KLC1_MOUSE
ID KLC1_MOUSE Reviewed; 541 AA.
AC O88447;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Kinesin light chain 1;
DE Short=KLC 1;
GN Name=Klc1; Synonyms=Kns2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9624122; DOI=10.1074/jbc.273.25.15395;
RA Rahman A., Friedman D.S., Goldstein L.S.;
RT "Two kinesin light chain genes in mice. Identification and characterization
RT of the encoded proteins.";
RL J. Biol. Chem. 273:15395-15403(1998).
RN [2]
RP INTERACTION WITH SPAG9.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=15767678; DOI=10.1128/mcb.25.7.2733-2743.2005;
RA Kelkar N., Standen C.L., Davis R.J.;
RT "Role of the JIP4 scaffold protein in the regulation of mitogen-activated
RT protein kinase signaling pathways.";
RL Mol. Cell. Biol. 25:2733-2743(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-448, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [4]
RP INTERACTION WITH ATCAY.
RX PubMed=19861499; DOI=10.1242/jcs.048579;
RA Aoyama T., Hata S., Nakao T., Tanigawa Y., Oka C., Kawaichi M.;
RT "Cayman ataxia protein caytaxin is transported by kinesin along neurites
RT through binding to kinesin light chains.";
RL J. Cell Sci. 122:4177-4185(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459; SER-520 AND SER-523, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Interacts with SPAG9 (PubMed:15767678). Interacts with ATCAY;
CC may link mitochondria to KLC1 and regulate mitochondria localization
CC into neuron projections (PubMed:19861499). Interacts (via TPR repeats)
CC with TOR1A; the interaction associates TOR1A with the kinesin
CC oligomeric complex. Interacts with BORCS5 (By similarity). Interacts
CC with MAPK8IP3/JIP3 and NTRK2/TRKB; interaction with NTRK2/TRKB is
CC mediated by MAPK8IP3/JIP3 (By similarity).
CC {ECO:0000250|UniProtKB:P37285, ECO:0000250|UniProtKB:Q07866,
CC ECO:0000269|PubMed:15767678, ECO:0000269|PubMed:19861499}.
CC -!- INTERACTION:
CC O88447; P63017: Hspa8; NbExp=3; IntAct=EBI-301550, EBI-433443;
CC O88447; Q9ESN9: Mapk8ip3; NbExp=9; IntAct=EBI-301550, EBI-301496;
CC O88447; P68619: VACWR159; Xeno; NbExp=2; IntAct=EBI-301550, EBI-7133540;
CC -!- SUBCELLULAR LOCATION: Cell projection, growth cone {ECO:0000250}.
CC Cytoplasmic vesicle {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the kinesin light chain family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AF055665; AAC27740.1; -; mRNA.
DR PDB; 6FUZ; X-ray; 2.70 A; A=199-495.
DR PDB; 6FV0; X-ray; 2.29 A; A=204-495.
DR PDBsum; 6FUZ; -.
DR PDBsum; 6FV0; -.
DR AlphaFoldDB; O88447; -.
DR SMR; O88447; -.
DR CORUM; O88447; -.
DR DIP; DIP-31520N; -.
DR ELM; O88447; -.
DR IntAct; O88447; 18.
DR MINT; O88447; -.
DR STRING; 10090.ENSMUSP00000082004; -.
DR iPTMnet; O88447; -.
DR PhosphoSitePlus; O88447; -.
DR SwissPalm; O88447; -.
DR EPD; O88447; -.
DR jPOST; O88447; -.
DR MaxQB; O88447; -.
DR PaxDb; O88447; -.
DR PeptideAtlas; O88447; -.
DR PRIDE; O88447; -.
DR ProteomicsDB; 264940; -.
DR MGI; MGI:107978; Klc1.
DR eggNOG; KOG1840; Eukaryota.
DR InParanoid; O88447; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-5625970; RHO GTPases activate KTN1.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR ChiTaRS; Klc1; mouse.
DR PRO; PR:O88447; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O88447; protein.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:HGNC-UCL.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0005871; C:kinesin complex; IDA:HGNC-UCL.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043227; C:membrane-bounded organelle; IDA:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0019894; F:kinesin binding; IBA:GO_Central.
DR GO; GO:0015631; F:tubulin binding; ISO:MGI.
DR GO; GO:0008088; P:axo-dendritic transport; IMP:MGI.
DR GO; GO:0006886; P:intracellular protein transport; ISO:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0035418; P:protein localization to synapse; ISO:MGI.
DR GO; GO:0035617; P:stress granule disassembly; IMP:BHF-UCL.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR002151; Kinesin_light.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF13176; TPR_7; 1.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS01160; KINESIN_LIGHT; 3.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Microtubule; Motor protein; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..541
FT /note="Kinesin light chain 1"
FT /id="PRO_0000215093"
FT REPEAT 211..244
FT /note="TPR 1"
FT REPEAT 253..286
FT /note="TPR 2"
FT REPEAT 295..328
FT /note="TPR 3"
FT REPEAT 337..370
FT /note="TPR 4"
FT REPEAT 380..413
FT /note="TPR 5"
FT REPEAT 463..496
FT /note="TPR 6"
FT REGION 156..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 27..156
FT COMPBIAS 156..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P37285"
FT MOD_RES 448
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 520
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000305, ECO:0007744|PubMed:21183079"
FT MOD_RES 523
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000305, ECO:0007744|PubMed:21183079"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:6FV0"
FT HELIX 227..244
FT /evidence="ECO:0007829|PDB:6FV0"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6FV0"
FT HELIX 250..265
FT /evidence="ECO:0007829|PDB:6FV0"
FT HELIX 269..286
FT /evidence="ECO:0007829|PDB:6FV0"
FT HELIX 292..307
FT /evidence="ECO:0007829|PDB:6FV0"
FT HELIX 311..329
FT /evidence="ECO:0007829|PDB:6FV0"
FT HELIX 334..348
FT /evidence="ECO:0007829|PDB:6FV0"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:6FV0"
FT HELIX 356..370
FT /evidence="ECO:0007829|PDB:6FV0"
FT HELIX 377..392
FT /evidence="ECO:0007829|PDB:6FV0"
FT HELIX 396..414
FT /evidence="ECO:0007829|PDB:6FV0"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:6FV0"
FT HELIX 425..434
FT /evidence="ECO:0007829|PDB:6FV0"
FT HELIX 460..475
FT /evidence="ECO:0007829|PDB:6FV0"
FT HELIX 479..493
FT /evidence="ECO:0007829|PDB:6FV0"
SQ SEQUENCE 541 AA; 61450 MW; 550F23AB36049C03 CRC64;
MYDNMSTMVY IKEEKLENVT QDEIISKTKQ VIQGLEALKN EHNSILQSLL ETLKCLKKDD
ESNLVEEKSS MIRKSLEMLE LGLSEAQVMM ALSNHLNAVE SEKQNVRAQV RRLCQENQWL
RDELANTQQK LQKSEQSVAQ LEEEKKHLEF MNQLKKYDDD ISPSEDKDSD SSKEPLDDLF
PNDEDEPGQG IQHSDSSAAA ARQGYEIPAR LRTLHNLVIQ YASQGRYEVA VPSCKQALED
LEKTSGHDHP DVATMLNILA LVYRDQNKYK DAANLLNDAL AIREKTLGRD HPAVAATLNN
LAVLYGKRGK YKEAEPLCKR ALEIREKVLG KDHPDVAKQL NNLALLCQNQ GKYEEVEYYY
QRALGIYQTK LGPDRTPNVA KTKNNLASCY LKQGKFKQAE TLYKEILTRA HEAEFGSVDD
ENKPIWMHAE EREECKGKQK DGSAFGEYGG WYKACKVDSP TVTTTLKNLG ALYRRQGKFE
AAETLEEAAM RSRKQGLDNV HKQRVAEVLN DPESMEKRRS RESLNMDVVK YESGPDGGEE
A
