ID A0A1I8GHU6_9PLAT Unreviewed; 500 AA.
AC A0A1I8GHU6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0002062-snap-gene-0.12-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0002062-snap-gene-0.12-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A1I8GHU6; -.
DR WBParaSite; maker-uti_cns_0002062-snap-gene-0.12-mRNA-1; maker-uti_cns_0002062-snap-gene-0.12-mRNA-1; maker-uti_cns_0002062-snap-gene-0.12.
DR Proteomes; UP000095280; 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; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45783; KINESIN LIGHT CHAIN; 1.
DR PANTHER; PTHR45783:SF3; KINESIN LIGHT CHAIN; 1.
DR Pfam; PF13424; TPR_12; 2.
DR Pfam; PF13176; TPR_7; 1.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 1.
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 Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU367020};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175,
KW ECO:0000256|RuleBase:RU367020}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT REPEAT 411..444
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 500 AA; 54485 MW; 1E429F2E85930111 CRC64;
MATSVATMAT GQHAQQSADS GSASAAAAES SVTEDVPALE NIVQQARSVM STLSAFRSSQ
AETLQRMRDR AGSADADSAG DEERELCDEK APRLGELVEK LELGIDEGEL LVAVSRHIQQ
LDSDKMKMRT QVRRLVQENA WLREELTAVQ GRLHERESAL VALEEERNHL KFMAEMRQID
PSSAAASGGA GPASTGKDDD TVSTAGDDDL LLGDAGGSPS HGGAGGSNAL AAGGGGYEVP
ARLRTLHNLV IQYASQGRYE VAVPLCKQAL DDLERTSGHD HPDVATMLNI LALVYRDQGK
YRESATLLND ALVIREKTLG PEHPAVAATL NNLAVLYGKR GKYREAEPLC ERALAIREKV
LGPAHPDVAK QLNNLALLCQ NQGKYEQVEK YYQRALNIYV QAQGPDDPNV AKTKNNLASA
YLKQGKYRQA EQLYKEVLSR AHERGESGRS GQPIWMLAEA REESRRTGQQ QQQQQQQQQH
LDVFCKEDQA IIGTTLRNLS
//
