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Showing Protein Transforming growth factor beta activator LRRC32 (HMDBP14558)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP14558
Secondary Accession Numbers None
Name Transforming growth factor beta activator LRRC32
Synonyms
  1. Garpin
  2. Glycoprotein A repetitions predominant
  3. Leucine-rich repeat-containing protein 32
  4. GARP
Gene Name LRRC32
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space (PubMed:19750484, PubMed:19651619, PubMed:22278742). Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta (PubMed:22278742). Able to outcompete LTBP1 for binding to LAP regulatory chain of TGF-beta (PubMed:22278742). Controls activation of TGF-beta-1 (TGFB1) on the surface of activated regulatory T-cells (Tregs) (PubMed:19750484, PubMed:19651619). Required for epithelial fusion during palate development by regulating activation of TGF-beta-3 (TGFB3) (By similarity).
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
negative regulation of cytokine production
negative regulation of activated T cell proliferation
regulation of transforming growth factor beta3 activation
regulation of transforming growth factor beta activation
secondary palate development
transforming growth factor beta receptor signaling pathway
positive regulation of gene expression
Cellular Component
cell surface
nucleoplasm
extracellular space
extracellular matrix
integral to plasma membrane
Molecular Function
transforming growth factor beta binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 662
Molecular Weight 71978.035
Theoretical pI 6.125
Pfam Domain Function
Signals
  • 1-19;
Transmembrane Regions
  • 628-648;
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q14392
UniProtKB/Swiss-Prot Entry Name LRC32_HUMAN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. [PubMed:19159218 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Tran DQ, Andersson J, Wang R, Ramsey H, Unutmaz D, Shevach EM: GARP (LRRC32) is essential for the surface expression of latent TGF-beta on platelets and activated FOXP3+ regulatory T cells. Proc Natl Acad Sci U S A. 2009 Aug 11;106(32):13445-50. doi: 10.1073/pnas.0901944106. Epub 2009 Jul 27. [PubMed:19651619 ]
  4. Ollendorff V, Noguchi T, deLapeyriere O, Birnbaum D: The GARP gene encodes a new member of the family of leucine-rich repeat-containing proteins. Cell Growth Differ. 1994 Feb;5(2):213-9. [PubMed:8180135 ]
  5. Wang R, Wan Q, Kozhaya L, Fujii H, Unutmaz D: Identification of a regulatory T cell specific cell surface molecule that mediates suppressive signals and induces Foxp3 expression. PLoS One. 2008 Jul 16;3(7):e2705. doi: 10.1371/journal.pone.0002705. [PubMed:18628982 ]
  6. Stockis J, Colau D, Coulie PG, Lucas S: Membrane protein GARP is a receptor for latent TGF-beta on the surface of activated human Treg. Eur J Immunol. 2009 Dec;39(12):3315-22. doi: 10.1002/eji.200939684. [PubMed:19750484 ]
  7. Chan DV, Somani AK, Young AB, Massari JV, Ohtola J, Sugiyama H, Garaczi E, Babineau D, Cooper KD, McCormick TS: Signal peptide cleavage is essential for surface expression of a regulatory T cell surface protein, leucine rich repeat containing 32 (LRRC32). BMC Biochem. 2011 May 26;12:27. doi: 10.1186/1471-2091-12-27. [PubMed:21615933 ]
  8. Wang R, Zhu J, Dong X, Shi M, Lu C, Springer TA: GARP regulates the bioavailability and activation of TGFbeta. Mol Biol Cell. 2012 Mar;23(6):1129-39. doi: 10.1091/mbc.E11-12-1018. Epub 2012 Jan 25. [PubMed:22278742 ]