KLC4_MOUSE
ID KLC4_MOUSE Reviewed; 619 AA.
AC Q9DBS5; Q3TCC5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Kinesin light chain 4;
DE Short=KLC 4;
DE AltName: Full=Kinesin-like protein 8;
GN Name=Klc4; Synonyms=Knsl8;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-566 AND SER-590, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, 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 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two light
CC chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the kinesin light chain family. {ECO:0000305}.
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DR EMBL; AK004774; BAB23552.1; -; mRNA.
DR EMBL; AK170793; BAE42032.1; -; mRNA.
DR CCDS; CCDS28832.1; -.
DR RefSeq; NP_083367.1; NM_029091.2.
DR RefSeq; XP_006525106.1; XM_006525043.2.
DR RefSeq; XP_011244990.1; XM_011246688.2.
DR RefSeq; XP_011244991.1; XM_011246689.1.
DR AlphaFoldDB; Q9DBS5; -.
DR SMR; Q9DBS5; -.
DR BioGRID; 217004; 28.
DR DIP; DIP-48704N; -.
DR IntAct; Q9DBS5; 8.
DR STRING; 10090.ENSMUSP00000003642; -.
DR iPTMnet; Q9DBS5; -.
DR PhosphoSitePlus; Q9DBS5; -.
DR SwissPalm; Q9DBS5; -.
DR EPD; Q9DBS5; -.
DR jPOST; Q9DBS5; -.
DR MaxQB; Q9DBS5; -.
DR PaxDb; Q9DBS5; -.
DR PeptideAtlas; Q9DBS5; -.
DR PRIDE; Q9DBS5; -.
DR ProteomicsDB; 263615; -.
DR Antibodypedia; 30259; 77 antibodies from 18 providers.
DR DNASU; 74764; -.
DR Ensembl; ENSMUST00000003642; ENSMUSP00000003642; ENSMUSG00000003546.
DR Ensembl; ENSMUST00000233974; ENSMUSP00000156564; ENSMUSG00000003546.
DR GeneID; 74764; -.
DR KEGG; mmu:74764; -.
DR UCSC; uc008ctj.1; mouse.
DR CTD; 89953; -.
DR MGI; MGI:1922014; Klc4.
DR VEuPathDB; HostDB:ENSMUSG00000003546; -.
DR eggNOG; KOG1840; Eukaryota.
DR GeneTree; ENSGT00940000161323; -.
DR HOGENOM; CLU_019953_0_0_1; -.
DR InParanoid; Q9DBS5; -.
DR OMA; LQHEGHE; -.
DR OrthoDB; 511880at2759; -.
DR PhylomeDB; Q9DBS5; -.
DR TreeFam; TF314010; -.
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 BioGRID-ORCS; 74764; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Klc4; mouse.
DR PRO; PR:Q9DBS5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9DBS5; protein.
DR Bgee; ENSMUSG00000003546; Expressed in small intestine Peyer's patch and 256 other tissues.
DR Genevisible; Q9DBS5; MM.
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; 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 Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NSK0"
FT CHAIN 2..619
FT /note="Kinesin light chain 4"
FT /id="PRO_0000215098"
FT REPEAT 55..88
FT /note="TPR 1"
FT REPEAT 211..244
FT /note="TPR 2"
FT REPEAT 253..286
FT /note="TPR 3"
FT REPEAT 295..328
FT /note="TPR 4"
FT REPEAT 337..370
FT /note="TPR 5"
FT REPEAT 379..412
FT /note="TPR 6"
FT REPEAT 464..497
FT /note="TPR 7"
FT REGION 156..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 65..155
FT /evidence="ECO:0000255"
FT COMPBIAS 156..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSK0"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSK0"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQM2"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 612
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSK0"
SQ SEQUENCE 619 AA; 68613 MW; BE2D6B3CD451A7BF CRC64;
MSGLVLGQRD EPAGHRLSQE EILGSTKVVS QGLEALHSEH QAVLQSLSHT IECLQQGGHE
EGLVHEKARQ LRRSMENIEL GLSEAQVMLA LASHLSTVES EKQKLRAQVR RLCQENQWLR
DELAGTQQRL QRSEQAVAQL EEEKKHLEFL RQLRQYDEDG HGMEEKEGEA TKDSLDDLFP
NEEEEDSGND LSRGQGAAAA QQGGYEIPAR LRTLHNLVIQ YAAQGRYEVA VPLCKQALED
LERTSGRGHP DVATMLNILA LVYRDQNKYK EAAHLLNDAL SIRESTLGRD HPAVAATLNN
LAVLYGKRGK YKEAEPLCQR ALEIREKVLG TDHPDVAKQL NNLALLCQNQ GKYEAVERYY
QRALAIYESQ LGPDNPNVAR TKNNLASCYL KQGKYSEAEA LYKEILTCAH VQEFGSVDDD
HKPIWMHAEE REEMSRSRPR DSSAPYAEYG GWYKACRVSS PTVNTTLKNL GALYRRQGKL
EAAETLEECA LRSRKQGTDP ISQTKVAELL GEGDGRKAIQ EGPGDSVKFE GGEDASVAVE
WSGDGSGTLQ RSGSLGKIRD VLRRSSELLV RKLQGTEPRP SSSSMKRAAS LNYLNQPNAA
PLQVSRGLSA STVDLSSSS
