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Database: UniProt
Entry: A0A087QQY0_APTFO
LinkDB: A0A087QQY0_APTFO
Original site: A0A087QQY0_APTFO 
ID   A0A087QQY0_APTFO        Unreviewed;       534 AA.
AC   A0A087QQY0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
DE   Flags: Fragment;
GN   ORFNames=AS27_00443 {ECO:0000313|EMBL:KFM03634.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM03634.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM03634.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM03634.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KL225818; KFM03634.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087QQY0; -.
DR   STRING; 9233.A0A087QQY0; -.
DR   Proteomes; UP000053286; 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   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:SF8; KINESIN LIGHT CHAIN; 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; 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:UP000053286};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}.
FT   REPEAT          251..284
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          293..326
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          152..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          85..147
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        152..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         534
FT                   /evidence="ECO:0000313|EMBL:KFM03634.1"
SQ   SEQUENCE   534 AA;  60637 MW;  46E0C6C355DEEAEE CRC64;
     MSTMVYPREE KLDKLSQEEI ISNTKLVMQG LEALKNEHNS ILHSLLETIK CLKKDEEANL
     VHEKSNLLRK SVEMIELGLG EAQVMMALSN HLNAVESEKQ KLRAQVRRLC QENQWLRDEL
     ANTQQKLQRS EQTVAQLEEE KKHLEFMNQL KKYDEDVSPS EEKEGDSAKD SLDDLFPNEE
     EEHGPGLPHQ HSSAVAAAQQ GGYEIPARLR TLHNLVIQYA SQGRYEVAVP LCKQALEDLE
     KTSGHDHPDV ATMLNILALV YRDQNKYKEA AHLLNDALSI REKTLGKDHP AVAATLNNLA
     VLYGKRGKYK EAEPLCKRAL EIREKVLGKD HPDVAKQLNN LALLCQNQGK YDEVEYYYCR
     ALEIYESCLG PDDPNVAKTK NNLASCYLKQ GKYKDAEVLY KEILTRAHVK EFGSVDDEHK
     PIWMHAEERE EMSKSKHRDS APYAEYGGWY KACKVSSPTV NTTLRNLGAL YRRQGKLEAA
     ETLEECAVRS RRQGIDPINQ TKVVEILKEG DGTERRRSLG GSVKYENATD GSEE
//
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