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   09-DEC-2015, entry version 122.
DE   RecName: Full=Kinesin light chain 2;
DE            Short=KLC 2;
GN   Name=Klc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; 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
RT   characterization of the encoded proteins.";
RL   J. Biol. Chem. 273:15395-15403(1998).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND IDENTIFICATION
RP   BY 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
RT   electron 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
RP   SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
RC   Spleen, 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Kinesin is a microtubule-associated force-producing
CC       protein that may play a role in organelle transport. The light
CC       chain may function in coupling of cargo to the heavy chain or in
CC       the modulation of its ATPase activity.
CC   -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two
CC       light chains.
CC   -!- INTERACTION:
CC       Q9ESN9:Mapk8ip3; NbExp=6; IntAct=EBI-301558, EBI-301496;
CC       P68619:VACWR159 (xeno); NbExp=3; IntAct=EBI-301558, EBI-7133540;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the kinesin light chain family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 6 TPR repeats. {ECO:0000255|PROSITE-
CC       ProRule:PRU00339}.
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DR   EMBL; AF055666; AAC27741.1; -; mRNA.
DR   UniGene; Mm.271648; -.
DR   PDB; 3ZFW; X-ray; 2.90 A; A/B=217-479.
DR   PDBsum; 3ZFW; -.
DR   ProteinModelPortal; O88448; -.
DR   SMR; O88448; 55-83, 178-478.
DR   DIP; DIP-31518N; -.
DR   IntAct; O88448; 14.
DR   MINT; MINT-136135; -.
DR   STRING; 10090.ENSMUSP00000112262; -.
DR   PhosphoSite; O88448; -.
DR   MaxQB; O88448; -.
DR   PaxDb; O88448; -.
DR   PRIDE; O88448; -.
DR   MGI; MGI:107953; Klc2.
DR   eggNOG; KOG1840; Eukaryota.
DR   eggNOG; COG0457; LUCA.
DR   HOVERGEN; HBG006217; -.
DR   InParanoid; O88448; -.
DR   ChiTaRS; Klc2; mouse.
DR   PRO; PR:O88448; -.
DR   Proteomes; UP000000589; Unplaced.
DR   CleanEx; MM_KLC2; -.
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.
DR   GO; GO:0005871; C:kinesin complex; IDA:HGNC.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0043234; C:protein complex; ISO:MGI.
DR   GO; GO:0019894; F:kinesin binding; IPI:BHF-UCL.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0008088; P:axon cargo transport; IMP:MGI.
DR   GO; GO:0007018; P:microtubule-based movement; TAS:HGNC.
DR   Gene3D; 1.25.40.10; -; 2.
DR   InterPro; IPR002151; Kinesin_light.
DR   InterPro; IPR015792; Kinesin_light_repeat.
DR   InterPro; IPR013026; TPR-contain_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom.
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; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Microtubule; Motor protein; Phosphoprotein; Reference proteome;
KW   Repeat; TPR repeat.
FT   CHAIN         1    599       Kinesin light chain 2.
FT                                /FTId=PRO_0000215096.
FT   REPEAT      197    230       TPR 1.
FT   REPEAT      239    272       TPR 2.
FT   REPEAT      281    314       TPR 3.
FT   REPEAT      323    356       TPR 4.
FT   REPEAT      365    398       TPR 5.
FT   REPEAT      447    480       TPR 6.
FT   COILED       78    143       {ECO:0000255}.
FT   MOD_RES     174    174       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     178    178       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     443    443       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     505    505       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     574    574       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H0B6}.
FT   MOD_RES     575    575       Phosphoserine.
FT                                {ECO:0000244|PubMed:19131326,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES     582    582       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H0B6}.
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
//