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Database: UniProt
Entry: G1QN58_NOMLE
LinkDB: G1QN58_NOMLE
Original site: G1QN58_NOMLE 
ID   G1QN58_NOMLE            Unreviewed;       404 AA.
AC   G1QN58;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
GN   Name=KLC3 {ECO:0000313|Ensembl:ENSNLEP00000002374.2};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000002374.2, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000002374.2, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000002374.2}
RP   IDENTIFICATION.
RG   Ensembl;
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       Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the kinesin light chain family.
CC       {ECO:0000256|ARBA:ARBA00009622, ECO:0000256|RuleBase:RU367020}.
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DR   EMBL; ADFV01101950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01101951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01101952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01101953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1QN58; -.
DR   Ensembl; ENSNLET00000002503.2; ENSNLEP00000002374.2; ENSNLEG00000001990.2.
DR   eggNOG; KOG1840; Eukaryota.
DR   GeneTree; ENSGT00940000162356; -.
DR   HOGENOM; CLU_019953_2_0_1; -.
DR   TreeFam; TF314010; -.
DR   Proteomes; UP000001073; Chromosome 17.
DR   GO; GO:0005871; C:kinesin complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-UniRule.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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:SF1; KINESIN LIGHT CHAIN 3; 1.
DR   Pfam; PF13424; TPR_12; 2.
DR   PRINTS; PR00381; KINESINLIGHT.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 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   Differentiation {ECO:0000256|ARBA:ARBA00022871};
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:UP000001073};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Spermatogenesis {ECO:0000256|ARBA:ARBA00022871};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}.
FT   REPEAT          193..226
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          235..268
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          98..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          39..94
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        101..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   404 AA;  44669 MW;  D575CB00D99AD901 CRC64;
     MPPVPSWGSP GSGGLTGVEP TSTWDPHPGQ VLLALSAHVG ALEAEKQRLR SQARRLAQEN
     VWLREELEET QRRLRASEEA VAQLEEEKRH LEFLGQLRQY DPPAENQQSE SPPRRDSLAS
     LFPSEEEERK GPEAAGAAAA QQGGYEIPAR LRTLHNLVIQ YAGQGRYEVA VPLCRQALED
     LERSSGHCHP DVATMLNILA LVYRDQNKYK EATDLLHDAL QIREQTLGPE HPAVAATLNN
     LAVLYGKRGR YREAEPLCQR ALEIREKVLG ADHPDVAKQL NNLALLCQNQ GKFEDVERHY
     ARALSIYEAL GGPHDPNVAK TKNNLASAYL KQNKYQQAEE LYKEILHKED LPAPLGAPNT
     GTAGDAEQTL RRSSSLSKIR ESIRRGSEKL VSRLRGEGAA GAAG
//
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