of several non-catalytic accessory components of
CC       the cytoplasmic dynein 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 changing or maintaining the spatial distribution of
CC       cytoskeletal structures (By similarity). Also a component of the
CC       nuclear pore complex (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q02647}.
CC   -!- SUBUNIT: Homodimer. Cytoplasmic dynein consists of two catalytic heavy
CC       chains (HCs) and a number of non-catalytic subunits which present
CC       intermediate chains (ICs), light intermediate chains (LICs) and light
CC       chains (LCs). Component of the nuclear pore complex (NPC). NPC
CC       constitutes the exclusive means of nucleocytoplasmic transport. NPCs
CC       allow the passive diffusion of ions and small molecules and the active,
CC       nuclear transport receptor-mediated bidirectional transport of
CC       macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and
CC       ribosomal subunits across the nuclear envelope. Due to its 8-fold
CC       rotational symmetry, all subunits are present with 8 copies or
CC       multiples thereof. {ECO:0000250|UniProtKB:Q02647}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q02647}. Nucleus, nuclear pore complex
CC       {ECO:0000250|UniProtKB:Q02647}.
CC   -!- SIMILARITY: Belongs to the dynein light chain family. {ECO:0000305}.
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DR   EMBL; AF197476; AAF05842.1; -; mRNA.
DR   EMBL; CU329670; CAB54155.1; -; Genomic_DNA.
DR   PIR; T39205; T39205.
DR   RefSeq; NP_594368.1; NM_001019789.2.
DR   AlphaFoldDB; Q9UR05; -.
DR   SMR; Q9UR05; -.
DR   BioGRID; 279948; 14.
DR   STRING; 4896.SPAC926.07c.1; -.
DR   MaxQB; Q9UR05; -.
DR   PaxDb; Q9UR05; -.
DR   EnsemblFungi; SPAC926.07c.1; SPAC926.07c.1:pep; SPAC926.07c.
DR   GeneID; 2543530; -.
DR   KEGG; spo:SPAC926.07c; -.
DR   PomBase; SPAC926.07c; dlc2.
DR   VEuPathDB; FungiDB:SPAC926.07c; -.
DR   eggNOG; KOG3430; Eukaryota.
DR   HOGENOM; CLU_070944_4_0_1; -.
DR   InParanoid; Q9UR05; -.
DR   OMA; RHGATWH; -.
DR   PhylomeDB; Q9UR05; -.
DR   BRENDA; 5.6.1.2; 5613.
DR   Reactome; R-SPO-1632852; Macroautophagy.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   Reactome; R-SPO-9646399; Aggrephagy.
DR   PRO; PR:Q9UR05; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005868; C:cytoplasmic dynein complex; ISO:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0035974; C:meiotic spindle pole body; IDA:PomBase.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR   GO; GO:0030437; P:ascospore formation; IC:PomBase.
DR   GO; GO:0030989; P:dynein-driven meiotic oscillatory nuclear movement; IC:PomBase.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0000743; P:nuclear migration involved in conjugation with cellular fusion; IC:PomBase.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.740.10; -; 1.
DR   InterPro; IPR037177; DLC_sf.
DR   InterPro; IPR019763; Dynein_light_1/2_CS.
DR   InterPro; IPR001372; Dynein_light_chain_typ-1/2.
DR   PANTHER; PTHR11886; PTHR11886; 1.
DR   Pfam; PF01221; Dynein_light; 1.
DR   SMART; SM01375; Dynein_light; 1.
DR   SUPFAM; SSF54648; SSF54648; 1.
DR   PROSITE; PS01239; DYNEIN_LIGHT_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; Dynein; Microtubule; Motor protein;
KW   mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW   Reference proteome; Translocation; Transport.
FT   CHAIN           1..85
FT                   /note="Dynein light chain 1, cytoplasmic"
FT                   /id="PRO_0000195148"
SQ   SEQUENCE   85 AA;  9822 MW;  81B5EC20D81D628A CRC64;
     MAVIKAVDMS EKMQQEAIHA AVQAMEKFTI EKDIAAFIKR EFDKKFSPTW HCIVGRNFGS
     FVTHESRHFI YFYLGTVAFL LFKSG
 
 
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