ID   KLC1_PONAB              Reviewed;         560 AA.
AC   Q5R581;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 3.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Kinesin light chain 1;
DE            Short=KLC 1;
GN   Name=KLC1; Synonyms=KNS2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Kinesin is a microtubule-associated force-producing protein
CC       that may play a role in organelle transport. The light chain may
CC       function in coupling of cargo to the heavy chain or in the modulation
CC       of its ATPase activity (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two light
CC       chains. Interacts with SPAG9. Interacts with ATCAY; may link
CC       mitochondria to KLC1 and regulate mitochondria localization into neuron
CC       projections. Interacts (via TPR repeats) with TOR1A; the interaction
CC       associates TOR1A with the kinesin oligomeric complex. Interacts with
CC       BORCS5. Interacts with MAPK8IP3/JIP3 and NTRK2/TRKB; interaction with
CC       NTRK2/TRKB is mediated by MAPK8IP3/JIP3 (By similarity).
CC       {ECO:0000250|UniProtKB:P37285, ECO:0000250|UniProtKB:Q07866}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, growth cone {ECO:0000250}.
CC       Cytoplasmic vesicle {ECO:0000250}. Cytoplasm, cytoskeleton
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the kinesin light chain family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; CR860983; CAH93085.1; -; mRNA.
DR   RefSeq; NP_001126827.1; NM_001133355.1.
DR   AlphaFoldDB; Q5R581; -.
DR   SMR; Q5R581; -.
DR   STRING; 9601.ENSPPYP00000007016; -.
DR   GeneID; 100173833; -.
DR   KEGG; pon:100173833; -.
DR   CTD; 3831; -.
DR   eggNOG; KOG1840; Eukaryota.
DR   InParanoid; Q5R581; -.
DR   OrthoDB; 511880at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR   GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; -; 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   Pfam; PF13176; TPR_7; 1.
DR   PRINTS; PR00381; KINESINLIGHT.
DR   SMART; SM00028; TPR; 5.
DR   SUPFAM; SSF48452; SSF48452; 2.
DR   PROSITE; PS01160; KINESIN_LIGHT; 4.
DR   PROSITE; PS50005; TPR; 6.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   2: Evidence at transcript level;
KW   Cell projection; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW   Microtubule; Motor protein; Phosphoprotein; Reference proteome; Repeat;
KW   TPR repeat.
FT   CHAIN           1..560
FT                   /note="Kinesin light chain 1"
FT                   /id="PRO_0000234299"
FT   REPEAT          213..246
FT                   /note="TPR 1"
FT   REPEAT          255..288
FT                   /note="TPR 2"
FT   REPEAT          297..330
FT                   /note="TPR 3"
FT   REPEAT          339..372
FT                   /note="TPR 4"
FT   REPEAT          381..414
FT                   /note="TPR 5"
FT   REPEAT          464..497
FT                   /note="TPR 6"
FT   REGION          155..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          31..99
FT                   /evidence="ECO:0000255"
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"
FT   MOD_RES         162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P37285"
FT   MOD_RES         449
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O88447"
FT   MOD_RES         460
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88447"
FT   MOD_RES         521
FT                   /note="Phosphoserine; by AMPK"
FT                   /evidence="ECO:0000250|UniProtKB:Q07866"
FT   MOD_RES         524
FT                   /note="Phosphoserine; by AMPK"
FT                   /evidence="ECO:0000250|UniProtKB:Q07866"
SQ   SEQUENCE   560 AA;  63888 MW;  410537162C2F8437 CRC64;
     MYDNMSTMVY IKEDKLEKLT QDEIISKTKQ VIQGLEALKN EHNSILQSLL ETLKCLKKDD
     ESNLVEEKSN MIRKSLEMLE LGLSEAQVMM ALSNHLNAVE SEKQKLRAQV RRLCQENQWL
     RDELANTQQK LQKSEQSVAQ LEEEKKHLEF MNQLKKYDDD ISPSEDKDTD STKEPLDDLF
     PNDEDDPGQG IQQQHSSAAA AAQQGDYEIP ARLRTLHNLV IQYASQGRYE VAVPLCKQAL
     EDLEKTSGHD HPDVATMLNI LALVYRDQNK YKDAANLLND ALAIREKTLG KDHPAVAATL
     NNLAVLYGKR GKYKEAEPLC KRALEIREKV LGKDHPDVAK QLNNLALLCQ NQGKYEEVEY
     YYQRALEIYQ TKLGPDDPNV AKTKNNLASC YLKQGKFKQA ETLYKEILTR AHEREFGSVD
     DENKPIWMHA EEREECKGKQ KDGTSFGEYG GWYKACKVDS PTVTTTLKNL GALYRRQGKF
     EAAETLEEAA MRSRKQGLDN VHKQRVAEVL NDPENMEKRR SRESLNVDVV KYESGPDGGE
     EVSMSVEWNG MRKMKLGLVK