KLC_CAEEL
ID KLC_CAEEL Reviewed; 540 AA.
AC P46822; Q18088; Q6BEW4; Q8I7M2; Q8TA80; Q95QV1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Kinesin light chain;
DE Short=KLC;
GN Name=klc-2 {ECO:0000312|WormBase:C18C4.10b};
GN ORFNames=C18C4.10 {ECO:0000312|WormBase:C18C4.10b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RX PubMed=8046755; DOI=10.1006/jmbi.1994.1465;
RA Fan J., Amos L.A.;
RT "Kinesin light chain isoforms in Caenorhabditis elegans.";
RL J. Mol. Biol. 240:507-512(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP INTERACTION WITH UNC-33.
RX PubMed=16236031; DOI=10.1111/j.1471-4159.2005.03490.x;
RA Tsuboi D., Hikita T., Qadota H., Amano M., Kaibuchi K.;
RT "Regulatory machinery of UNC-33 Ce-CRMP localization in neurites during
RT neuronal development in Caenorhabditis elegans.";
RL J. Neurochem. 95:1629-1641(2005).
RN [4]
RP FUNCTION, INTERACTION WITH UNC-83, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19605495; DOI=10.1242/dev.038596;
RA Meyerzon M., Fridolfsson H.N., Ly N., McNally F.J., Starr D.A.;
RT "UNC-83 is a nuclear-specific cargo adaptor for kinesin-1-mediated nuclear
RT migration.";
RL Development 136:2725-2733(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27697906; DOI=10.1242/dev.141192;
RA Bone C.R., Chang Y.T., Cain N.E., Murphy S.P., Starr D.A.;
RT "Nuclei migrate through constricted spaces using microtubule motors and
RT actin networks in C. elegans hypodermal cells.";
RL Development 143:4193-4202(2016).
CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing protein
CC that may play a role in organelle transport (Probable). The light chain
CC may function in coupling of cargo to the heavy chain or in the
CC modulation of its ATPase activity (Probable). Recruits unc-83 (within
CC the unc-83-unc-84 LINC complex) to the nuclear envelope during nuclear
CC migration to mediate the link between the nuclear envelope and the
CC microtubule cytoskeleton in hypodermal precursor cells
CC (PubMed:19605495, PubMed:27697906). {ECO:0000269|PubMed:19605495,
CC ECO:0000269|PubMed:27697906, ECO:0000305}.
CC -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two light
CC chains (Probable). Interacts with unc-83; the interaction is direct
CC (PubMed:19605495). Interacts with unc-33; the interaction regulates
CC unc-33 neurite localization (PubMed:16236031).
CC {ECO:0000269|PubMed:16236031, ECO:0000269|PubMed:19605495,
CC ECO:0000305}.
CC -!- INTERACTION:
CC P46822; P34609: unc-16; NbExp=4; IntAct=EBI-315578, EBI-315684;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:19605495}. Nucleus envelope
CC {ECO:0000269|PubMed:19605495}. Note=Recruited to the nuclear envelope
CC by unc-83 during nuclear migrations. {ECO:0000269|PubMed:19605495}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000312|WormBase:C18C4.10b};
CC IsoId=P46822-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:C18C4.10a};
CC IsoId=P46822-2; Sequence=VSP_002881, VSP_002882;
CC Name=c {ECO:0000312|WormBase:C18C4.10c};
CC IsoId=P46822-3; Sequence=VSP_002882;
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 -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in defects in
CC nuclear migration in hyp7 hypodermal precursor cells (PubMed:27697906).
CC RNAi-mediated knockdown in a dhc-1 (js319) mutant background results in
CC defective nuclei migrations in larval hypodermal P-cells
CC (PubMed:27697906). {ECO:0000269|PubMed:27697906}.
CC -!- SIMILARITY: Belongs to the kinesin light chain family. {ECO:0000305}.
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DR EMBL; Z29644; CAA82752.1; -; mRNA.
DR EMBL; Z29645; CAA82753.1; -; mRNA.
DR EMBL; BX284605; CCD65110.1; -; Genomic_DNA.
DR EMBL; BX284605; CCD65111.1; -; Genomic_DNA.
DR EMBL; BX284605; CCD65112.1; -; Genomic_DNA.
DR PIR; H89052; H89052.
DR PIR; S41864; S41864.
DR PIR; S47997; S47997.
DR RefSeq; NP_001023663.1; NM_001028492.3. [P46822-2]
DR RefSeq; NP_001023664.1; NM_001028493.3. [P46822-1]
DR RefSeq; NP_001023665.1; NM_001028494.3. [P46822-3]
DR AlphaFoldDB; P46822; -.
DR SMR; P46822; -.
DR BioGRID; 43991; 24.
DR ComplexPortal; CPX-1390; Kinesin I motor complex, klc-2 variant.
DR IntAct; P46822; 14.
DR STRING; 6239.C18C4.10b.1; -.
DR iPTMnet; P46822; -.
DR EPD; P46822; -.
DR PaxDb; P46822; -.
DR PeptideAtlas; P46822; -.
DR EnsemblMetazoa; C18C4.10a.1; C18C4.10a.1; WBGene00002215. [P46822-2]
DR EnsemblMetazoa; C18C4.10b.1; C18C4.10b.1; WBGene00002215. [P46822-1]
DR EnsemblMetazoa; C18C4.10b.2; C18C4.10b.2; WBGene00002215. [P46822-1]
DR EnsemblMetazoa; C18C4.10b.3; C18C4.10b.3; WBGene00002215. [P46822-1]
DR EnsemblMetazoa; C18C4.10c.1; C18C4.10c.1; WBGene00002215. [P46822-3]
DR GeneID; 178942; -.
DR KEGG; cel:CELE_C18C4.10; -.
DR UCSC; C18C4.10d.1; c. elegans. [P46822-1]
DR CTD; 178942; -.
DR WormBase; C18C4.10a; CE27362; WBGene00002215; klc-2. [P46822-2]
DR WormBase; C18C4.10b; CE32802; WBGene00002215; klc-2. [P46822-1]
DR WormBase; C18C4.10c; CE32803; WBGene00002215; klc-2. [P46822-3]
DR eggNOG; KOG1840; Eukaryota.
DR GeneTree; ENSGT00940000155555; -.
DR InParanoid; P46822; -.
DR OMA; EQDDTCE; -.
DR OrthoDB; 511880at2759; -.
DR PhylomeDB; P46822; -.
DR Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-CEL-983189; Kinesins.
DR PRO; PR:P46822; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00002215; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0016938; C:kinesin I complex; IPI:WormBase.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0019894; F:kinesin binding; IPI:WormBase.
DR GO; GO:0048675; P:axon extension; IMP:WormBase.
DR GO; GO:0051295; P:establishment of meiotic spindle localization; IMP:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0030473; P:nuclear migration along microtubule; IMP:UniProtKB.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IMP:ComplexPortal.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:WormBase.
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; 1.
DR PROSITE; PS01160; KINESIN_LIGHT; 4.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleus; Reference proteome; Repeat; TPR repeat; Transport.
FT CHAIN 1..540
FT /note="Kinesin light chain"
FT /id="PRO_0000215101"
FT REPEAT 206..239
FT /note="TPR 1"
FT REPEAT 248..281
FT /note="TPR 2"
FT REPEAT 290..323
FT /note="TPR 3"
FT REPEAT 332..365
FT /note="TPR 4"
FT REPEAT 374..407
FT /note="TPR 5"
FT REPEAT 456..489
FT /note="TPR 6"
FT COILED 34..138
FT VAR_SEQ 1
FT /note="M -> MNLAGSTIQAYRQRKIESLAKM (in isoform a)"
FT /evidence="ECO:0000303|PubMed:8046755"
FT /id="VSP_002881"
FT VAR_SEQ 489..540
FT /note="HEPLRSGAMGGIDEMSQSMMASTIGGSRNSMTTSTSQTGLKNKLMNALGFNS
FT -> MSESRRMERSVMY (in isoform a and isoform c)"
FT /evidence="ECO:0000303|PubMed:8046755"
FT /id="VSP_002882"
FT CONFLICT 141
FT /note="F -> L (in Ref. 1; CAA82752/CAA82753)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="K -> N (in Ref. 1; CAA82753)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 60225 MW; BDA3B2CD06D38D06 CRC64;
MSNMSQDDVT TGLRTVQQGL EALREEHSTI SNTLETSVKG VKEDEAPLPK QKLSQINDNL
DKLVCGVDET SLMLMVFQLT QGMDAQHQKY QAQRRRLCQE NAWLRDELSS TQIKLQQSEQ
MVAQLEEENK HLKYMASIKQ FDDGTQSDTK TSVDVGPQPV TNETLQELGF GPEDEEDMNA
SQFNQPTPAN QMAASANVGY EIPARLRTLH NLVIQYASQG RYEVAVPLCK QALEDLEKTS
GHDHPDVATM LNILALVYRD QNKYKEAANL LNEALSIREK CLGESHPAVA ATLNNLAVLF
GKRGKFKDAE PLCKRALEIR EKVLGDDHPD VAKQLNNLAL LCQNQGKYEE VEKYYKRALE
IYESKLGPDD PNVAKTKNNL SSAYLKQGKY KEAEELYKQI LTRAHEREFG QISGENKPIW
QIAEEREENK HKGEGATANE QAGWAKAAKV DSPTVTTTLK NLGALYRRQG KYEAAETLED
VALRAKKQHE PLRSGAMGGI DEMSQSMMAS TIGGSRNSMT TSTSQTGLKN KLMNALGFNS
