ID Q21592_CAEEL Unreviewed; 516 AA. AC Q21592; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 2. DT 27-MAR-2024, entry version 178. DE RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020}; GN Name=klc-1 {ECO:0000313|EMBL:CAA92746.2, ECO:0000313|WormBase:M7.2a}; GN ORFNames=CELE_M7.2 {ECO:0000313|EMBL:CAA92746.2}, M7.2 GN {ECO:0000313|WormBase:M7.2a}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAA92746.2, ECO:0000313|Proteomes:UP000001940}; RN [1] {ECO:0000313|EMBL:CAA92746.2, ECO:0000313|Proteomes:UP000001940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA92746.2, RC ECO:0000313|Proteomes:UP000001940}; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RA Sulson J.E., Waterston R.; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing protein CC that play a role in organelle transport. CC {ECO:0000256|RuleBase:RU367020}. CC -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two light CC chains. {ECO:0000256|RuleBase:RU367020}. CC -!- INTERACTION: CC Q21592; Q9TZK8: meg-4; NbExp=3; IntAct=EBI-316831, EBI-314126; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU367020}. CC -!- SIMILARITY: Belongs to the kinesin light chain family. CC {ECO:0000256|ARBA:ARBA00009622, ECO:0000256|RuleBase:RU367020}. 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; BX284604; CAA92746.2; -; Genomic_DNA. DR PIR; C88827; C88827. DR PIR; T23827; T23827. DR RefSeq; NP_001255535.1; NM_001268606.1. DR AlphaFoldDB; Q21592; -. DR SMR; Q21592; -. DR DIP; DIP-26939N; -. DR IntAct; Q21592; 3. DR EPD; Q21592; -. DR PeptideAtlas; Q21592; -. DR EnsemblMetazoa; M7.2a.1; M7.2a.1; WBGene00002214. DR GeneID; 178007; -. DR AGR; WB:WBGene00002214; -. DR WormBase; M7.2a; CE23882; WBGene00002214; klc-1. DR GeneTree; ENSGT00940000155555; -. DR HOGENOM; CLU_019953_0_0_1; -. DR OrthoDB; 5392083at2759; -. DR PhylomeDB; Q21592; -. DR Proteomes; UP000001940; Chromosome IV. DR Bgee; WBGene00002214; Expressed in germ line (C elegans) and 4 other cell types or tissues. DR ExpressionAtlas; Q21592; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005871; C:kinesin complex; IEA:UniProtKB-UniRule. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-UniRule. DR GO; GO:0019894; F:kinesin binding; IBA:GO_Central. DR GO; GO:0051295; P:establishment of meiotic spindle localization; IMP:WormBase. DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central. DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:WormBase. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1. DR InterPro; IPR002151; Kinesin_light. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR45783; KINESIN LIGHT CHAIN; 1. DR PANTHER; PTHR45783:SF3; KINESIN LIGHT CHAIN; 1. DR Pfam; PF13424; TPR_12; 2. DR Pfam; PF13176; TPR_7; 1. DR PRINTS; PR00381; KINESINLIGHT. DR SMART; SM00028; TPR; 4. DR SUPFAM; SSF48452; TPR-like; 2. DR PROSITE; PS50005; TPR; 1. PE 1: Evidence at protein level; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|RuleBase:RU367020}; KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212, KW ECO:0000256|RuleBase:RU367020}; KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU367020}; KW Motor protein {ECO:0000256|ARBA:ARBA00023175, KW ECO:0000256|RuleBase:RU367020}; KW Proteomics identification {ECO:0007829|EPD:Q21592, KW ECO:0007829|PeptideAtlas:Q21592}; KW Reference proteome {ECO:0000313|Proteomes:UP000001940}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE- KW ProRule:PRU00339}. FT REPEAT 327..360 FT /note="TPR" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339" FT REGION 474..494 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 108..135 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 477..494 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 516 AA; 58070 MW; 2636215BD9CA344D CRC64; MVISLGDDIT TVLKTVQQTL FALRDEHEAA TRILEANLIN SDSSEPSLPS EKMGLIDESL GKVMDGGDEA SLLIMMDKLM QSYDVQLSKN HESIRLLRQE NTWLLDELTT TQRKLQESER TVAHLEEERD HYKFQDSMNY LNSDFQHTTS VDATPMMVDT LQELGFGPEE EDQNNNQADQ GCRSSSFSNP ISNDYQLPTR LQTLQNLVIQ YMEQGRFEVA IPLCKQALED VVKVHGNVHL DVATMLNVLA IVYRNQENFK DAAIYLEKAL SIRVQCCGEN HHSVAATLNN LAIAYGKRGK YKESEPLCKR ALEIRKNLLG PNHPDVAKQL TNLGIVTQQL EKYEETENYF KQALSIYNRA FPENHQNVIK TKNQLASVFL KQGKYQEAEE MYKNILSKVA ITGNKPIWRI AEDREERQRN GIPKVDDESF NVNPTTVMDS NVMSTIKNLA AVYRKQGKEE AAGTLEEALG AKKQINGGAD HTNSTASSVE TSSAVAINPA QSGIKKRIMH FVGLNF //