KLC_DROME
ID KLC_DROME Reviewed; 508 AA.
AC P46824; Q9VU05;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Kinesin light chain;
DE Short=KLC;
GN Name=Klc; ORFNames=CG5433;
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=Head;
RX PubMed=8514798; DOI=10.1016/s0021-9258(19)38698-3;
RA Gauger A.K., Goldstein L.S.B.;
RT "The Drosophila kinesin light chain. Primary structure and interaction with
RT kinesin heavy chain.";
RL J. Biol. Chem. 268:13657-13666(1993).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-168; THR-477; SER-480 AND
RP SER-485, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing protein
CC that may play a role in organelle transport. The light chain may
CC function in coupling of cargo to the heavy chain or in the modulation
CC of its ATPase activity.
CC -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two light
CC chains.
CC -!- INTERACTION:
CC P46824; P17210: Khc; NbExp=4; IntAct=EBI-77490, EBI-102445;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The light chain is composed of three structural domains: a
CC large globular N-terminal domain which may be involved in binding to
CC kinesin heavy chains, a central alpha-helical coiled-coil domain that
CC mediates the light chain dimerization; and a small globular C-terminal
CC which may play a role in regulating mechanochemical activity or
CC attachment of kinesin to membrane-bound organelles.
CC -!- SIMILARITY: Belongs to the kinesin light chain family. {ECO:0000305}.
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DR EMBL; L11013; AAA02481.1; -; mRNA.
DR EMBL; L11328; AAA28669.1; -; mRNA.
DR EMBL; AE014296; AAF49890.2; -; Genomic_DNA.
DR EMBL; AY061164; AAL28712.1; -; mRNA.
DR RefSeq; NP_001261780.1; NM_001274851.1.
DR RefSeq; NP_524049.1; NM_079325.3.
DR AlphaFoldDB; P46824; -.
DR SMR; P46824; -.
DR BioGRID; 64793; 68.
DR DIP; DIP-19091N; -.
DR IntAct; P46824; 34.
DR STRING; 7227.FBpp0075683; -.
DR iPTMnet; P46824; -.
DR PaxDb; P46824; -.
DR PRIDE; P46824; -.
DR EnsemblMetazoa; FBtr0075951; FBpp0075683; FBgn0010235.
DR EnsemblMetazoa; FBtr0331555; FBpp0303945; FBgn0010235.
DR GeneID; 39445; -.
DR KEGG; dme:Dmel_CG5433; -.
DR CTD; 39445; -.
DR FlyBase; FBgn0010235; Klc.
DR VEuPathDB; VectorBase:FBgn0010235; -.
DR eggNOG; KOG1840; Eukaryota.
DR GeneTree; ENSGT00940000155555; -.
DR InParanoid; P46824; -.
DR PhylomeDB; P46824; -.
DR Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-983189; Kinesins.
DR BioGRID-ORCS; 39445; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39445; -.
DR PRO; PR:P46824; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0010235; Expressed in embryonic/larval hemocyte (Drosophila) and 47 other tissues.
DR ExpressionAtlas; P46824; baseline and differential.
DR Genevisible; P46824; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0019894; F:kinesin binding; IBA:GO_Central.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0007018; P:microtubule-based movement; IDA:FlyBase.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR002151; Kinesin_light.
DR InterPro; IPR015792; Kinesin_light_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS01160; KINESIN_LIGHT; 4.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Motor protein;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..508
FT /note="Kinesin light chain"
FT /id="PRO_0000215102"
FT REPEAT 186..219
FT /note="TPR 1"
FT REPEAT 228..261
FT /note="TPR 2"
FT REPEAT 270..303
FT /note="TPR 3"
FT REPEAT 312..345
FT /note="TPR 4"
FT REPEAT 354..387
FT /note="TPR 5"
FT REPEAT 437..470
FT /note="TPR 6"
FT REGION 156..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 34..129
FT COMPBIAS 488..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 168
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 477
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 508 AA; 58044 MW; B7893FF47EE638A9 CRC64;
MTQMSQDEII TNTKTVLQGL EALRVEHVSI MNGIAEVQKD NEKSDMLRKN IENIELGLSE
AQVMMALTSH LQNIEAEKHK LKTQVRRLHQ ENAWLRDELA NTQQKFQASE QLVAQLEEEK
KHLEFMASVK KYDENQEQDD ACDKSRTDPV VELFPDEENE DRHNMSPTPP SQFANQTSGY
EIPARLRTLH NLVIQYASQG RYEVAVPLCK QALEDLERTS GHDHPDVATM LNILALVYRD
QNKYKEAANL LNDALSIRGK TLGENHPAVA ATLNNLAVLY GKRGKYKDAE PLCKRALEIR
EKVLGKDHPD VAKQLNNLAL LCQNQGKYDE VEKYYQRALD IYESKLGPDD PNVAKTKNNL
AGCYLKQGRY TEAEILYKQV LTRAHEREFG AIDSKNKPIW QVAEEREEHK FDNRENTPYG
EYGGWHKAAK VDSPTVTTTL KNLGALYRRQ GMFEAAETLE DCAMRSKKEA YDLAKQTKLS
QLLTSNEKRR SKAIKEDLDF SEEKNAKP
