ID M7AW13_CHEMY Unreviewed; 269 AA.
AC M7AW13;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
GN ORFNames=UY3_15672 {ECO:0000313|EMBL:EMP27230.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP27230.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- FUNCTION: Kinesin is a microtubule-associated force-producing protein
CC that play a role in organelle transport.
CC {ECO:0000256|RuleBase:RU367020}.
CC -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two light
CC chains. {ECO:0000256|RuleBase:RU367020}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU367020}.
CC Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the kinesin light chain family.
CC {ECO:0000256|ARBA:ARBA00009622, ECO:0000256|RuleBase:RU367020}.
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DR EMBL; KB572445; EMP27230.1; -; Genomic_DNA.
DR AlphaFoldDB; M7AW13; -.
DR STRING; 8469.M7AW13; -.
DR eggNOG; KOG1840; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005871; C:kinesin complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR002151; Kinesin_light.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45783; KINESIN LIGHT CHAIN; 1.
DR PANTHER; PTHR45783:SF1; KINESIN LIGHT CHAIN 3; 1.
DR Pfam; PF13374; TPR_10; 2.
DR Pfam; PF13424; TPR_12; 1.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|RuleBase:RU367020};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|RuleBase:RU367020};
KW Differentiation {ECO:0000256|ARBA:ARBA00022871};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU367020};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175,
KW ECO:0000256|RuleBase:RU367020};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Spermatogenesis {ECO:0000256|ARBA:ARBA00022871};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT REPEAT 41..74
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 125..158
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 160..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 269 AA; 29530 MW; 833E337A7F1C35FB CRC64;
MLNILALVYR DQNKYKEATD LLNDALDIRE QALGVEHPAV AATLNNLAVL YGKRGKYKEA
EPLCKRALEI REKVLGTTHP DVAKQLNNLA LLCQNQGKFE EVERYYERAL RIYQSQLGPH
DPNVAKTKNN LASSYLKQGK YQQAEELYKE ILTSHDKELA PARHGDPAAG QSSADPLSQD
AMGHVRRSSS FSKLRESIRR GSEKLVSRLK GESVQPIDPN PGMKRASSLN VLHVGERPPV
PAASPAVPSR NLSASSQNLS PSSSLSSAG
//
