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Database: UniProt
Entry: V8NQ85_OPHHA
LinkDB: V8NQ85_OPHHA
Original site: V8NQ85_OPHHA 
ID   V8NQ85_OPHHA            Unreviewed;       764 AA.
AC   V8NQ85;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
DE   Flags: Fragment;
GN   Name=KLC1 {ECO:0000313|EMBL:ETE64429.1};
GN   ORFNames=L345_09810 {ECO:0000313|EMBL:ETE64429.1};
OS   Ophiophagus hannah (King cobra) (Naja hannah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX   NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE64429.1, ECO:0000313|Proteomes:UP000018936};
RN   [1] {ECO:0000313|EMBL:ETE64429.1, ECO:0000313|Proteomes:UP000018936}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Blood {ECO:0000313|EMBL:ETE64429.1};
RX   PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA   Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA   McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA   Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA   de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA   Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA   Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA   Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT   "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT   snake venom system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(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   -!- SIMILARITY: Belongs to the kinesin light chain family.
CC       {ECO:0000256|ARBA:ARBA00009622, ECO:0000256|RuleBase:RU367020}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETE64429.1}.
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DR   EMBL; AZIM01002262; ETE64429.1; -; Genomic_DNA.
DR   AlphaFoldDB; V8NQ85; -.
DR   Proteomes; UP000018936; Unassembled WGS sequence.
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   GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IEA:InterPro.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR018796; COA8.
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; PF10231; COA8; 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   PROSITE; PS01160; KINESIN_LIGHT; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000018936};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}.
FT   REPEAT          433..466
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          34..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          328..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          705..764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          261..323
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        328..350
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..756
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ETE64429.1"
SQ   SEQUENCE   764 AA;  87056 MW;  AD54487CC677481A CRC64;
     MAALVRSRGF LHSLSGCPYL VSSCFGCRFL SSSVSGGSSR GEEPEKKNAP SPPKRKVSCF
     HPPSDSCCDW IGPPDQYSNL RPVIFYVPKH ETPLERRLRE LRQETQAWNQ EFWTNQNLSF
     RKKASLTVEE MAEFYKDFLS KNLKKNVYYN REWYKRNFAI TFLMGQVAFE KAMYDNMSTM
     VYLKEDKLEK LTQDEIISKT KQVIQGLEAL KNEHNSILQS LLETLKCLKK DDETNLVEEK
     SNMIRKSLEM LELGLSEAQV MMALSNHLNA VESEKQKLRA QVRRLCQENQ WLRDELANTQ
     QKLQKSEQSV AQLEEEKKHL EFMNQLKKYD DDISPSEDKD ADSAKEPLDD LFPNDEDDQG
     QGSRYEVAVP LCKQALEDLE KTSGHDHPDV ATMLNILALV YRDQNKYKDA ANLLNDALAI
     REKTLGKDHP AVAATLNNLA VLYGKRGKYK EAEPLCKRAL EIREKVLGKD HPDVAKQLNN
     LALLCQNQGK YEEVEYYYQR ALEIYQTKLG PDDPNVAKTK NNLASCYLKQ GKFKQAETLY
     KEILTRAHER EFGSVDDENK PIWMHAEERE ECKGKQKDGM TFGEYGGWYK ACKVDSPTVT
     TTLKNLGALY RRQGKFEAAE TLEEAAMRSR KQASTITQKV LNDPESIERR QSRESLNIDV
     VKYESGPDGG EEVSMSLEWN GDGTGSLKRS GSFSKLRASI RRSSEKLVRK LKGGSSRESP
     GMKRASSMNI LNVGGKTTED HFQGRTNCLT DSRAKSVSHT DLAH
//
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