ID A0A2K6ESQ5_PROCO Unreviewed; 590 AA.
AC A0A2K6ESQ5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
GN Name=KLC1 {ECO:0000313|Ensembl:ENSPCOP00000004767.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000004767.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000004767.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K6ESQ5; -.
DR Ensembl; ENSPCOT00000015077.1; ENSPCOP00000004767.1; ENSPCOG00000013111.1.
DR GeneTree; ENSGT00940000155555; -.
DR Proteomes; UP000233160; 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:UP000233160};
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 REGION 493..523
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 590 AA; 67089 MW; DE8D10CF468DEE29 CRC64;
MYDNMSTMVY IKEDKLEKLT QDEIISKTKQ VIQGLEALKN EHNSILQSLL ETLKCLKKDD
ESNLVEEKSN MIRKSLEMLE LGLSEAQVMM ALSNHLNAVE SEKQKLRAQV RRLCQENQWL
RDELANTQQK LQKSEQSVAQ LEEEKKHLEF MNQLKKYDDD ISPSEDKDTD STKEPLDDLF
PNDEDDPGQG IQQQHSSAAA AAQQGGYEIP ARLRTLHNLV IQYASQGRYE VAVPLCKQAL
EDLEKTSGHD HPDVATMLNI LALVYRDQNK YKDAANLLND ALAIREKTLG KDHPAVAATL
NNLAVLYGKR GKYKEAEPLC KRALEIREKV LGKDHPDVAK QLNNLALLCQ NQGKYEEVEY
YYQRALDIYQ TKLGPDDPNV AKTKNNLASC YLKQGKFKQA ETLYKEILTR AHEREFGSVD
DENKPIWMHA EEREECKGKQ KDGTSFGEYG GWYKACKVDS PTVTTTLKNL GALYRRQGKF
EAAETLEEAA MRSRKQGLDN AHKQRVAEVL NDPENTEKRR SRESLNVDVV KYESGPDGGE
EVSMSVEWNG VSTLCGVLQQ QPQSPHSFHT AAVLRFLRVF IFFLAHPKLV
//