ID   KLC3_PONAB              Reviewed;         504 AA.
AC   Q5R8E2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Kinesin light chain 3;
GN   Name=KLC3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR859811; CAH91968.1; -; mRNA.
DR   RefSeq; NP_001126140.1; NM_001132668.1.
DR   AlphaFoldDB; Q5R8E2; -.
DR   SMR; Q5R8E2; -.
DR   STRING; 9601.ENSPPYP00000011315; -.
DR   GeneID; 100173098; -.
DR   KEGG; pon:100173098; -.
DR   CTD; 147700; -.
DR   eggNOG; KOG1840; Eukaryota.
DR   InParanoid; Q5R8E2; -.
DR   Proteomes; UP000001595; Unplaced.
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: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..504
FT                   /note="Kinesin light chain 3"
FT                   /id="PRO_0000230787"
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          153..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          90..150
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        157..171
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         466
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P597"
FT   MOD_RES         498
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P597"
FT   MOD_RES         502
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P597"
SQ   SEQUENCE   504 AA;  55445 MW;  46818DD23F6CEB69 CRC64;
     MSVQVAAPGS AGLGPERLSP EELVRQTRQV VQGLEALRAE HHGLVGHLAE ALAGQGPVTG
     LEMLEEKQQV VSHSLEAIEL GLGEAQVLLA LSAHVGALEA EKQRLRSQAR RLAQENVWLR
     EELEETQRRL RASEEAVAQL EEEKRHLEFL GQLRQYDPPA ESQQSESPPR RDSLASLFPS
     EEEERKGPEA AGAAAAQQGG YEIPARLRTL HNLVIQYAGQ GRYEVAVPLC RQALEDLERS
     SGHCHPDVAT MLNILALVYR DQNKYKEATD LLHDALQIRE QTLGPEHPAV AATLNNLAVL
     YGKRGRYREA EPLCQRALEI REKVLGADHP DVAKQLNNLA LLCQNQGKFE DVERHYARAL
     SIYEALGGPH DPNVAKTKNN LASAYLKQNK YQQAEELYKE ILHKEDLPAP LGAPNTGTAG
     DAEQALRRSS SLSKIRESIR RGSEKLVSRL RGEGAAGAAG MKRAMSLNTL NVDAPRALGT
     QFPSWHLDKA PRTLSASTHD LSPH