KLC_STRPU
ID KLC_STRPU Reviewed; 686 AA.
AC Q05090; Q04801; Q05088; Q05089;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Kinesin light chain;
DE Short=KLC;
OS Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS KLC-1; KLC-2; KLC-3 AND KLC-4).
RC TISSUE=Egg;
RX PubMed=8496962; DOI=10.1006/jmbi.1993.1267;
RA Wedaman K.P., Knight A.E., Kendrick-Jones J., Scholey J.M.;
RT "Sequences of sea urchin kinesin light chain isoforms.";
RL J. Mol. Biol. 231:155-158(1993).
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=KLC-3;
CC IsoId=Q05090-1; Sequence=Displayed;
CC Name=KLC-1;
CC IsoId=Q05090-2; Sequence=VSP_002878;
CC Name=KLC-2;
CC IsoId=Q05090-3; Sequence=VSP_002877;
CC Name=KLC-4;
CC IsoId=Q05090-4; Sequence=VSP_002879, VSP_002880;
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 -!- PTM: Phosphorylation may modulate the process of mechanochemical
CC coupling.
CC -!- SIMILARITY: Belongs to the kinesin light chain family. {ECO:0000305}.
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DR EMBL; L10235; AAA03059.1; -; mRNA.
DR EMBL; L10234; AAA03058.1; -; mRNA.
DR EMBL; L10233; AAA03057.1; -; mRNA.
DR EMBL; L08258; AAA03060.1; -; mRNA.
DR PIR; S33813; S33813.
DR PIR; S33814; S33814.
DR PIR; S33815; S33815.
DR PIR; S33816; S33816.
DR RefSeq; NP_999735.1; NM_214570.2. [Q05090-4]
DR RefSeq; NP_999736.1; NM_214571.1. [Q05090-1]
DR RefSeq; NP_999737.1; NM_214572.1. [Q05090-3]
DR RefSeq; NP_999738.1; NM_214573.1. [Q05090-2]
DR RefSeq; XP_011674949.1; XM_011676647.1.
DR RefSeq; XP_011674951.1; XM_011676649.1.
DR RefSeq; XP_011674955.1; XM_011676653.1.
DR AlphaFoldDB; Q05090; -.
DR SMR; Q05090; -.
DR STRING; 7668.SPU_018898-tr; -.
DR EnsemblMetazoa; NM_214570; NP_999735; LOC373373. [Q05090-4]
DR EnsemblMetazoa; NM_214571; NP_999736; LOC373373. [Q05090-1]
DR EnsemblMetazoa; NM_214572; NP_999737; LOC373373. [Q05090-3]
DR EnsemblMetazoa; NM_214573; NP_999738; LOC373373. [Q05090-2]
DR EnsemblMetazoa; XM_030998277; XP_030854137; LOC373373. [Q05090-1]
DR EnsemblMetazoa; XM_030998279; XP_030854139; LOC373373. [Q05090-3]
DR EnsemblMetazoa; XM_030998284; XP_030854144; LOC373373. [Q05090-2]
DR EnsemblMetazoa; XM_030999429; XP_030855289; LOC105446921. [Q05090-1]
DR EnsemblMetazoa; XM_030999431; XP_030855291; LOC105446921. [Q05090-3]
DR EnsemblMetazoa; XM_030999436; XP_030855296; LOC105446921. [Q05090-2]
DR GeneID; 373373; -.
DR KEGG; spu:373373; -.
DR eggNOG; KOG1840; Eukaryota.
DR HOGENOM; CLU_019953_0_0_1; -.
DR InParanoid; Q05090; -.
DR OrthoDB; 511880at2759; -.
DR PhylomeDB; Q05090; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
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:0007018; P:microtubule-based movement; IBA:GO_Central.
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; 5.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..686
FT /note="Kinesin light chain"
FT /id="PRO_0000215100"
FT REPEAT 215..248
FT /note="TPR 1"
FT REPEAT 257..290
FT /note="TPR 2"
FT REPEAT 299..332
FT /note="TPR 3"
FT REPEAT 341..374
FT /note="TPR 4"
FT REPEAT 383..416
FT /note="TPR 5"
FT REPEAT 472..505
FT /note="TPR 6"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 20..160
FT COMPBIAS 627..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 441..451
FT /note="GKFKDNAPYGD -> VKKRKPKPAKS (in isoform KLC-4)"
FT /evidence="ECO:0000303|PubMed:8496962"
FT /id="VSP_002879"
FT VAR_SEQ 452..686
FT /note="Missing (in isoform KLC-4)"
FT /evidence="ECO:0000303|PubMed:8496962"
FT /id="VSP_002880"
FT VAR_SEQ 564..600
FT /note="Missing (in isoform KLC-1)"
FT /evidence="ECO:0000303|PubMed:8496962"
FT /id="VSP_002878"
FT VAR_SEQ 564..572
FT /note="Missing (in isoform KLC-2)"
FT /evidence="ECO:0000303|PubMed:8496962"
FT /id="VSP_002877"
SQ SEQUENCE 686 AA; 76517 MW; 603D71186CC0364B CRC64;
MSGSKLSTPN NSGGGQGNLS QEQIITGTRE VIKGLEQLKN EHNDILNSLY QSLKMLKKDT
PGDSNLVEEK TDIIEKSLES LELGLGEAKV MMALGHHLNM VEAEKQKLRA QVRRLVQENT
WLRDELAATQ QKLQTSEQNL ADLEVKYKHL EYMNSIKKYD EDRTPDEEAS SSDPLDLGFP
EDDDGGQADE SYPQPQTGSG SVSAAAGGYE IPARLRTLHN LVIQYASQSR YEVAVPLCKQ
ALEDLEKTSG HDHPDVATML NILALVYRDQ NKYKEAGNLL HDALAIREKT LGPDHPAVAA
TLNNLAVLYG KRGKYKEAEP LCKRALEIRE KVLGKDHPDV AKQLNNLALL CQNQGKYEEV
EWYYQRALEI YEKKLGPDDP NVAKTKNNLA AAYLKQGKYK AAETLYKQVL TRAHEREFGL
SADDKDNKPI WMQAEEREEK GKFKDNAPYG DYGGWHKAAK VDSRSRSSPT VTTTLKNLGA
LYRRQGKYDA AEILEECAMK SRRNALDMVR ETKVRELLGQ DLSTDVPRSE AMAKERHHRR
SSGTPRHGST ESVSYEKTDG SEEVSIGVAW KAKRKAKDRS RSIPAGYVEI PRSPPHVLVE
NGDGKLRRSG SLSKLRASVR RSSTKLLNKL KGRESDDDGG MKRASSMSVL PSRGNDESTP
APIQLSQRGR VGSHDNLSSR RQSGNF
