LPXN_HUMAN
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 03-AUG-2022, entry version 190.
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}.
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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; 64.
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; O60711; -.
DR PeptideAtlas; O60711; -.
DR PRIDE; O60711; -.
DR ProteomicsDB; 49535; -. [O60711-1]
DR ProteomicsDB; 49536; -. [O60711-2]
DR Antibodypedia; 27661; 184 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 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; THCKKEI; -.
DR OrthoDB; 1593918at2759; -.
DR PhylomeDB; O60711; -.
DR TreeFam; TF314113; -.
DR PathwayCommons; O60711; -.
DR SignaLink; O60711; -.
DR SIGNOR; O60711; -.
DR BioGRID-ORCS; 9404; 13 hits in 1078 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 158 other tissues.
DR ExpressionAtlas; O60711; baseline and differential.
DR Genevisible; O60711; HS.
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:UniProtKB.
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 InterPro; IPR017305; Tgfb1i1/Leupaxin/TGFB1I1.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 4.
DR PIRSF; PIRSF037881; Leupaxin; 1.
DR SMART; SM00132; LIM; 4.
DR PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 4.
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
