KLC3_BOVIN
ID KLC3_BOVIN Reviewed; 505 AA.
AC Q2TBQ9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Kinesin light chain 3;
GN Name=KLC3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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. Interacts with
CC KIF5C. Interacts with ODF1. Interacts with LRGUK (By similarity).
CC Interacts with VDAC2 (By similarity). {ECO:0000250|UniProtKB:Q68G30,
CC ECO:0000250|UniProtKB:Q91W40}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q68G30, ECO:0000250|UniProtKB:Q91W40}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q91W40}. Note=In elongating
CC spermatid tail midpiece, localized in outer dense fibers (ODFs) and
CC associates with mitochondria. Also localizes to the manchette in
CC elongating spermatids. {ECO:0000250|UniProtKB:Q68G30,
CC ECO:0000250|UniProtKB:Q91W40}.
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 -!- SIMILARITY: Belongs to the kinesin light chain family. {ECO:0000305}.
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DR EMBL; BC109786; AAI09787.1; -; mRNA.
DR RefSeq; NP_001033638.1; NM_001038549.1.
DR AlphaFoldDB; Q2TBQ9; -.
DR SMR; Q2TBQ9; -.
DR STRING; 9913.ENSBTAP00000041235; -.
DR PaxDb; Q2TBQ9; -.
DR PRIDE; Q2TBQ9; -.
DR GeneID; 517633; -.
DR KEGG; bta:517633; -.
DR CTD; 147700; -.
DR eggNOG; KOG1840; Eukaryota.
DR InParanoid; Q2TBQ9; -.
DR Proteomes; UP000009136; Unplaced.
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:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:GOC.
DR GO; GO:0019894; F:kinesin binding; IBA:GO_Central.
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 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 2: Evidence at transcript 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_0000244524"
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 157..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 88..150
FT /evidence="ECO:0000255"
FT COMPBIAS 413..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..505
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"
SQ SEQUENCE 505 AA; 55583 MW; AFDBCC1FF7031651 CRC64;
MSVQVAAPGG LGLGLERPSP EELVRQTRQV VKGLEALRAE HRGLAGHLAE ALAAQGPAAG
LELLEEKQQV VSHSLEAIEL GLGEAQVLLA LSAHVGALEA EKQRLRAQAR RLAQENAWLR
EELEETQRRL RASEEAVAQL EEEKSHLEFL GQLRQYDPPA ESQQPESPPR RDSLASLFPS
EEEERRGPEA VGAAAAQQGG YEIPARLRTL HNLVIQYAGQ GRYEVAVPLC RQALEDLERS
SGHCHPDVAT MLNILALVYR DQNKYKEATD LLHDALQIRE QTLGPEHPAV AATLNNLAVL
YGKRGRYREA EPLCQRALEI REKVLGADHP DVAKQLNNLA LLCQNQGKFE EVERHYARAL
SIYEALGGPH DPNVAKTKNN LASAYLKQNK YQQAEELYKE ILHREALPAP LGAPNTGTTS
DTQQQTLSRS SSFSKLRESI RRGSEKLVSR LRGEGAAGAA GMKRAMSLSM LNTDGSRAPE
NQFPRQHLSE ASRTLSTSTQ DLGPR
