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Identification
HMDB Protein ID HMDBP14183
Secondary Accession Numbers None
Name Lipocalin-1
Synonyms
  1. Tear lipocalin
  2. Tear prealbumin
  3. von Ebner gland protein
  4. Tlc
  5. TP
  6. VEG protein
Gene Name LCN1
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Could play a role in taste reception. Could be necessary for the concentration and delivery of sapid molecules in the gustatory system. Can bind various ligands, with chemical structures ranging from lipids and retinoids to the macrocyclic antibiotic rifampicin and even to microbial siderophores. Exhibits an extremely wide ligand pocket.
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
retina homeostasis
sensory perception of taste
proteolysis
long-chain fatty acid transport
response to stimulus
Cellular Component
extracellular region
extracellular space
Molecular Function
cysteine-type endopeptidase inhibitor activity
small molecule binding
receptor binding
chloride ion binding
zinc ion 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 176
Molecular Weight 19249.845
Theoretical pI 5.572
Pfam Domain Function
Signals
  • 1-18;
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P31025
UniProtKB/Swiss-Prot Entry Name LCN1_HUMAN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. 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 ]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed:15164053 ]
  3. Azkargorta M, Soria J, Ojeda C, Guzman F, Acera A, Iloro I, Suarez T, Elortza F: Human Basal Tear Peptidome Characterization by CID, HCD, and ETD Followed by in Silico and in Vitro Analyses for Antimicrobial Peptide Identification. J Proteome Res. 2015 Jun 5;14(6):2649-58. doi: 10.1021/acs.jproteome.5b00179. Epub 2015 May 20. [PubMed:25946035 ]
  4. Blaker M, Kock K, Ahlers C, Buck F, Schmale H: Molecular cloning of human von Ebner's gland protein, a member of the lipocalin superfamily highly expressed in lingual salivary glands. Biochim Biophys Acta. 1993 Feb 20;1172(1-2):131-7. doi: 10.1016/0167-4781(93)90279-m. [PubMed:7679926 ]
  5. Redl B, Holzfeind P, Lottspeich F: cDNA cloning and sequencing reveals human tear prealbumin to be a member of the lipophilic-ligand carrier protein superfamily. J Biol Chem. 1992 Oct 5;267(28):20282-7. [PubMed:1400345 ]
  6. Lassagne H, Gachon AM: Cloning of a human lacrimal lipocalin secreted in tears. Exp Eye Res. 1993 May;56(5):605-9. doi: 10.1006/exer.1993.1075. [PubMed:8500570 ]
  7. Holzfeind P, Redl B: Structural organization of the gene encoding the human lipocalin tear prealbumin and synthesis of the recombinant protein in Escherichia coli. Gene. 1994 Feb 25;139(2):177-83. doi: 10.1016/0378-1119(94)90752-8. [PubMed:8112601 ]
  8. Wojnar P, Lechner M, Merschak P, Redl B: Molecular cloning of a novel lipocalin-1 interacting human cell membrane receptor using phage display. J Biol Chem. 2001 Jun 8;276(23):20206-12. doi: 10.1074/jbc.M101762200. Epub 2001 Apr 3. [PubMed:11287427 ]
  9. Gasymov OK, Abduragimov AR, Merschak P, Redl B, Glasgow BJ: Oligomeric state of lipocalin-1 (LCN1) by multiangle laser light scattering and fluorescence anisotropy decay. Biochim Biophys Acta. 2007 Oct;1774(10):1307-15. doi: 10.1016/j.bbapap.2007.07.014. Epub 2007 Aug 14. [PubMed:17869594 ]
  10. Breustedt DA, Korndorfer IP, Redl B, Skerra A: The 1.8-A crystal structure of human tear lipocalin reveals an extended branched cavity with capacity for multiple ligands. J Biol Chem. 2005 Jan 7;280(1):484-93. doi: 10.1074/jbc.M410466200. Epub 2004 Oct 15. [PubMed:15489503 ]