KLC4_RAT
ID KLC4_RAT Reviewed; 619 AA.
AC Q5PQM2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Kinesin light chain 4;
DE Short=KLC 4;
DE AltName: Full=Kinesin-like protein 8;
GN Name=Klc4; Synonyms=Knsl8;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-565; SER-566 AND SER-590, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the kinesin light chain family. {ECO:0000305}.
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DR EMBL; BC087116; AAH87116.1; -; mRNA.
DR RefSeq; NP_001009601.1; NM_001009601.1.
DR RefSeq; XP_006244578.1; XM_006244516.3.
DR RefSeq; XP_006244579.1; XM_006244517.3.
DR AlphaFoldDB; Q5PQM2; -.
DR SMR; Q5PQM2; -.
DR IntAct; Q5PQM2; 3.
DR STRING; 10116.ENSRNOP00000038363; -.
DR iPTMnet; Q5PQM2; -.
DR PhosphoSitePlus; Q5PQM2; -.
DR jPOST; Q5PQM2; -.
DR PaxDb; Q5PQM2; -.
DR PRIDE; Q5PQM2; -.
DR Ensembl; ENSRNOT00000031625; ENSRNOP00000038363; ENSRNOG00000018168.
DR GeneID; 316226; -.
DR KEGG; rno:316226; -.
DR UCSC; RGD:1306555; rat.
DR CTD; 89953; -.
DR RGD; 1306555; Klc4.
DR eggNOG; KOG1840; Eukaryota.
DR GeneTree; ENSGT00940000161323; -.
DR InParanoid; Q5PQM2; -.
DR OMA; LQHEGHE; -.
DR OrthoDB; 511880at2759; -.
DR PhylomeDB; Q5PQM2; -.
DR TreeFam; TF314010; -.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-5625970; RHO GTPases activate KTN1.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-983189; Kinesins.
DR PRO; PR:Q5PQM2; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000018168; Expressed in jejunum and 19 other tissues.
DR Genevisible; Q5PQM2; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0019894; F:kinesin binding; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
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 PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS01160; KINESIN_LIGHT; 3.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NSK0"
FT CHAIN 2..619
FT /note="Kinesin light chain 4"
FT /id="PRO_0000384582"
FT REPEAT 55..88
FT /note="TPR 1"
FT REPEAT 211..244
FT /note="TPR 2"
FT REPEAT 253..286
FT /note="TPR 3"
FT REPEAT 295..328
FT /note="TPR 4"
FT REPEAT 337..370
FT /note="TPR 5"
FT REPEAT 379..412
FT /note="TPR 6"
FT REPEAT 464..497
FT /note="TPR 7"
FT REGION 156..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..150
FT /evidence="ECO:0000255"
FT COMPBIAS 156..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSK0"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBS5"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSK0"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 612
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSK0"
SQ SEQUENCE 619 AA; 68964 MW; 6873D2D80C174BB2 CRC64;
MSGLVLGQRD EPAGHRLSQE EILGSTRLVS QGLESLHSEH QAVLQSLSHT IECLQQGGHE
EGLVHEKARQ LRRSMENIEL GLSEAQVMLA LASHLSTVES EKQKLRAQVR RLCQENQWLR
DELAGTQQRL QRSEQAVAQL EEEKKHLEFL RQLRQYDEDG HSMEEKEGDA SKDSLDDLFP
NEEEEDSSND LSRGQGAAAA QQGGYEIPAR LRTLHNLVIQ YAAQGRYEVA VPLCKQALED
LERTSGRGHP DVATMLNILA LVYRDQNKYK EAAHLLNDAL SIRESTLGRD HPAVAATLNN
LAVLYGKRGK YKEAEPLCQR ALEIREKVLG TDHPDVAKQL NNLALLCQNQ GKYEAVERYY
QRALAIYERQ LGPDNPNVAR TKNNLASCYL KQGKYSEAET LYKEILTRAH VQEFGSVDDD
HKPIWMHAEE REEMSRSRSR ESGTPYAEYG GWYKACRVSS PTVNTTLRNL GALYRRQGKL
EAAETLEECA LRSRKQGTDP ISQTKVAELL GEGDGRKTMQ EGPGDSVKFE GGEDASVAVE
WSGDGSGTLQ RSGSLGKIRD VLRRSSELLV RKLQGTEPRP SSSNMKRAAS LNYLNQPNAA
PLQTSRGLSA STVDLSSSS