KLC3_MOUSE
ID KLC3_MOUSE Reviewed; 508 AA.
AC Q91W40; Q3TZ56;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Kinesin light chain 3;
GN Name=Klc3;
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; TISSUE=Inner ear;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11319135; DOI=10.1095/biolreprod64.5.1320;
RA Junco A., Bhullar B., Tarnasky H.A., van der Hoorn F.A.;
RT "Kinesin light-chain KLC3 expression in testis is restricted to
RT spermatids.";
RL Biol. Reprod. 64:1320-1330(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-467, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, 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).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VDAC2, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22561200; DOI=10.1016/j.ydbio.2012.04.026;
RA Zhang Y., Ou Y., Cheng M., Saadi H.S., Thundathil J.C., van der Hoorn F.A.;
RT "KLC3 is involved in sperm tail midpiece formation and sperm function.";
RL Dev. Biol. 366:101-110(2012).
RN [6]
RP INTERACTION WITH LRGUK, AND SUBCELLULAR LOCATION.
RX PubMed=28003339; DOI=10.1096/fj.201600909r;
RA Okuda H., DeBoer K., O'Connor A.E., Merriner D.J., Jamsai D., O'Bryan M.K.;
RT "LRGUK1 is part of a multiprotein complex required for manchette function
RT and male fertility.";
RL FASEB J. 31:1141-1152(2017).
CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing protein
CC that may play a role in organelle transport. Plays a role during
CC spermiogenesis in the development of the sperm tail midpiece and in the
CC normal function of spermatozoa (PubMed:22561200). May play a role in
CC the formation of the mitochondrial sheath formation in the developing
CC spermatid midpiece (PubMed:22561200). {ECO:0000269|PubMed:22561200}.
CC -!- SUBUNIT: Oligomer composed of two heavy chains and two light chains (By
CC similarity). Associates with microtubulin in an ATP-dependent manner
CC (By similarity). Interacts with KIF5C. Interacts with ODF1 (By
CC similarity). Interacts with LRGUK (PubMed:28003339). Interacts with
CC VDAC2 (PubMed:22561200). {ECO:0000250|UniProtKB:Q68G30,
CC ECO:0000269|PubMed:22561200, ECO:0000269|PubMed:28003339}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:28003339, ECO:0000305|PubMed:11319135}.
CC Mitochondrion {ECO:0000269|PubMed:22561200}. Note=In elongating
CC spermatid tail midpiece, localized in outer dense fibers (ODFs) and
CC associates with mitochondria (By similarity). Also localizes to the
CC manchette in elongating spermatids (PubMed:28003339).
CC {ECO:0000250|UniProtKB:Q68G30, ECO:0000269|PubMed:28003339}.
CC -!- TISSUE SPECIFICITY: Expressed in postmeiotic male germ cells (at
CC protein level). Expressed in spleen, intestine, brain, ovary, testis,
CC spermatocytes and spermatids. {ECO:0000269|PubMed:11319135}.
CC -!- DOMAIN: The heptad repeat (HR) motif is sufficient for interaction with
CC kinesin heavy (KHL) chains and ODF1. The TPR region is involved in
CC mitochondrial binding (By similarity). {ECO:0000250|UniProtKB:Q68G30}.
CC -!- DISRUPTION PHENOTYPE: Male transgenic mice (expressing a KLC3 deletion
CC mutant) display significantly reduced reproductive efficiency siring
CC small sized litters (PubMed:22561200). Show significantly reduced sperm
CC count, defective mitochondrial sheath structure in a number of
CC spermatids and produce spermatozoa that exhibit abnormal motility
CC parameters (PubMed:22561200). {ECO:0000269|PubMed:22561200}.
CC -!- SIMILARITY: Belongs to the kinesin light chain family. {ECO:0000305}.
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DR EMBL; AK158094; BAE34354.1; -; mRNA.
DR EMBL; BC017147; AAH17147.1; -; mRNA.
DR CCDS; CCDS20901.1; -.
DR RefSeq; NP_001272967.1; NM_001286038.1.
DR RefSeq; NP_001272968.1; NM_001286039.1.
DR RefSeq; NP_666294.1; NM_146182.4.
DR AlphaFoldDB; Q91W40; -.
DR SMR; Q91W40; -.
DR BioGRID; 231327; 19.
DR DIP; DIP-48703N; -.
DR IntAct; Q91W40; 17.
DR STRING; 10090.ENSMUSP00000104099; -.
DR iPTMnet; Q91W40; -.
DR PhosphoSitePlus; Q91W40; -.
DR EPD; Q91W40; -.
DR jPOST; Q91W40; -.
DR MaxQB; Q91W40; -.
DR PaxDb; Q91W40; -.
DR PRIDE; Q91W40; -.
DR ProteomicsDB; 263447; -.
DR Antibodypedia; 31299; 146 antibodies from 22 providers.
DR DNASU; 232943; -.
DR Ensembl; ENSMUST00000047170; ENSMUSP00000038091; ENSMUSG00000040714.
DR Ensembl; ENSMUST00000108458; ENSMUSP00000104098; ENSMUSG00000040714.
DR Ensembl; ENSMUST00000108459; ENSMUSP00000104099; ENSMUSG00000040714.
DR GeneID; 232943; -.
DR KEGG; mmu:232943; -.
DR UCSC; uc009fls.2; mouse.
DR CTD; 147700; -.
DR MGI; MGI:1277971; Klc3.
DR VEuPathDB; HostDB:ENSMUSG00000040714; -.
DR eggNOG; KOG1840; Eukaryota.
DR GeneTree; ENSGT00940000162356; -.
DR InParanoid; Q91W40; -.
DR OrthoDB; 511880at2759; -.
DR PhylomeDB; Q91W40; -.
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; 232943; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Klc3; mouse.
DR PRO; PR:Q91W40; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q91W40; protein.
DR Bgee; ENSMUSG00000040714; Expressed in lip and 147 other tissues.
DR ExpressionAtlas; Q91W40; baseline and differential.
DR Genevisible; Q91W40; MM.
DR GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IMP:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0019894; F:kinesin binding; IDA:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0008088; P:axo-dendritic transport; IMP:MGI.
DR GO; GO:0042073; P:intraciliary transport; TAS:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0120317; P:sperm mitochondrial sheath assembly; IMP:UniProtKB.
DR GO; GO:0007286; P:spermatid development; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
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 PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Differentiation; Microtubule;
KW Mitochondrion; Motor protein; Phosphoprotein; Reference proteome; Repeat;
KW Spermatogenesis; TPR repeat.
FT CHAIN 1..508
FT /note="Kinesin light chain 3"
FT /id="PRO_0000230786"
FT REPEAT 207..240
FT /note="TPR 1"
FT REPEAT 249..282
FT /note="TPR 2"
FT REPEAT 291..324
FT /note="TPR 3"
FT REPEAT 333..366
FT /note="TPR 4"
FT REPEAT 375..408
FT /note="TPR 5"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 88..150
FT /evidence="ECO:0000255"
FT COMPBIAS 417..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 502
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P597"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P597"
FT CONFLICT 313
FT /note="L -> P (in Ref. 1; BAE34354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 56006 MW; 7F6F11CB943792C2 CRC64;
MSVQVAAPGS TGLGPERLNP EELVRQTRQV VQGLEALRAE HHSLAGHLAE ALAGPGPVAG
VELLEEKQQV VNHSLEAIEL GLGEAQVLLA LSAHVSVLEA EKQRLRAQAR RLAQENTWLR
EELEETQRRL RASEEAVAQL EEEKSHLQFL GQLRQYDPPE ESQRPESPPR RDSLASLFPS
EEEEKKGPEA AGAAAAQQGG YEIPARLRTL HNLVIQYAGQ GRYEVAVPLC RQALEDLERS
SGHCHPDVAT MLNILALVYR DQNKYKEATE LLHDALQIRE QTLGPEHPAV AATLNNLAVL
YGKRGRYREA EPLCQRALEI REKVLGADHP DVAKQLNNLA LLCQNQGKFQ DVERHYARAL
SIYEALGGPQ DPNVAKTKNN LASAYLKQNK YQQAEELYKE ILSQEALPAP LGAPQGGTAG
DTQQQVLRRS SSFSKLRESI RRGSEKLVSR LRGEGMAGAA GMKRAMSLNM LNVDGPRAAR
TQLSQLSTRH LSEAPRTLSI STQDLSPR
