ID LPXN_HUMAN Reviewed; 386 AA. AC O60711; B2R8B4; B4DV71; Q53FW6; Q6FI07; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 199. DE RecName: Full=Leupaxin; GN Name=LPXN; Synonyms=LDLP; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PTK2B/PYK2, AND RP CHARACTERIZATION. RC TISSUE=Spleen; RX PubMed=9565592; DOI=10.1074/jbc.273.19.11709; RA Lipsky B.P., Beals C.R., Staunton D.E.; RT "Leupaxin is a novel LIM domain protein that forms a complex with PYK2."; RL J. Biol. Chem. 273:11709-11713(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Small intestine, and Spleen; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=B-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 [8] RP INTERACTION WITH ITGA4. RX PubMed=10604475; DOI=10.1038/45264; RA Liu S., Thomas S.M., Woodside D.G., Rose D.M., Kiosses W.B., Pfaff M., RA Ginsberg M.H.; RT "Binding of paxillin to alpha4 integrins modifies integrin-dependent RT biological responses."; RL Nature 402:676-681(1999). RN [9] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=12674328; DOI=10.1359/jbmr.2003.18.4.669; RA Gupta A., Lee B.S., Khadeer M.A., Tang Z., Chellaiah M., Abu-Amer Y., RA Goldknopf J., Hruska K.A.; RT "Leupaxin is a critical adaptor protein in the adhesion zone of the RT osteoclast."; RL J. Bone Miner. Res. 18:669-685(2003). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from RT human T cells using immobilized metal affinity chromatography and tandem RT mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [11] RP IDENTIFICATION BY 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 [12] RP INTERACTION WITH PTK2B/PYK2 AND PTPN12, AND SUBCELLULAR LOCATION. RX PubMed=17329398; DOI=10.1152/ajpcell.00503.2006; RA Sahu S.N., Nunez S., Bai G., Gupta A.; RT "Interaction of Pyk2 and PTP-PEST with leupaxin in prostate cancer cells."; RL Am. J. Physiol. 292:C2288-C2296(2007). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-72 BY LYN, AND RP INTERACTION WITH LYN. RX PubMed=17640867; DOI=10.1074/jbc.m704625200; RA Chew V., Lam K.P.; RT "Leupaxin negatively regulates B cell receptor signaling."; RL J. Biol. Chem. 282:27181-27191(2007). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH RP PTK2/FAK AND SRF. RX PubMed=18497331; DOI=10.1161/circresaha.107.170357; RA Sundberg-Smith L.J., DiMichele L.A., Sayers R.L., Mack C.P., Taylor J.M.; RT "The LIM protein leupaxin is enriched in smooth muscle and functions as an RT serum response factor cofactor to induce smooth muscle cell gene RT transcription."; RL Circ. Res. 102:1502-1511(2008). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH RP AR. RX PubMed=18451096; DOI=10.1210/me.2006-0546; RA Kaulfuss S., Grzmil M., Hemmerlein B., Thelen P., Schweyer S., Neesen J., RA Bubendorf L., Glass A.G., Jarry H., Auber B., Burfeind P.; RT "Leupaxin, a novel coactivator of the androgen receptor, is expressed in RT prostate cancer and plays a role in adhesion and invasion of prostate RT carcinoma cells."; RL Mol. Endocrinol. 22:1606-1621(2008). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [17] RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYR-22; TYR-62 AND RP TYR-72. RX PubMed=20543562; DOI=10.4161/cam.4.4.12399; RA Chen P.W., Kroog G.S.; RT "Leupaxin is similar to paxillin in focal adhesion targeting and tyrosine RT phosphorylation but has distinct roles in cell adhesion and spreading."; RL Cell Adh. Migr. 4:527-540(2010). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [22] RP STRUCTURE BY NMR OF 260-326. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the LIM domain of human leupaxin."; RL Submitted (JAN-2006) to the PDB data bank. CC -!- FUNCTION: Transcriptional coactivator for androgen receptor (AR) and CC serum response factor (SRF). Contributes to the regulation of cell CC adhesion, spreading and cell migration and acts as a negative regulator CC in integrin-mediated cell adhesion events. Suppresses the integrin- CC induced tyrosine phosphorylation of paxillin (PXN). May play a critical CC role as an adapter protein in the formation of the adhesion zone in CC osteoclasts. Negatively regulates B-cell antigen receptor (BCR) CC signaling. {ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:18451096, CC ECO:0000269|PubMed:18497331, ECO:0000269|PubMed:20543562}. CC -!- SUBUNIT: Interacts with PTPN22 (By similarity). Interacts with CC unphosphorylated ITGA4. Interacts with PTK2B/PYK2, PTPN12, AR and SRF. CC Interacts (via LD motif 3) with LYN and the interaction is induced upon CC B-cell antigen receptor (BCR) activation. Interacts (via LD motif 3) CC with PTK2/FAK. {ECO:0000250, ECO:0000269|PubMed:10604475, CC ECO:0000269|PubMed:17329398, ECO:0000269|PubMed:17640867, CC ECO:0000269|PubMed:18451096, ECO:0000269|PubMed:18497331, CC ECO:0000269|PubMed:9565592}. CC -!- INTERACTION: CC O60711; P21549: AGXT; NbExp=3; IntAct=EBI-744222, EBI-727098; CC O60711; P29972: AQP1; NbExp=3; IntAct=EBI-744222, EBI-745213; CC O60711; P31274: HOXC9; NbExp=7; IntAct=EBI-744222, EBI-1779423; CC O60711; P25800: LMO1; NbExp=7; IntAct=EBI-744222, EBI-8639312; CC O60711; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-744222, EBI-11742507; CC O60711; Q96CV9: OPTN; NbExp=3; IntAct=EBI-744222, EBI-748974; CC O60711; Q8IVE3: PLEKHH2; NbExp=4; IntAct=EBI-744222, EBI-2815745; CC O60711; Q494U1: PLEKHN1; NbExp=3; IntAct=EBI-744222, EBI-10241513; CC O60711; Q494U1-3: PLEKHN1; NbExp=3; IntAct=EBI-744222, EBI-12014286; CC O60711; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-744222, EBI-11956563; CC O60711; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-744222, EBI-11984663; CC O60711; Q06455-4: RUNX1T1; NbExp=3; IntAct=EBI-744222, EBI-10224192; CC O60711; P01137: TGFB1; NbExp=3; IntAct=EBI-744222, EBI-779636; CC O60711; Q63HR2: TNS2; NbExp=3; IntAct=EBI-744222, EBI-949753; CC O60711; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-744222, EBI-6116822; CC O60711; P18206-2: VCL; NbExp=3; IntAct=EBI-744222, EBI-11027067; CC O60711; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-744222, EBI-3957603; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion. CC Nucleus. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, CC podosome. Cell membrane. Note=Shuttles between the cytoplasm and CC nucleus. Recruited to the cell membrane following B-cell antigen CC receptor (BCR) cross-linking in B-cells. Enhanced focal adhesion kinase CC activity (PTK2/FAK) attenuates its nuclear accumulation and limits its CC ability to enhance serum response factor (SRF)-dependent gene CC transcription. Targeting to focal adhesions is essential for its CC tyrosine phosphorylation in response to bombesin. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O60711-1; Sequence=Displayed; CC Name=2; CC IsoId=O60711-2; Sequence=VSP_042655; CC -!- TISSUE SPECIFICITY: Macrophages, monocytes and osteoclasts (at protein CC level). Strongly expressed in cells and tissues of hematopoietic CC origin. Highest expression in lymphoid tissues such as spleen, lymph CC node, thymus and appendix and in the vascular smooth muscle. Lower CC levels in bone marrow and fetal liver. Also expressed in peripheral CC blood lymphocytes and a number of hematopoietic cell lines. Very low CC levels found in epithelial cell lines. Expressed in prostate cancer CC (PCa) cells and its expression intensity is directly linked to PCa CC progression. {ECO:0000269|PubMed:12674328, ECO:0000269|PubMed:18451096, CC ECO:0000269|PubMed:18497331}. CC -!- DOMAIN: The LIM domain 3 is critical for focal adhesion targeting and CC the suppression of paxillin (PXN) tyrosine phosphorylation. The LIM CC domain 3 alone or both LIM domains 3 and 4 can mediate interaction with CC AR. CC -!- PTM: Phosphorylated on tyrosine residues. Phosphorylation on Tyr-72 is CC important for its inhibitory function. Bombesin stimulates CC phosphorylation on Tyr-22, Tyr-62 and Tyr-72. CC {ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:20543562}. CC -!- SIMILARITY: Belongs to the paxillin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF062075; AAC16014.1; -; mRNA. DR EMBL; AK300955; BAG62583.1; -; mRNA. DR EMBL; AK313306; BAG36111.1; -; mRNA. DR EMBL; CR536531; CAG38768.1; -; mRNA. DR EMBL; AK223165; BAD96885.1; -; mRNA. DR EMBL; AP001350; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP003557; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471076; EAW73808.1; -; Genomic_DNA. DR EMBL; BC019035; AAH19035.1; -; mRNA. DR CCDS; CCDS53635.1; -. [O60711-2] DR CCDS; CCDS7969.1; -. [O60711-1] DR RefSeq; NP_001137467.1; NM_001143995.2. [O60711-2] DR RefSeq; NP_001294880.1; NM_001307951.1. DR RefSeq; NP_004802.1; NM_004811.2. [O60711-1] DR PDB; 1X3H; NMR; -; A=260-326. DR PDB; 4XEF; X-ray; 2.50 A; B/C/E/F=1-20. DR PDB; 4XEK; X-ray; 1.79 A; C=86-104. DR PDB; 4XEV; X-ray; 2.01 A; C/F=86-104. DR PDBsum; 1X3H; -. DR PDBsum; 4XEF; -. DR PDBsum; 4XEK; -. DR PDBsum; 4XEV; -. DR AlphaFoldDB; O60711; -. DR SMR; O60711; -. DR BioGRID; 114801; 66. DR IntAct; O60711; 69. DR MINT; O60711; -. DR STRING; 9606.ENSP00000431284; -. DR iPTMnet; O60711; -. DR PhosphoSitePlus; O60711; -. DR BioMuta; LPXN; -. DR EPD; O60711; -. DR jPOST; O60711; -. DR MassIVE; O60711; -. DR MaxQB; O60711; -. DR PaxDb; 9606-ENSP00000431284; -. DR PeptideAtlas; O60711; -. DR ProteomicsDB; 49535; -. [O60711-1] DR ProteomicsDB; 49536; -. [O60711-2] DR Pumba; O60711; -. DR Antibodypedia; 27661; 208 antibodies from 25 providers. DR DNASU; 9404; -. DR Ensembl; ENST00000395074.7; ENSP00000378512.2; ENSG00000110031.13. [O60711-1] DR Ensembl; ENST00000528954.5; ENSP00000431284.1; ENSG00000110031.13. [O60711-2] DR GeneID; 9404; -. DR KEGG; hsa:9404; -. DR MANE-Select; ENST00000395074.7; ENSP00000378512.2; NM_004811.3; NP_004802.1. DR UCSC; uc001nmw.4; human. [O60711-1] DR AGR; HGNC:14061; -. DR CTD; 9404; -. DR DisGeNET; 9404; -. DR GeneCards; LPXN; -. DR HGNC; HGNC:14061; LPXN. DR HPA; ENSG00000110031; Tissue enhanced (lymphoid). DR MIM; 605390; gene. DR neXtProt; NX_O60711; -. DR OpenTargets; ENSG00000110031; -. DR PharmGKB; PA30441; -. DR VEuPathDB; HostDB:ENSG00000110031; -. DR eggNOG; KOG1703; Eukaryota. DR GeneTree; ENSGT00940000160259; -. DR HOGENOM; CLU_001357_1_1_1; -. DR InParanoid; O60711; -. DR OMA; QNGKTYC; -. DR OrthoDB; 370973at2759; -. DR PhylomeDB; O60711; -. DR TreeFam; TF314113; -. DR PathwayCommons; O60711; -. DR SignaLink; O60711; -. DR SIGNOR; O60711; -. DR BioGRID-ORCS; 9404; 13 hits in 1156 CRISPR screens. DR ChiTaRS; LPXN; human. DR EvolutionaryTrace; O60711; -. DR GeneWiki; LPXN; -. DR GenomeRNAi; 9404; -. DR Pharos; O60711; Tbio. DR PRO; PR:O60711; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; O60711; Protein. DR Bgee; ENSG00000110031; Expressed in granulocyte and 160 other cell types or tissues. DR ExpressionAtlas; O60711; baseline and differential. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005925; C:focal adhesion; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0002102; C:podosome; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB. DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc. DR GO; GO:0043542; P:endothelial cell migration; IBA:GO_Central. DR GO; GO:0050859; P:negative regulation of B cell receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0007162; P:negative regulation of cell adhesion; IDA:UniProtKB. DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc. DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central. DR CDD; cd09406; LIM1_Leupaxin; 1. DR CDD; cd09408; LIM2_Leupaxin; 1. DR CDD; cd09410; LIM3_Leupaxin; 1. DR CDD; cd09339; LIM4_Paxillin_like; 1. DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 4. DR InterPro; IPR017305; Tgfb1i1/Leupaxin/TGFB1I1. DR InterPro; IPR001781; Znf_LIM. DR PANTHER; PTHR24214; PDZ AND LIM DOMAIN PROTEIN ZASP; 1. DR PANTHER; PTHR24214:SF38; PDZ AND LIM DOMAIN PROTEIN ZASP; 1. DR Pfam; PF00412; LIM; 4. DR PIRSF; PIRSF037881; Leupaxin; 1. DR SMART; SM00132; LIM; 4. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 5. DR PROSITE; PS00478; LIM_DOMAIN_1; 4. DR PROSITE; PS50023; LIM_DOMAIN_2; 4. DR Genevisible; O60711; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; Cell adhesion; KW Cell junction; Cell membrane; Cell projection; Cytoplasm; LIM domain; KW Membrane; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; Transcription; Transcription regulation; Zinc. FT CHAIN 1..386 FT /note="Leupaxin" FT /id="PRO_0000075836" FT DOMAIN 150..208 FT /note="LIM zinc-binding 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 209..267 FT /note="LIM zinc-binding 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 268..326 FT /note="LIM zinc-binding 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 327..386 FT /note="LIM zinc-binding 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT REGION 13..41 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 3..15 FT /note="LD motif 1" FT MOTIF 70..82 FT /note="LD motif 2" FT MOTIF 92..103 FT /note="LD motif 3" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378, FT ECO:0007744|PubMed:25944712" FT MOD_RES 19 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15144186" FT MOD_RES 22 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:20543562" FT MOD_RES 54 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99N69" FT MOD_RES 62 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:20543562" FT MOD_RES 72 FT /note="Phosphotyrosine; by LYN" FT /evidence="ECO:0000269|PubMed:17640867, FT ECO:0000269|PubMed:20543562" FT MOD_RES 81 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..4 FT /note="MEEL -> MSTLLISSS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042655" FT VARIANT 148 FT /note="P -> T (in dbSNP:rs12271558)" FT /id="VAR_050152" FT CONFLICT 2 FT /note="E -> D (in Ref. 3; CAG38768)" FT /evidence="ECO:0000305" FT CONFLICT 14 FT /note="S -> T (in Ref. 4; BAD96885)" FT /evidence="ECO:0000305" FT CONFLICT 100 FT /note="L -> M (in Ref. 3; CAG38768)" FT /evidence="ECO:0000305" FT HELIX 2..14 FT /evidence="ECO:0007829|PDB:4XEF" FT HELIX 88..98 FT /evidence="ECO:0007829|PDB:4XEK" FT TURN 271..273 FT /evidence="ECO:0007829|PDB:1X3H" FT STRAND 282..284 FT /evidence="ECO:0007829|PDB:1X3H" FT STRAND 287..289 FT /evidence="ECO:0007829|PDB:1X3H" FT TURN 291..293 FT /evidence="ECO:0007829|PDB:1X3H" FT STRAND 297..299 FT /evidence="ECO:0007829|PDB:1X3H" FT STRAND 309..313 FT /evidence="ECO:0007829|PDB:1X3H" FT HELIX 318..325 FT /evidence="ECO:0007829|PDB:1X3H" SQ SEQUENCE 386 AA; 43332 MW; C8D2BE61FAB11F3A CRC64; MEELDALLEE LERSTLQDSD EYSNPAPLPL DQHSRKETNL DETSEILSIQ DNTSPLPAQL VYTTNIQELN VYSEAQEPKE SPPPSKTSAA AQLDELMAHL TEMQAKVAVR ADAGKKHLPD KQDHKASLDS MLGGLEQELQ DLGIATVPKG HCASCQKPIA GKVIHALGQS WHPEHFVCTH CKEEIGSSPF FERSGLAYCP NDYHQLFSPR CAYCAAPILD KVLTAMNQTW HPEHFFCSHC GEVFGAEGFH EKDKKPYCRK DFLAMFSPKC GGCNRPVLEN YLSAMDTVWH PECFVCGDCF TSFSTGSFFE LDGRPFCELH YHHRRGTLCH GCGQPITGRC ISAMGYKFHP EHFVCAFCLT QLSKGIFREQ NDKTYCQPCF NKLFPL //