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DYLT_DROME
ID   DYLT_DROME              Reviewed;         111 AA.
AC   Q94524; Q9VE95;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Dynein light chain Tctex-type;
DE   AltName: Full=TCTEX-1 protein homolog;
GN   Name=Dlc90F; Synonyms=Tctex; ORFNames=CG12363;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=10071211; DOI=10.1007/s004380050942;
RA   Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., Caizzi R.,
RA   Barsanti P.;
RT   "Identification of nuclear genes encoding mitochondrial proteins: isolation
RT   of a collection of D. melanogaster cDNAs homologous to sequences in the
RT   Human Gene Index database.";
RL   Mol. Gen. Genet. 261:64-70(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11405626; DOI=10.1007/s004380000431;
RA   Caggese C., Moschetti R., Ragone G., Barsanti P., Caizzi R.;
RT   "dtctex-1, the Drosophila melanogaster homolog of a putative murine t-
RT   complex distorter encoding a dynein light chain, is required for production
RT   of functional sperm.";
RL   Mol. Genet. Genomics 265:436-444(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   SUBUNIT, FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15090621; DOI=10.1091/mbc.e04-01-0013;
RA   Li M.G., Serr M., Newman E.A., Hays T.S.;
RT   "The Drosophila tctex-1 light chain is dispensable for essential
RT   cytoplasmic dynein functions but is required during spermatid
RT   differentiation.";
RL   Mol. Biol. Cell 15:3005-3014(2004).
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 acts as a motor for the intracellular
CC       retrograde motility of vesicles and organelles along microtubules.
CC       Required for spermatid differentiation. Is not required for polarized
CC       transport in rhabdomere development and appears to be a non-essential
CC       component of the cytoplasmic dynein complex.
CC       {ECO:0000269|PubMed:15090621}.
CC   -!- SUBUNIT: The cytoplasmic dynein complex consists of two catalytic heavy
CC       chains (HCs) and a number of non-catalytic subunits presented by
CC       intermediate chains (ICs), light intermediate chains (LICs) and light
CC       chains (LCs). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q94524; Q94524: Dlc90F; NbExp=3; IntAct=EBI-158251, EBI-158251;
CC       Q94524; Q9VH45: Dmel\CG5359; NbExp=4; IntAct=EBI-158251, EBI-155608;
CC       Q94524; P22979: Hsp67Bc; NbExp=6; IntAct=EBI-158251, EBI-165408;
CC       Q94524; Q9VIT3: msb1l; NbExp=3; IntAct=EBI-158251, EBI-121559;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Male sterility. {ECO:0000269|PubMed:15090621}.
CC   -!- SIMILARITY: Belongs to the dynein light chain Tctex-type family.
CC       {ECO:0000305}.
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DR   EMBL; Y08968; CAA70165.1; -; mRNA.
DR   EMBL; AF123058; AAD30033.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF55532.1; -; Genomic_DNA.
DR   EMBL; AY069608; AAL39753.1; -; mRNA.
DR   RefSeq; NP_477356.1; NM_058008.4.
DR   PDB; 1YGT; X-ray; 1.70 A; A=1-111.
DR   PDB; 2PG1; X-ray; 2.80 A; E/F/G/H=1-111.
DR   PDB; 3FM7; X-ray; 3.50 A; A/B=1-111.
DR   PDBsum; 1YGT; -.
DR   PDBsum; 2PG1; -.
DR   PDBsum; 3FM7; -.
DR   AlphaFoldDB; Q94524; -.
DR   SMR; Q94524; -.
DR   BioGRID; 67217; 48.
DR   DIP; DIP-17339N; -.
DR   IntAct; Q94524; 24.
DR   MINT; Q94524; -.
DR   STRING; 7227.FBpp0082996; -.
DR   PaxDb; Q94524; -.
DR   PRIDE; Q94524; -.
DR   DNASU; 42199; -.
DR   EnsemblMetazoa; FBtr0083575; FBpp0082996; FBgn0024432.
DR   GeneID; 42199; -.
DR   KEGG; dme:Dmel_CG12363; -.
DR   CTD; 42199; -.
DR   FlyBase; FBgn0024432; Dlc90F.
DR   VEuPathDB; VectorBase:FBgn0024432; -.
DR   eggNOG; KOG4081; Eukaryota.
DR   GeneTree; ENSGT00940000154531; -.
DR   HOGENOM; CLU_097204_7_2_1; -.
DR   InParanoid; Q94524; -.
DR   OMA; TSDACYV; -.
DR   OrthoDB; 1474572at2759; -.
DR   PhylomeDB; Q94524; -.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   SignaLink; Q94524; -.
DR   BioGRID-ORCS; 42199; 1 hit in 3 CRISPR screens.
DR   EvolutionaryTrace; Q94524; -.
DR   GenomeRNAi; 42199; -.
DR   PRO; PR:Q94524; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0024432; Expressed in eye disc (Drosophila) and 35 other tissues.
DR   ExpressionAtlas; Q94524; baseline and differential.
DR   Genevisible; Q94524; DM.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005868; C:cytoplasmic dynein complex; ISS:FlyBase.
DR   GO; GO:0030286; C:dynein complex; IDA:FlyBase.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR   GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR   GO; GO:0045505; F:dynein intermediate chain binding; IPI:FlyBase.
DR   GO; GO:0051959; F:dynein light intermediate chain binding; IDA:FlyBase.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR   GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase.
DR   GO; GO:0008090; P:retrograde axonal transport; IMP:FlyBase.
DR   GO; GO:0007286; P:spermatid development; IMP:FlyBase.
DR   Gene3D; 3.30.1140.40; -; 1.
DR   IDEAL; IID50099; -.
DR   InterPro; IPR005334; Tctex-1-like.
DR   InterPro; IPR038586; Tctex-1-like_sf.
DR   PANTHER; PTHR21255; PTHR21255; 1.
DR   Pfam; PF03645; Tctex-1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Cytoskeleton; Dynein; Microtubule; Motor protein;
KW   Reference proteome.
FT   CHAIN           1..111
FT                   /note="Dynein light chain Tctex-type"
FT                   /id="PRO_0000195155"
FT   HELIX           14..27
FT                   /evidence="ECO:0007829|PDB:1YGT"
FT   HELIX           34..53
FT                   /evidence="ECO:0007829|PDB:1YGT"
FT   TURN            54..56
FT                   /evidence="ECO:0007829|PDB:3FM7"
FT   STRAND          58..69
FT                   /evidence="ECO:0007829|PDB:1YGT"
FT   STRAND          75..83
FT                   /evidence="ECO:0007829|PDB:2PG1"
FT   TURN            85..87
FT                   /evidence="ECO:0007829|PDB:1YGT"
FT   STRAND          89..96
FT                   /evidence="ECO:0007829|PDB:1YGT"
FT   STRAND          98..110
FT                   /evidence="ECO:0007829|PDB:1YGT"
SQ   SEQUENCE   111 AA;  12479 MW;  544CC39F5B318137 CRC64;
     MDDSREESQF IVDDVSKTIK EAIETTIGGN AYQHDKVNNW TGQVVENCLT VLTKEQKPYK
     YIVTAMIMQK NGAGLHTASS CYWNNDTDGS CTVRWENKTM YCIVSVFGLA V
 
 
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