LPP_MOUSE
ID LPP_MOUSE Reviewed; 613 AA.
AC Q8BFW7; Q5U407; Q8BHI1; Q8BKI0; Q8BKN2; Q8BLF4; Q8BLG3; Q8C101;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Lipoma-preferred partner homolog;
GN Name=Lpp;
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] (ISOFORMS 1; 2; 3; 4 AND 5).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Aorta, Embryo, Eye, Head, Ovary, Spinal ganglion, Testis, Thymus,
RC and Vein;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C3H/He; TISSUE=Mesenchymal stem cell;
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 [3]
RP NEOPLASTIC TRANSFORMATION.
RX PubMed=9696033; DOI=10.1038/sj.onc.1201952;
RA Fedele M., Berlingieri M.T., Scala S., Chiariotti L., Viglietto G.,
RA Rippel V., Bullerdiek J., Santoro M., Fusco A.;
RT "Truncated and chimeric HMGI-C genes induce neoplastic transformation of
RT NIH3T3 murine fibroblasts.";
RL Oncogene 17:413-418(1998).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-245, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-302, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-245, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-109, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-250, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May play a structural role at sites of cell adhesion in
CC maintaining cell shape and motility. In addition to these structural
CC functions, it may also be implicated in signaling events and activation
CC of gene transcription. May be involved in signal transduction from cell
CC adhesion sites to the nucleus allowing successful integration of
CC signals arising from soluble factors and cell-cell adhesion sites. Also
CC suggested to serve as a scaffold protein upon which distinct protein
CC complexes are assembled in the cytoplasm and in the nucleus (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with VASP, with PDZ domains of SCRIB and with
CC ACTN1/alpha-actinin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cell junction {ECO:0000250}. Note=Found in the nucleus, in the
CC cytoplasm and at cell adhesion sites. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8BFW7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BFW7-2; Sequence=VSP_016353, VSP_016354;
CC Name=3;
CC IsoId=Q8BFW7-3; Sequence=VSP_016351, VSP_016353, VSP_016354;
CC Name=4;
CC IsoId=Q8BFW7-4; Sequence=VSP_016350, VSP_016352;
CC Name=5;
CC IsoId=Q8BFW7-5; Sequence=VSP_016355, VSP_016356;
CC -!- MISCELLANEOUS: Fusion protein carrying the DNA-binding domains of
CC HMGA2/HMGIC and the LIM domain of LPP causes malignant transformation
CC of NIH3T3 cells.
CC -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
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DR EMBL; AK029335; BAC26401.1; -; mRNA.
DR EMBL; AK029567; BAC26516.1; -; mRNA.
DR EMBL; AK040643; BAC30654.1; -; mRNA.
DR EMBL; AK045288; BAC32298.1; -; mRNA.
DR EMBL; AK045341; BAC32316.1; -; mRNA.
DR EMBL; AK051345; BAC34608.1; -; mRNA.
DR EMBL; AK051937; BAC34815.1; -; mRNA.
DR EMBL; AK054550; BAC35821.1; -; mRNA.
DR EMBL; AK076989; BAC36552.1; -; mRNA.
DR EMBL; AK169780; BAE41362.1; -; mRNA.
DR EMBL; BC085321; AAH85321.1; -; mRNA.
DR CCDS; CCDS28083.1; -. [Q8BFW7-1]
DR CCDS; CCDS49807.1; -. [Q8BFW7-4]
DR RefSeq; NP_001139424.1; NM_001145952.1. [Q8BFW7-1]
DR RefSeq; NP_001139426.1; NM_001145954.1. [Q8BFW7-4]
DR RefSeq; NP_848780.3; NM_178665.5. [Q8BFW7-1]
DR RefSeq; XP_006522020.1; XM_006521957.3. [Q8BFW7-1]
DR AlphaFoldDB; Q8BFW7; -.
DR SMR; Q8BFW7; -.
DR BioGRID; 229132; 5.
DR IntAct; Q8BFW7; 2.
DR MINT; Q8BFW7; -.
DR STRING; 10090.ENSMUSP00000036304; -.
DR iPTMnet; Q8BFW7; -.
DR PhosphoSitePlus; Q8BFW7; -.
DR EPD; Q8BFW7; -.
DR jPOST; Q8BFW7; -.
DR MaxQB; Q8BFW7; -.
DR PaxDb; Q8BFW7; -.
DR PeptideAtlas; Q8BFW7; -.
DR PRIDE; Q8BFW7; -.
DR ProteomicsDB; 252486; -. [Q8BFW7-1]
DR ProteomicsDB; 252487; -. [Q8BFW7-2]
DR ProteomicsDB; 252488; -. [Q8BFW7-3]
DR ProteomicsDB; 252489; -. [Q8BFW7-4]
DR ProteomicsDB; 252490; -. [Q8BFW7-5]
DR Antibodypedia; 2772; 272 antibodies from 41 providers.
DR DNASU; 210126; -.
DR Ensembl; ENSMUST00000038053; ENSMUSP00000036304; ENSMUSG00000033306. [Q8BFW7-1]
DR Ensembl; ENSMUST00000078988; ENSMUSP00000078005; ENSMUSG00000033306. [Q8BFW7-1]
DR Ensembl; ENSMUST00000115314; ENSMUSP00000110969; ENSMUSG00000033306. [Q8BFW7-4]
DR GeneID; 210126; -.
DR KEGG; mmu:210126; -.
DR UCSC; uc007yub.2; mouse. [Q8BFW7-2]
DR UCSC; uc007yuc.2; mouse. [Q8BFW7-3]
DR UCSC; uc007yud.2; mouse. [Q8BFW7-5]
DR UCSC; uc007yue.2; mouse. [Q8BFW7-1]
DR UCSC; uc007yuh.2; mouse. [Q8BFW7-4]
DR CTD; 4026; -.
DR MGI; MGI:2441849; Lpp.
DR VEuPathDB; HostDB:ENSMUSG00000033306; -.
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000156022; -.
DR HOGENOM; CLU_001357_10_0_1; -.
DR InParanoid; Q8BFW7; -.
DR OMA; FNPYKQM; -.
DR OrthoDB; 483341at2759; -.
DR PhylomeDB; Q8BFW7; -.
DR TreeFam; TF320310; -.
DR BioGRID-ORCS; 210126; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Lpp; mouse.
DR PRO; PR:Q8BFW7; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BFW7; protein.
DR Bgee; ENSMUSG00000033306; Expressed in ascending aorta and 245 other tissues.
DR ExpressionAtlas; Q8BFW7; baseline and differential.
DR Genevisible; Q8BFW7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR InterPro; IPR028771; LPP.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24207:SF0; PTHR24207:SF0; 1.
DR Pfam; PF00412; LIM; 3.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Cell adhesion; Cell junction;
KW Cytoplasm; Isopeptide bond; LIM domain; Metal-binding; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc.
FT CHAIN 1..613
FT /note="Lipoma-preferred partner homolog"
FT /id="PRO_0000075833"
FT DOMAIN 415..474
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 475..535
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 536..604
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..96
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XI07"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XI07"
FT MOD_RES 245
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455,
FT ECO:0007744|PubMed:19131326"
FT MOD_RES 250
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 302
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT CROSSLNK 328
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q93052"
FT VAR_SEQ 1..125
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016350"
FT VAR_SEQ 102
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016351"
FT VAR_SEQ 126..144
FT /note="TSILADLECSSPYKPRPPQ -> MELLGKVGACLKRSTGTLK (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016352"
FT VAR_SEQ 145..152
FT /note="GSASSIAS -> VGTSHSAA (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016353"
FT VAR_SEQ 153..613
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016354"
FT VAR_SEQ 373..378
FT /note="GGYPGP -> VRNLLT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016355"
FT VAR_SEQ 379..613
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016356"
FT CONFLICT 29
FT /note="F -> V (in Ref. 1; BAC32298)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="I -> T (in Ref. 1; BAC34815)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="P -> S (in Ref. 2; AAH85321)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="E -> D (in Ref. 1; BAC26401)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="E -> A (in Ref. 1; BAC34608)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="C -> R (in Ref. 2; AAH85321)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 65891 MW; E34BE2EF2A3B7126 CRC64;
MSHPSWLPPK STGEPLGHVP ARMETTHSFG NPSISVSTQQ PPKKYAPVVA PKPKYNPYKQ
PGGEGDLLPP PPPPLEDPGT IPPGPGHFPP PPPLDEGAFK VQQGNPGGKT LEERRSSLDA
EIDSLTSILA DLECSSPYKP RPPQGSASSI ASPPVSTPVT GHKRMVIPQQ PPLTATKKSA
TKPQPAPQAA PIPVTPIGTL KPQPQPVPAS YTTASTSSRP TFNVQVKSAQ PSPHYMAGPS
SGQIYGPGPR GYNNQPVPVS GQCPPPPTCV GTDYAYIPPS GHPPESGYGY TSNQGRYYEP
YYAAGPSYGG RSEGDTAYGQ QVQPNTWKRE AAYAPPASGN QNHPGMYPVS GPKKTYITDP
VSAPCAPPLQ PKGGYPGPMG PPSIPPSFRP EDELEHLTKK MLYDMENPPA DDYFGRCARC
GENVVGEGTG CTAMDQVFHV DCFTCIVCDV KLRGQPFYAV EKKAYCEPCY INTLEQCSVC
SKPIMERILR ATGKAYHPHC FTCVMCHRSL DGIPFTVDAC GLIHCIEDFH KKFAPRCSVC
KEPIMPAPGQ EETVRIVALD RDFHVHCYRC EDCGGLLSEG DNQGCYPLDG HILCKTCNSA
RIRVLTAKAS TDL
