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Protein

Leupaxin

Gene

Lpxn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional coactivator for androgen receptor (AR) and serum response factor (SRF). Contributes to the regulation of cell adhesion, spreading and cell migration and acts as a negative regulator in integrin-mediated cell adhesion events. Suppresses the integrin-induced tyrosine phosphorylation of paxillin (PXN). May play a critical role as an adapter protein in the formation of the adhesion zone in osteoclasts. Negatively regulates B-cell antigen receptor (BCR) signaling.4 Publications

GO - Molecular functioni

  • transcription cofactor activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell adhesion, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Leupaxin
Gene namesi
Name:Lpxn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:2147677. Lpxn.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell junctionfocal adhesion
  • Nucleus
  • Cytoplasmperinuclear region
  • Cell projectionpodosome
  • Cell membrane

  • Note: Shuttles between the cytoplasm and nucleus. Recruited to the cell membrane following B-cell antigen receptor (BCR) cross-linking in B-cells. Enhanced focal adhesion kinase activity (PTK2/FAK) attenuates its nuclear accumulation and limits its ability to enhance serum response factor (SRF)-dependent gene transcription. Targeting to focal adhesions is essential for its tyrosine phosphorylation in response to bombesin (By similarity).By similarity

GO - Cellular componenti

  • cell projection Source: UniProtKB-KW
  • cytoplasm Source: MGI
  • focal adhesion Source: UniProtKB
  • membrane Source: MGI
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • plasma membrane Source: MGI
  • podosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 386386LeupaxinPRO_0000075837Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei19 – 191PhosphoserineBy similarity
Modified residuei22 – 221PhosphotyrosineCombined sources
Modified residuei54 – 541PhosphoserineCombined sources
Modified residuei62 – 621PhosphotyrosineCombined sources
Modified residuei72 – 721Phosphotyrosine; by LYNCombined sources1 Publication
Modified residuei81 – 811PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on tyrosine residues. Phosphorylation on Tyr-72 is important for its inhibitory function. Bombesin stimulates phosphorylation on Tyr-22, Tyr-62 and Tyr-72 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ99N69.
MaxQBiQ99N69.
PaxDbiQ99N69.
PeptideAtlasiQ99N69.
PRIDEiQ99N69.

PTM databases

iPTMnetiQ99N69.
PhosphoSiteiQ99N69.

Expressioni

Tissue specificityi

Expressed in osteoclasts (at protein level). Highly expressed in vascular smooth muscle.2 Publications

Gene expression databases

BgeeiQ99N69.
CleanExiMM_LPXN.
GenevisibleiQ99N69. MM.

Interactioni

Subunit structurei

Interacts with unphosphorylated ITGA4. Interacts with AR and SRF (By similarity). Interacts with PTK2B/PYK2, PTPN22 and PTPN12. Interacts (via LD motif 3) with LYN and the interaction is induced upon B-cell antigen receptor (BCR) activation. Interacts (via LD motif 3) with PTK2/FAK.By similarity4 Publications

Protein-protein interaction databases

BioGridi223241. 3 interactions.
IntActiQ99N69. 1 interaction.
STRINGi10090.ENSMUSP00000025601.

Structurei

3D structure databases

ProteinModelPortaliQ99N69.
SMRiQ99N69. Positions 152-379.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini150 – 20859LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini209 – 26759LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini268 – 32659LIM zinc-binding 3PROSITE-ProRule annotationAdd
BLAST
Domaini327 – 38660LIM zinc-binding 4PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi3 – 1513LD motif 1Add
BLAST
Motifi70 – 8213LD motif 2Add
BLAST
Motifi92 – 10312LD motif 3Add
BLAST

Domaini

The LIM domain 3 is critical for focal adhesion targeting and the suppression of paxillin (PXN) tyrosine phosphorylation. The LIM domain 3 alone or both LIM domains 3 and 4 can mediate interaction with AR.1 Publication

Sequence similaritiesi

Belongs to the paxillin family.Curated
Contains 4 LIM zinc-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiKOG1703. Eukaryota.
ENOG410XRD4. LUCA.
GeneTreeiENSGT00760000118910.
HOGENOMiHOG000018764.
HOVERGENiHBG001512.
InParanoidiQ99N69.
OMAiCKEEIGS.
OrthoDBiEOG70ZZQN.
PhylomeDBiQ99N69.
TreeFamiTF314113.

Family and domain databases

Gene3Di2.10.110.10. 4 hits.
InterProiIPR017305. Tgfb1i1/Leupaxin.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 4 hits.
[Graphical view]
PIRSFiPIRSF037881. Leupaxin. 1 hit.
SMARTiSM00132. LIM. 4 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99N69-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEELDALLEE LERCTFQDSE EYSNPVSCHL DQQSTEESKI PQTPKTLSSQ
60 70 80 90 100
GNTSPLKVQL VYATNIQEPN VYSEVQEPKE SVLPPKTSAA AQLDELMAHL
110 120 130 140 150
SEMQAKVSVK ADTSRKPLPD QQDHKASLDS MLGDLEQELQ DLGIATVPKG
160 170 180 190 200
YCASCQKPIA GKVIHALGQS WHPEHFVCTH CKEELGSSPF FERSGLAYCS
210 220 230 240 250
KDYHRLFSPR CAYCAAPITD KVLTAMNKTW HPEHFFCSHC GEVFGAEGFH
260 270 280 290 300
EKDKKPYCRK DFLAMFSPKC GGCNRPVLEN YLSAMNTVWH PECFVCGDCF
310 320 330 340 350
SSFSSGSFFE LDGRPFCELH YHHRRGTLCH DCGQPITGRC ISAMGHKFHP
360 370 380
EHFVCAFCLT QLPKGIFKEQ NNKTYCEKCF TKLFSQ
Length:386
Mass (Da):43,478
Last modified:October 1, 2002 - v2
Checksum:iAA7EB76AEF5983C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB053936 mRNA. Translation: BAB40667.2.
AB071194 mRNA. Translation: BAC22615.1.
CCDSiCCDS29638.1.
RefSeqiNP_598913.1. NM_134152.3.
UniGeneiMm.313136.

Genome annotation databases

EnsembliENSMUST00000025601; ENSMUSP00000025601; ENSMUSG00000024696.
GeneIDi107321.
KEGGimmu:107321.
UCSCiuc008guq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB053936 mRNA. Translation: BAB40667.2.
AB071194 mRNA. Translation: BAC22615.1.
CCDSiCCDS29638.1.
RefSeqiNP_598913.1. NM_134152.3.
UniGeneiMm.313136.

3D structure databases

ProteinModelPortaliQ99N69.
SMRiQ99N69. Positions 152-379.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi223241. 3 interactions.
IntActiQ99N69. 1 interaction.
STRINGi10090.ENSMUSP00000025601.

PTM databases

iPTMnetiQ99N69.
PhosphoSiteiQ99N69.

Proteomic databases

EPDiQ99N69.
MaxQBiQ99N69.
PaxDbiQ99N69.
PeptideAtlasiQ99N69.
PRIDEiQ99N69.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025601; ENSMUSP00000025601; ENSMUSG00000024696.
GeneIDi107321.
KEGGimmu:107321.
UCSCiuc008guq.1. mouse.

Organism-specific databases

CTDi9404.
MGIiMGI:2147677. Lpxn.

Phylogenomic databases

eggNOGiKOG1703. Eukaryota.
ENOG410XRD4. LUCA.
GeneTreeiENSGT00760000118910.
HOGENOMiHOG000018764.
HOVERGENiHBG001512.
InParanoidiQ99N69.
OMAiCKEEIGS.
OrthoDBiEOG70ZZQN.
PhylomeDBiQ99N69.
TreeFamiTF314113.

Miscellaneous databases

PROiQ99N69.
SOURCEiSearch...

Gene expression databases

BgeeiQ99N69.
CleanExiMM_LPXN.
GenevisibleiQ99N69. MM.

Family and domain databases

Gene3Di2.10.110.10. 4 hits.
InterProiIPR017305. Tgfb1i1/Leupaxin.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 4 hits.
[Graphical view]
PIRSFiPIRSF037881. Leupaxin. 1 hit.
SMARTiSM00132. LIM. 4 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The noncatalytic domain of protein-tyrosine phosphatase-PEST forms a complex with leupaxin that is a novel LIM domain protein."
    Ishizuka H., Amano N., Watanabe N., Mashima K.
    Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Spleen.
  2. "LIM domain-containing adaptor, leupaxin, localizes in focal adhesion and suppresses the integrin-induced tyrosine phosphorylation of paxillin."
    Tanaka T., Moriwaki K., Murata S., Miyasaka M.
    Cancer Sci. 101:363-368(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PTK2/FAK, DOMAIN LIM-3.
    Tissue: Spleen.
  3. "Leupaxin is a critical adaptor protein in the adhesion zone of the osteoclast."
    Gupta A., Lee B.S., Khadeer M.A., Tang Z., Chellaiah M., Abu-Amer Y., Goldknopf J., Hruska K.A.
    J. Bone Miner. Res. 18:669-685(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PTK2/FAK; PTPN12 AND PTK2B/PYK2, PHOSPHORYLATION.
  4. "Leupaxin binds to PEST domain tyrosine phosphatase PEP."
    Watanabe N., Amano N., Ishizuka H., Mashima K.
    Mol. Cell. Biochem. 269:13-17(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTPN22 AND PTPN12.
  5. "Leupaxin negatively regulates B cell receptor signaling."
    Chew V., Lam K.P.
    J. Biol. Chem. 282:27181-27191(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT TYR-72 BY LYN, INTERACTION WITH LYN.
  6. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-22; TYR-62 AND TYR-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  7. "The LIM protein leupaxin is enriched in smooth muscle and functions as an serum response factor cofactor to induce smooth muscle cell gene transcription."
    Sundberg-Smith L.J., DiMichele L.A., Sayers R.L., Mack C.P., Taylor J.M.
    Circ. Res. 102:1502-1511(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung and Spleen.

Entry informationi

Entry nameiLPXN_MOUSE
AccessioniPrimary (citable) accession number: Q99N69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: October 1, 2002
Last modified: July 6, 2016
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.