LURA1_MOUSE
ID LURA1_MOUSE Reviewed; 239 AA.
AC Q9D6I9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Leucine rich adaptor protein 1;
DE AltName: Full=Leucine repeat adapter protein 35A;
GN Name=Lurap1; Synonyms=Lrap35a, Lrp35a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-126, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. In concert with MYO18A and
CC 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 (By
CC similarity). {ECO:0000250|UniProtKB:D4A8G3}.
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. Interacts with CDC42BPA and CDC42BPB.
CC {ECO:0000250|UniProtKB:D4A8G3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96LR2}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:D4A8G3}.
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DR EMBL; AK013564; BAB28908.1; -; mRNA.
DR CCDS; CCDS51275.1; -.
DR RefSeq; NP_080823.1; NM_026547.1.
DR AlphaFoldDB; Q9D6I9; -.
DR SMR; Q9D6I9; -.
DR BioGRID; 212642; 4.
DR STRING; 10090.ENSMUSP00000030469; -.
DR iPTMnet; Q9D6I9; -.
DR PhosphoSitePlus; Q9D6I9; -.
DR MaxQB; Q9D6I9; -.
DR PaxDb; Q9D6I9; -.
DR PRIDE; Q9D6I9; -.
DR ProteomicsDB; 295729; -.
DR Antibodypedia; 32773; 65 antibodies from 14 providers.
DR Ensembl; ENSMUST00000030469; ENSMUSP00000030469; ENSMUSG00000028701.
DR GeneID; 68075; -.
DR KEGG; mmu:68075; -.
DR UCSC; uc008ugg.2; mouse.
DR CTD; 541468; -.
DR MGI; MGI:1915325; Lurap1.
DR VEuPathDB; HostDB:ENSMUSG00000028701; -.
DR eggNOG; ENOG502QQFH; Eukaryota.
DR GeneTree; ENSGT00530000063790; -.
DR HOGENOM; CLU_066656_1_0_1; -.
DR InParanoid; Q9D6I9; -.
DR OMA; PCPEMDW; -.
DR OrthoDB; 1385244at2759; -.
DR PhylomeDB; Q9D6I9; -.
DR TreeFam; TF332089; -.
DR BioGRID-ORCS; 68075; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Lurap1; mouse.
DR PRO; PR:Q9D6I9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D6I9; protein.
DR Bgee; ENSMUSG00000028701; Expressed in spermatid and 95 other tissues.
DR ExpressionAtlas; Q9D6I9; baseline and differential.
DR Genevisible; Q9D6I9; MM.
DR GO; GO:0042641; C:actomyosin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031032; P:actomyosin structure organization; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
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_0000271079"
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 105..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A8G3"
SQ SEQUENCE 239 AA; 25830 MW; 5BFF6F204DCFB2D1 CRC64;
MEGTAESQTP DLRDVEGKVG RKIPEGLLRG LRGECELGTS GDVLLPGAPS TGHGLGDKIM
ALRMELAYLR AIDVKILQQL VTLNEGIEAV RWLLEERGTL TSHCSSLTSS QYSLTGGSPG
RSRRGSWDSL PDTSSTDRLD SVSIGSFLDT VTPRELDEQG LPGPSCPEID WAKVIPTEDR
ARTEVDMTST KLGSLTATWK LPGDGLQCGP PEPSEDGNAN QGFEAHWYWG QCQDDVTFL
