LURA1_RAT
ID LURA1_RAT Reviewed; 239 AA.
AC D4A8G3;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Leucine rich adaptor protein 1;
DE AltName: Full=Leucine repeat adapter protein 35A;
GN Name=Lurap1; Synonyms=Lrap35a, Lrp35a;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH
RP CDC42BPA/CDC42BPB AND MYO18A, AND PHOSPHORYLATION.
RX PubMed=18854160; DOI=10.1016/j.cell.2008.09.018;
RA Tan I., Yong J., Dong J.M., Lim L., Leung T.;
RT "A tripartite complex containing MRCK modulates lamellar actomyosin
RT retrograde flow.";
RL Cell 135:123-136(2008).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-129, 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).
RN [4]
RP INTERACTION WITH CDC42BPA AND CDC42BPB.
RC TISSUE=Brain;
RX PubMed=25107909; DOI=10.1074/jbc.m114.588079;
RA Lee I.C., Leung T., Tan I.;
RT "Adaptor protein LRAP25 mediates myotonic dystrophy kinase-related Cdc42-
RT binding kinase (MRCK) regulation of LIMK1 protein in lamellipodial F-actin
RT dynamics.";
RL J. Biol. Chem. 289:26989-27003(2014).
CC -!- FUNCTION: Acts as an activator of the canonical NF-kappa-B pathway and
CC drive the production of pro-inflammatory cytokines. Promotes the
CC antigen (Ag)-presenting and priming function of dendritic cells via the
CC canonical NF-kappa-B pathway (By similarity). In concert with MYO18A
CC and CDC42BPA/CDC42BPB, is involved in modulating lamellar actomyosin
CC retrograde flow that is crucial to cell protrusion and migration.
CC Activates CDC42BPA/CDC42BPB and targets it to actomyosin through its
CC interaction with MYO18A, leading to MYL9/MLC2 phosphorylation and
CC MYH9/MYH10-dependent actomyosin assembly in the lamella. {ECO:0000250,
CC ECO:0000269|PubMed:18854160}.
CC -!- SUBUNIT: Forms a tripartite complex with CDC42BPA/CDC42BPB and MYO18A
CC acting as an adapter connecting both. Its binding to CDC42BPA/CDC42BPB
CC results in their activation by abolition of their negative
CC autoregulation (PubMed:18854160). Interacts with CDC42BPA and CDC42BPB
CC (PubMed:25107909). {ECO:0000269|PubMed:18854160,
CC ECO:0000269|PubMed:25107909}.
CC -!- INTERACTION:
CC D4A8G3; O54874: Cdc42bpa; NbExp=8; IntAct=EBI-2015467, EBI-689253;
CC D4A8G3; Q7TT49: Cdc42bpb; NbExp=4; IntAct=EBI-2015467, EBI-692673;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96LR2}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:18854160}.
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DR EMBL; CH474008; EDL90291.1; -; Genomic_DNA.
DR RefSeq; NP_001102733.1; NM_001109263.1.
DR AlphaFoldDB; D4A8G3; -.
DR SMR; D4A8G3; -.
DR IntAct; D4A8G3; 3.
DR STRING; 10116.ENSRNOP00000030673; -.
DR iPTMnet; D4A8G3; -.
DR PhosphoSitePlus; D4A8G3; -.
DR PaxDb; D4A8G3; -.
DR PeptideAtlas; D4A8G3; -.
DR PRIDE; D4A8G3; -.
DR GeneID; 500527; -.
DR KEGG; rno:500527; -.
DR UCSC; RGD:1566001; rat.
DR CTD; 541468; -.
DR RGD; 1566001; Lurap1.
DR eggNOG; ENOG502QQFH; Eukaryota.
DR HOGENOM; CLU_066656_1_0_1; -.
DR InParanoid; D4A8G3; -.
DR OMA; PCPEMDW; -.
DR OrthoDB; 1385244at2759; -.
DR PhylomeDB; D4A8G3; -.
DR TreeFam; TF332089; -.
DR PRO; PR:D4A8G3; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Proteomes; UP000234681; Chromosome 5.
DR Bgee; ENSRNOG00000023459; Expressed in cerebellum and 18 other tissues.
DR Genevisible; D4A8G3; RN.
DR GO; GO:0042641; C:actomyosin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031032; P:actomyosin structure organization; IMP:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR InterPro; IPR039499; LURA1/LRA25.
DR InterPro; IPR037443; LURAP1.
DR PANTHER; PTHR33767; PTHR33767; 1.
DR Pfam; PF14854; LURAP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Leucine-rich repeat; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..239
FT /note="Leucine rich adaptor protein 1"
FT /id="PRO_0000414028"
FT REPEAT 55..83
FT /note="LRR 1"
FT /evidence="ECO:0000250"
FT REPEAT 93..114
FT /note="LRR 2"
FT /evidence="ECO:0000250"
FT REGION 107..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D6I9"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 239 AA; 25891 MW; 68A1110A31C7C4D9 CRC64;
MEGTAESQTP DLRDVEGKVG RKTPEGLLRG LRGECDLGTS GDVLLPGASS TGHGLGDKIM
ALRMELAYLR AIDVKILQQL VTLNEGIEAV RWLLEERGTL TSHCSSLTSS QYSLTGGSPE
RSRRGSWDSL PDTSSTDRLD SVSIGSFLDT VAPRELDEQG HPGPSCPEID WAKVIPSEDR
ARTEVDMTST KLGSLTATWK LPGDGLQCGP PEPSEDDSAK QGFEAHWYWG QCQDDVTFL
