ID   A0A2Y9JP85_ENHLU        Unreviewed;       616 AA.
AC   A0A2Y9JP85;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
GN   Name=LOC111147688 {ECO:0000313|RefSeq:XP_022359620.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022359620.1};
RN   [1] {ECO:0000313|RefSeq:XP_022359620.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022359620.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- SIMILARITY: Belongs to the kinesin light chain family.
CC       {ECO:0000256|ARBA:ARBA00009622, ECO:0000256|RuleBase:RU367020}.
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DR   RefSeq; XP_022359620.1; XM_022503912.1.
DR   AlphaFoldDB; A0A2Y9JP85; -.
DR   KEGG; elk:111147688; -.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005871; C:kinesin complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR002151; Kinesin_light.
DR   InterPro; IPR015792; Kinesin_light_repeat.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45783; KINESIN LIGHT CHAIN; 1.
DR   PANTHER; PTHR45783:SF6; KINESIN LIGHT CHAIN 4; 1.
DR   Pfam; PF13374; TPR_10; 2.
DR   Pfam; PF13424; TPR_12; 2.
DR   PRINTS; PR00381; KINESINLIGHT.
DR   SMART; SM00028; TPR; 5.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   PROSITE; PS01160; KINESIN_LIGHT; 1.
DR   PROSITE; PS50005; TPR; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|RuleBase:RU367020};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW   ECO:0000256|RuleBase:RU367020};
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:UP000248482};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}.
FT   REPEAT          250..283
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          292..325
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          154..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          95..150
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        154..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   616 AA;  68322 MW;  DAE00FAC0B8E8B7B CRC64;
     MSGLVLGQRD EPAGHRLSQE EILGSTRLVS QGLEALHSEH QAVLQSLSHT IECLQQGGHE
     EGLVHEKARQ LRRSMENIEL GLSEAQVMLA LASHLSTVES EKQKLRAQVR RLCQENQWLR
     DELAGTQQRL QRSEQAVAQL EEEKKHLEFL GQLRQYDEDG HTAEEKEGDA TKDSLDDLFP
     NEEEEDSSNG LSRSQGAQHS GYEIPARLRT LHNLVIQYAA QGRYEVAVPL CKQALEDLER
     TSGRGHPDVA TMLNILALVY RDQNKYKEAA HLLNDALNIR ESTLGRDHPA VAATLNNLAV
     LYGKRGKYKE AEPLCQRALE IREKVLGTDH PDVAKQLNNL ALLCQNQGKY EAVERYYRRA
     LAIYEGQLGP DNPNVARTKN NLASCYLKQG KYAEAETLYK EILTRAHVQE FGSVDDDHKP
     IWMHAEEREE MSKSQHREGG TPYTEYGGWY KACKVSSPTV NTTLRNLGAL YRRQGKLEAA
     ETLEECALRS QKQGTDPISQ TKVAELLGEG DSGRTSQEGP GGSVKFEGGE DASVAVEWSG
     DGSGTLQRSG SLGKIRDVLR RSSELLVRKL QGTEPRPSSS NMKRAASLNY LNQPSAAPLQ
     VSRGLSASTT DLSSSS
//