KLC1_RAT
ID KLC1_RAT Reviewed; 560 AA.
AC P37285;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Kinesin light chain 1;
DE Short=KLC 1;
GN Name=Klc1; Synonyms=Klc, Kns2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
RC TISSUE=Brain;
RX PubMed=1946431; DOI=10.1073/pnas.88.22.10114;
RA Cyr J.L., Pfister K.K., Bloom G.S., Slaughter C.A., Brady S.T.;
RT "Molecular genetics of kinesin light chains: generation of isoforms by
RT alternative splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10114-10118(1991).
RN [2]
RP INTERACTION WITH TOR1A, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14970196; DOI=10.1074/jbc.m401332200;
RA Kamm C., Boston H., Hewett J., Wilbur J., Corey D.P., Hanson P.I.,
RA Ramesh V., Breakefield X.O.;
RT "The early onset dystonia protein torsinA interacts with kinesin light
RT chain 1.";
RL J. Biol. Chem. 279:19882-19892(2004).
RN [3]
RP FUNCTION, AND 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-521 AND SER-524, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP INTERACTION WITH NTRK2 AND MAPK8IP3.
RX PubMed=21775604; DOI=10.1523/jneurosci.0436-11.2011;
RA Huang S.H., Duan S., Sun T., Wang J., Zhao L., Geng Z., Yan J., Sun H.J.,
RA Chen Z.Y.;
RT "JIP3 mediates TrkB axonal anterograde transport and enhances BDNF
RT signaling by directly bridging TrkB with kinesin-1.";
RL J. Neurosci. 31:10602-10614(2011).
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. {ECO:0000269|PubMed:19861499}.
CC -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two light
CC chains. Interacts with SPAG9. Interacts with ATCAY; may link
CC mitochondria to KLC1 and regulate mitochondria localization into neuron
CC projections. Interacts (via TPR repeats) with TOR1A; the interaction
CC associates TOR1A with the kinesin oligomeric complex. Interacts with
CC BORCS5 (By similarity). Interacts with MAPK8IP3/JIP3 and NTRK2/TRKB;
CC interaction with NTRK2/TRKB is mediated by MAPK8IP3/JIP3
CC (PubMed:21775604). {ECO:0000250|UniProtKB:Q07866,
CC ECO:0000269|PubMed:14970196, ECO:0000269|PubMed:19861499,
CC ECO:0000269|PubMed:21775604}.
CC -!- INTERACTION:
CC P37285; P68619: VACWR159; Xeno; NbExp=4; IntAct=EBI-917396, EBI-7133540;
CC -!- SUBCELLULAR LOCATION: Cell projection, growth cone
CC {ECO:0000269|PubMed:14970196}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:14970196}. Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:14970196}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=C;
CC IsoId=P37285-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P37285-2; Sequence=VSP_002872;
CC Name=B;
CC IsoId=P37285-3; Sequence=VSP_002871;
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:14970196}.
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; M75146; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M75147; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M75148; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001075442.1; NM_001081973.1. [P37285-3]
DR RefSeq; NP_001075443.1; NM_001081974.1. [P37285-1]
DR AlphaFoldDB; P37285; -.
DR SMR; P37285; -.
DR BioGRID; 251058; 7.
DR CORUM; P37285; -.
DR DIP; DIP-36927N; -.
DR ELM; P37285; -.
DR IntAct; P37285; 4.
DR MINT; P37285; -.
DR STRING; 10116.ENSRNOP00000015935; -.
DR ChEMBL; CHEMBL2176819; -.
DR iPTMnet; P37285; -.
DR PhosphoSitePlus; P37285; -.
DR SwissPalm; P37285; -.
DR jPOST; P37285; -.
DR PaxDb; P37285; -.
DR PRIDE; P37285; -.
DR Ensembl; ENSRNOT00000015935; ENSRNOP00000015935; ENSRNOG00000011572. [P37285-3]
DR Ensembl; ENSRNOT00000092774; ENSRNOP00000075931; ENSRNOG00000011572. [P37285-1]
DR GeneID; 171041; -.
DR KEGG; rno:171041; -.
DR UCSC; RGD:621411; rat. [P37285-1]
DR CTD; 3831; -.
DR RGD; 621411; Klc1.
DR eggNOG; KOG1840; Eukaryota.
DR GeneTree; ENSGT00940000155555; -.
DR InParanoid; P37285; -.
DR OrthoDB; 511880at2759; -.
DR PhylomeDB; P37285; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-5625970; RHO GTPases activate KTN1.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-983189; Kinesins.
DR PRO; PR:P37285; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000011572; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; P37285; baseline and differential.
DR Genevisible; P37285; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0035253; C:ciliary rootlet; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0005871; C:kinesin complex; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0043227; C:membrane-bounded organelle; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0031982; C:vesicle; IDA:RGD.
DR GO; GO:0019894; F:kinesin binding; IBA:GO_Central.
DR GO; GO:0015631; F:tubulin binding; IDA:RGD.
DR GO; GO:0008088; P:axo-dendritic transport; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IMP:RGD.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0035418; P:protein localization to synapse; IMP:UniProtKB.
DR GO; GO:0035617; P:stress granule disassembly; ISO:RGD.
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 Pfam; PF13176; TPR_7; 1.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 2.
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; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Microtubule; Motor protein;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..560
FT /note="Kinesin light chain 1"
FT /id="PRO_0000215094"
FT REPEAT 213..246
FT /note="TPR 1"
FT REPEAT 255..288
FT /note="TPR 2"
FT REPEAT 297..330
FT /note="TPR 3"
FT REPEAT 339..372
FT /note="TPR 4"
FT REPEAT 381..414
FT /note="TPR 5"
FT REPEAT 464..497
FT /note="TPR 6"
FT REGION 156..203
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 187..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 449
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O88447"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88447"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 542..560
FT /note="VSMSVEWNGMRKMKLGLVK -> A (in isoform A)"
FT /evidence="ECO:0000303|PubMed:1946431"
FT /id="VSP_002872"
FT VAR_SEQ 542..550
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:1946431"
FT /id="VSP_002871"
SQ SEQUENCE 560 AA; 63745 MW; 24D0C4CF9E304366 CRC64;
MHDNMSTMVY MKEEKLEKLT QDEIISKTKQ VIQGLEALKN EHNSILQSLL ETLKCLKKDD
ESNLVEEKSS MIRKSLEMLE LGLSEAQVMM ALSNHLNAVE SEKQKLRAQV RRLCQENQWL
RDELANTQQK LQKSEQSVAQ LEEEKKHLEF MNQLKKYDDD ISPSEDKDSD SSKEPLDDLF
PNDEDDPGQG IQQQHSSAAA AAQQGGYEIP ARLRTLHNLV IQYASQGRYE VAVPLCKQAL
EDLEKTSGHD HPDVATMLNI LALVYRDQNK YKDAANLLND ALAIREKTLG RDHPAVAATL
NNLAVLYGKR GKYKEAEPLC KRALEIREKV LGKDHPDVAK QLNNLALLCQ NQGKYEEVEY
YYQRALEIYQ TKLGPDDPNV AKTKNNLASC YLKQGKFKQA ETLYKEILTR AHEREFGSVD
DENKPIWMHA EEREECKGKQ KDGSSFGEYG GWYKACKVDS PTVTTTLKNL GALYRRQGKF
EAAETLEEAA LRSRKQGLDN VHKQRVAEVL NDPENVEKRR SRESLNVDVV KYESGPDGGE
EVSMSVEWNG MRKMKLGLVK
