KLC2_MOUSE
ID KLC2_MOUSE Reviewed; 599 AA.
AC O88448;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Kinesin light chain 2 {ECO:0000305};
DE Short=KLC 2;
GN Name=Klc2 {ECO:0000312|MGI:MGI:107953};
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-178; SER-443;
RP SER-505 AND SER-575, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
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).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=30973865; DOI=10.1371/journal.pbio.3000194;
RA Ingham N.J., Pearson S.A., Vancollie V.E., Rook V., Lewis M.A., Chen J.,
RA Buniello A., Martelletti E., Preite L., Lam C.C., Weiss F.D., Powis Z.,
RA Suwannarat P., Lelliott C.J., Dawson S.J., White J.K., Steel K.P.;
RT "Mouse screen reveals multiple new genes underlying mouse and human hearing
RT loss.";
RL PLoS Biol. 17:E3000194-E3000194(2019).
CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing protein
CC that plays a role in organelle transport. The light chain functions in
CC coupling of cargo to the heavy chain or in the modulation of its ATPase
CC activity. Through binding with PLEKHM2 and ARL8B, recruits kinesin-1 to
CC lysosomes and hence direct lysosomes movement toward microtubule plus
CC ends. {ECO:0000250|UniProtKB:Q9H0B6}.
CC -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two light
CC chains. Interacts (via TPR repeats) with PLEKHM2.
CC {ECO:0000250|UniProtKB:Q9H0B6}.
CC -!- INTERACTION:
CC O88448; Q9ESN9: Mapk8ip3; NbExp=6; IntAct=EBI-301558, EBI-301496;
CC O88448; P68619: VACWR159; Xeno; NbExp=3; IntAct=EBI-301558, EBI-7133540;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9H0B6}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q9H0B6}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9H0B6}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9H0B6}.
CC -!- DISRUPTION PHENOTYPE: Mutants show a progressive hearing loss with an
CC increase in auditory brainstem response (ABR) thresholds with age,
CC mostly affecting low frequencies, with a sensorineural (not conductive)
CC pathology. At one month old, there is extensive loss of outer hair cell
CC (OHC) hair bundles. {ECO:0000269|PubMed:30973865}.
CC -!- SIMILARITY: Belongs to the kinesin light chain family. {ECO:0000305}.
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DR EMBL; AF055666; AAC27741.1; -; mRNA.
DR PDB; 3ZFW; X-ray; 2.90 A; A/B=217-478.
DR PDB; 5FJY; X-ray; 4.00 A; A/B/C=160-478.
DR PDB; 6EJN; X-ray; 3.20 A; A/B=190-477.
DR PDBsum; 3ZFW; -.
DR PDBsum; 5FJY; -.
DR PDBsum; 6EJN; -.
DR AlphaFoldDB; O88448; -.
DR SMR; O88448; -.
DR CORUM; O88448; -.
DR DIP; DIP-31518N; -.
DR ELM; O88448; -.
DR IntAct; O88448; 14.
DR MINT; O88448; -.
DR STRING; 10090.ENSMUSP00000112262; -.
DR iPTMnet; O88448; -.
DR PhosphoSitePlus; O88448; -.
DR SwissPalm; O88448; -.
DR EPD; O88448; -.
DR jPOST; O88448; -.
DR MaxQB; O88448; -.
DR PaxDb; O88448; -.
DR PeptideAtlas; O88448; -.
DR PRIDE; O88448; -.
DR ProteomicsDB; 263614; -.
DR MGI; MGI:107953; Klc2.
DR eggNOG; KOG1840; Eukaryota.
DR InParanoid; O88448; -.
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; Klc2; mouse.
DR PRO; PR:O88448; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O88448; protein.
DR GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:HGNC-UCL.
DR GO; GO:0005871; C:kinesin complex; IDA:HGNC-UCL.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0019894; F:kinesin binding; IPI:BHF-UCL.
DR GO; GO:0008088; P:axo-dendritic transport; IMP:MGI.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
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; 4.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS01160; KINESIN_LIGHT; 2.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Cytoskeleton; Lysosome; Membrane;
KW Microtubule; Motor protein; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat.
FT CHAIN 1..599
FT /note="Kinesin light chain 2"
FT /id="PRO_0000215096"
FT REPEAT 197..230
FT /note="TPR 1"
FT REPEAT 239..272
FT /note="TPR 2"
FT REPEAT 281..314
FT /note="TPR 3"
FT REPEAT 323..356
FT /note="TPR 4"
FT REPEAT 365..398
FT /note="TPR 5"
FT REPEAT 447..480
FT /note="TPR 6"
FT REGION 154..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 78..143
FT /evidence="ECO:0000255"
FT COMPBIAS 494..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0B6"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0B6"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0B6"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:6EJN"
FT HELIX 213..230
FT /evidence="ECO:0007829|PDB:6EJN"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:6EJN"
FT HELIX 236..251
FT /evidence="ECO:0007829|PDB:3ZFW"
FT HELIX 255..272
FT /evidence="ECO:0007829|PDB:3ZFW"
FT HELIX 278..293
FT /evidence="ECO:0007829|PDB:3ZFW"
FT HELIX 297..314
FT /evidence="ECO:0007829|PDB:3ZFW"
FT HELIX 320..334
FT /evidence="ECO:0007829|PDB:3ZFW"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:3ZFW"
FT HELIX 339..356
FT /evidence="ECO:0007829|PDB:3ZFW"
FT HELIX 362..377
FT /evidence="ECO:0007829|PDB:3ZFW"
FT HELIX 381..400
FT /evidence="ECO:0007829|PDB:3ZFW"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:6EJN"
FT HELIX 410..418
FT /evidence="ECO:0007829|PDB:3ZFW"
FT HELIX 444..459
FT /evidence="ECO:0007829|PDB:3ZFW"
FT HELIX 463..476
FT /evidence="ECO:0007829|PDB:3ZFW"
SQ SEQUENCE 599 AA; 66662 MW; A5E6F9081609E1CE CRC64;
MATMVLPREE KLSQDEIVLG TKAVIQGLET LRGEHRALLA PLASHEAGEA EPGSQERCLL
LRRSLEAIEL GLGEAQVILA LSSHLGAVES EKQKLRAQVR RLVQENQWLR EELAGTQQKL
QRSEQAVAQL EEEKQHLLFM SQIRKLDEML PQEEKGDVPK DSLDDLFPNE DEQSPAPSPG
GGDVAAQHGG YEIPARLRTL HNLVIQYASQ GRYEVAVPLC KQALEDLEKT SGHDHPDVAT
MLNILALVYR DQNKYKDAAH LLNDALAIRE KTLGKDHPAV AATLNNLAVL YGKRGKYKEA
EPLCKRALEI REKVLGKFHP DVAKQLSNLA LLCQNQGKAE EVEYYYRRAL EIYATRLGPD
DPNVAKTKNN LASCYLKQGK YQDAETLYKE ILTRAHEKEF GSVNGENKPI WMHAEEREES
KDKRRDRRPM EYGSWYKACK VDSPTVNTTL RTLGALYRPE GKLEAAHTLE DCASRSRKQG
LDPASQTKVV ELLKDGSGRG HRRGSRDVAG PQSESDLEES GPAAEWSGDG SGSLRRSGSF
GKLRDALRRS SEMLVRKLQG GGPQEPNSRM KRASSLNFLN KSVEEPVQPG GRVFLTAAL
