KLC3_RAT
ID KLC3_RAT Reviewed; 505 AA.
AC Q68G30; Q9ESH7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Kinesin light chain 3;
DE AltName: Full=Kinesin light chain KLCt;
GN Name=Klc3;
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], ASSOCIATION WITH MICROTUBULES, INTERACTION WITH
RP KIF5C, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DOMAIN.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 INTERACTION WITH ODF1, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=12594206; DOI=10.1074/jbc.m213126200;
RA Bhullar B., Zhang Y., Junco A., Oko R., van der Hoorn F.A.;
RT "Association of kinesin light chain with outer dense fibers in a
RT microtubule-independent fashion.";
RL J. Biol. Chem. 278:16159-16168(2003).
RN [4]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=15464570; DOI=10.1016/j.ydbio.2004.07.014;
RA Zhang Y., Oko R., van der Hoorn F.A.;
RT "Rat kinesin light chain 3 associates with spermatid mitochondria.";
RL Dev. Biol. 275:23-33(2004).
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 (By similarity). May play a role in the
CC formation of the mitochondrial sheath formation in the developing
CC spermatid midpiece (By similarity). {ECO:0000250|UniProtKB:Q91W40}.
CC -!- SUBUNIT: Oligomer composed of two heavy chains and two light chains.
CC Associates with microtubulin in an ATP-dependent manner
CC (PubMed:11319135). Interacts with KIF5C (PubMed:11319135). Interacts
CC with ODF1 (PubMed:12594206). Interacts with LRGUK (By similarity).
CC Interacts with VDAC2 (By similarity). {ECO:0000250|UniProtKB:Q91W40,
CC ECO:0000269|PubMed:11319135, ECO:0000269|PubMed:12594206}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:11319135, ECO:0000305|PubMed:12594206,
CC ECO:0000305|PubMed:15464570}. Mitochondrion
CC {ECO:0000269|PubMed:12594206, ECO:0000269|PubMed:15464570}. Note=In
CC elongating spermatid tail midpiece, localized in outer dense fibers
CC (ODFs) and associates with mitochondria (PubMed:12594206,
CC PubMed:15464570). Also localizes to the manchette in elongating
CC spermatids (By similarity). {ECO:0000250|UniProtKB:Q91W40,
CC ECO:0000269|PubMed:12594206, ECO:0000269|PubMed:15464570}.
CC -!- TISSUE SPECIFICITY: Expressed in postmeiotic male germ cells (at
CC protein level). {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. {ECO:0000269|PubMed:11319135,
CC ECO:0000269|PubMed:12594206, ECO:0000269|PubMed:15464570}.
CC -!- SIMILARITY: Belongs to the kinesin light chain family. {ECO:0000305}.
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DR EMBL; AF166267; AAG15432.1; -; mRNA.
DR EMBL; BC078736; AAH78736.1; -; mRNA.
DR EMBL; BC097284; AAH97284.1; -; mRNA.
DR RefSeq; NP_612529.1; NM_138520.1.
DR RefSeq; XP_006228440.2; XM_006228378.3.
DR RefSeq; XP_006228442.1; XM_006228380.3.
DR AlphaFoldDB; Q68G30; -.
DR SMR; Q68G30; -.
DR STRING; 10116.ENSRNOP00000060483; -.
DR iPTMnet; Q68G30; -.
DR PhosphoSitePlus; Q68G30; -.
DR jPOST; Q68G30; -.
DR PaxDb; Q68G30; -.
DR PRIDE; Q68G30; -.
DR Ensembl; ENSRNOT00000068092; ENSRNOP00000060483; ENSRNOG00000018101.
DR GeneID; 171549; -.
DR KEGG; rno:171549; -.
DR UCSC; RGD:621432; rat.
DR CTD; 147700; -.
DR RGD; 621432; Klc3.
DR eggNOG; KOG1840; Eukaryota.
DR GeneTree; ENSGT00940000162356; -.
DR HOGENOM; CLU_019953_2_0_1; -.
DR InParanoid; Q68G30; -.
DR OMA; LEHTSGH; -.
DR OrthoDB; 511880at2759; -.
DR PhylomeDB; Q68G30; -.
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:Q68G30; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018101; Expressed in testis and 18 other tissues.
DR Genevisible; Q68G30; RN.
DR GO; GO:0035253; C:ciliary rootlet; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005871; C:kinesin complex; TAS:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0031514; C:motile cilium; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0019894; F:kinesin binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0003777; F:microtubule motor activity; TAS:RGD.
DR GO; GO:0008088; P:axo-dendritic transport; ISO:RGD.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0120317; P:sperm mitochondrial sheath assembly; ISS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS: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 Pfam; PF13176; TPR_7; 1.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 5.
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..505
FT /note="Kinesin light chain 3"
FT /id="PRO_0000230788"
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..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 90..150
FT /evidence="ECO:0000255"
FT COMPBIAS 418..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91W40"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P597"
FT MOD_RES 499
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P597"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P597"
FT CONFLICT 205
FT /note="A -> D (in Ref. 1; AAG15432)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="L -> V (in Ref. 1; AAG15432)"
FT /evidence="ECO:0000305"
FT CONFLICT 220..221
FT /note="QG -> HV (in Ref. 1; AAG15432)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="V -> I (in Ref. 1; AAG15432)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="E -> V (in Ref. 1; AAG15432)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="C -> F (in Ref. 1; AAG15432)"
FT /evidence="ECO:0000305"
FT CONFLICT 249..254
FT /note="ATMLNI -> PTMVDF (in Ref. 1; AAG15432)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="L -> F (in Ref. 1; AAG15432)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="T -> I (in Ref. 1; AAG15432)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 55655 MW; DA457FE4E82F6F37 CRC64;
MSVQVAAPGS TGLGPERLNP EELVRQTRQV VQGLEALRAE HHSLAGHLAE ALAGPGPVAG
VELLEEKQQV VNHSLEAIEL GLGEAQVLLA LSAHVGVLEA EKQRLRAQAR RLAQENTWLR
EELEETQRRL RASEEAVAQL EEEKSHLQFL GQLRQYDPPE ESQRPDSPPR RDSLASLFPS
EEEEKKGPEA AGAAAAQQGG YEIPARLRTL HNLVIQYASQ GRYEVAVPLC RQALEDLERS
SGHCHPDVAT MLNILALVYR DQNKYKEATE LLHDALQIRE QTLGPEHPAV AATLNNLAVL
YGKRGRYREA EPLCQRALEI REKVLGADHP DVAKQLNNLA LLCQNQGKFQ DVERHYARAL
SIYEALGGPQ DPNVAKTKNN LASAYLKQNK YQQAEELYKE ILSQEALPAP LGAPQGGTAG
EAQQQVLRRS SSFSKLRESI RRGSEKLVSR LRGESMAGAA GMKRAMSLNM LNVDGPRAAR
MQLSTQHLNE ASRTLSASTQ DLSPR
