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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
 
 
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