ID A0A2Y9JIP0_ENHLU Unreviewed; 551 AA.
AC A0A2Y9JIP0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
GN Name=LOC111148551 {ECO:0000313|RefSeq:XP_022360913.1,
GN ECO:0000313|RefSeq:XP_022360915.1, ECO:0000313|RefSeq:XP_022360916.1};
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_022360913.1};
RN [1] {ECO:0000313|RefSeq:XP_022360913.1, ECO:0000313|RefSeq:XP_022360915.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022360913.1,
RC ECO:0000313|RefSeq:XP_022360915.1};
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_022360913.1; XM_022505205.1.
DR RefSeq; XP_022360915.1; XM_022505207.1.
DR RefSeq; XP_022360916.1; XM_022505208.1.
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:SF7; KINESIN LIGHT CHAIN 1; 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; 2.
DR PROSITE; PS01160; KINESIN_LIGHT; 1.
DR PROSITE; PS50005; TPR; 1.
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 297..330
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 155..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 89..151
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 155..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 62826 MW; 52386AA4A1DFF269 CRC64;
MYDNMSTMVY IKEDKLEKLT QDEIISKTKQ VIQGLEALKN EHNSILQSLL ETLKCLKKDD
ESNLVEEKSN MIRKSLEMLE LGLSEAQVMM ALSNHLNAVE SEKQKLRAQV RRLCQENQWL
RDELANTQQK LQKSEQSVAQ LEEEKKHLEF MNQLKKYDDD ISPSEDKDTD STKEPLDDLF
PNDDDDPGQG IQQQHSSAAA AAQQGGYEIP ARLRTLHNLV IQYASQGRYE VAVPLCKQAL
EDLEKTSGHD HPDVATMLNI LALVYRDQNK YKDAANLLND ALAIREKTLG KDHPAVAATL
NNLAVLYGKR GKYKEAEPLC KRALEIREKV LGKDHPDVAK QLNNLALLCQ NQGKYEEVEY
YYQRALEIYQ TKLGPDDPNV AKTKNNLASC YLKQGKFKQA ETLYKEILTR AHEREFGSVD
DENKPIWMHA EEREECKGKQ KDGTSFGEYG GWYKACKVDS PTVTTTLKNL GALYRRQGKF
EAAETLEEAA MRSRKQGLDN VHKQRVAEVL NDPENMEKRR SRESLNVDVV KYESGPDGGE
EMRKMKLGLV K
//
