Full text data of LCN1
LCN1
(VEGP)
[Confidence: low (only semi-automatic identification from reviews)]
Lipocalin-1 (Tear lipocalin; Tlc; Tear prealbumin; TP; Von Ebner gland protein; VEG protein; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Lipocalin-1 (Tear lipocalin; Tlc; Tear prealbumin; TP; Von Ebner gland protein; VEG protein; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P31025
ID LCN1_HUMAN Reviewed; 176 AA.
AC P31025; Q5T8A1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1993, sequence version 1.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=Lipocalin-1;
DE AltName: Full=Tear lipocalin;
DE Short=Tlc;
DE AltName: Full=Tear prealbumin;
DE Short=TP;
DE AltName: Full=Von Ebner gland protein;
DE Short=VEG protein;
DE Flags: Precursor;
GN Name=LCN1; Synonyms=VEGP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tongue;
RX PubMed=7679926;
RA Blaeker M., Kock K., Ahlers C., Buck F., Schmale H.;
RT "Molecular cloning of human von Ebner's gland protein, a member of the
RT lipocalin superfamily highly expressed in lingual salivary glands.";
RL Biochim. Biophys. Acta 1172:131-137(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tear;
RX PubMed=1400345;
RA Redl B., Holzfeind P., Lottspeich F.;
RT "cDNA cloning and sequencing reveals human tear prealbumin to be a
RT member of the lipophilic-ligand carrier protein superfamily.";
RL J. Biol. Chem. 267:20282-20287(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tear;
RX PubMed=8500570; DOI=10.1006/exer.1993.1075;
RA Lassagne H., Gachon A.-M.;
RT "Cloning of a human lacrimal lipocalin secreted in tears.";
RL Exp. Eye Res. 56:605-609(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8112601; DOI=10.1016/0378-1119(94)90752-8;
RA Holzfeind P., Redl B.;
RT "Structural organization of the gene encoding the human lipocalin tear
RT prealbumin and synthesis of the recombinant protein in Escherichia
RT coli.";
RL Gene 139:177-183(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 19-38.
RC TISSUE=Nasal mucus;
RA Scalfari F., Castagna M., Fattori B., Andreini I., Maremmani C.,
RA Pelosi P.;
RT "Expression of a lipocalin in human nasal mucosa.";
RL Comp. Biochem. Physiol. 118B:819-824(1997).
RN [9]
RP INTERACTION WITH LMBR1L.
RC TISSUE=Pituitary;
RX PubMed=11287427; DOI=10.1074/jbc.M101762200;
RA Wojnar P., Lechner M., Merschak P., Redl B.;
RT "Molecular cloning of a novel lipocalin-1 interacting human cell
RT membrane receptor using phage display.";
RL J. Biol. Chem. 276:20206-20212(2001).
RN [10]
RP INTERACTION WITH LMBR1L, AND ENDOCYTOSIS.
RX PubMed=12591932; DOI=10.1074/jbc.M210922200;
RA Wojnar P., Lechner M., Redl B.;
RT "Antisense down-regulation of lipocalin-interacting membrane receptor
RT expression inhibits cellular internalization of lipocalin-1 in human
RT NT2 cells.";
RL J. Biol. Chem. 278:16209-16215(2003).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 23-175.
RX PubMed=15489503; DOI=10.1074/jbc.M410466200;
RA Breustedt D.A., Korndorfer I.P., Redl B., Skerra A.;
RT "The 1.8-A crystal structure of human tear lipocalin reveals an
RT extended branched cavity with capacity for multiple ligands.";
RL J. Biol. Chem. 280:484-493(2005).
CC -!- FUNCTION: Could play a role in taste reception. Could be necessary
CC for the concentration and delivery of sapid molecules in the
CC gustatory system. Can bind various ligands, with chemical
CC structures ranging from lipids and retinoids to the macrocyclic
CC antibiotic rifampicin and even to microbial siderophores. Exhibits
CC an extremely wide ligand pocket.
CC -!- SUBUNIT: Homodimer (By similarity). Binds to LMBR1L which may
CC mediate its endocytosis.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Mainly expressed in lachrymal and salivary
CC glands. Also expressed in the prostate.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X62418; CAA44284.1; -; mRNA.
DR EMBL; M90424; AAA61845.1; -; mRNA.
DR EMBL; X67647; CAA47889.1; -; mRNA.
DR EMBL; L14927; AAA18633.1; -; Genomic_DNA.
DR EMBL; AL161452; CAI14045.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88156.1; -; Genomic_DNA.
DR EMBL; BC065721; AAH65721.1; -; mRNA.
DR EMBL; BC074925; AAH74925.1; -; mRNA.
DR EMBL; BC074926; AAH74926.1; -; mRNA.
DR PIR; A44029; LCHUL.
DR RefSeq; NP_001239546.1; NM_001252617.1.
DR RefSeq; NP_001239547.1; NM_001252618.1.
DR RefSeq; NP_001239548.1; NM_001252619.1.
DR RefSeq; NP_002288.1; NM_002297.3.
DR UniGene; Hs.530311; -.
DR PDB; 1XKI; X-ray; 1.80 A; A=23-175.
DR PDB; 3EYC; X-ray; 2.60 A; A/B/C/D=23-175.
DR PDBsum; 1XKI; -.
DR PDBsum; 3EYC; -.
DR DisProt; DP00647; -.
DR ProteinModelPortal; P31025; -.
DR SMR; P31025; 31-173.
DR IntAct; P31025; 1.
DR STRING; 9606.ENSP00000263598; -.
DR Allergome; 3990; Hom s TL.
DR PhosphoSite; P31025; -.
DR DMDM; 401346; -.
DR UCD-2DPAGE; P31025; -.
DR PeptideAtlas; P31025; -.
DR PRIDE; P31025; -.
DR Ensembl; ENST00000263598; ENSP00000263598; ENSG00000160349.
DR Ensembl; ENST00000371781; ENSP00000360846; ENSG00000160349.
DR GeneID; 3933; -.
DR KEGG; hsa:3933; -.
DR UCSC; uc004cfz.2; human.
DR CTD; 3933; -.
DR GeneCards; GC09P138413; -.
DR HGNC; HGNC:6525; LCN1.
DR MIM; 151675; gene.
DR neXtProt; NX_P31025; -.
DR PharmGKB; PA30308; -.
DR HOGENOM; HOG000231562; -.
DR HOVERGEN; HBG101411; -.
DR InParanoid; P31025; -.
DR OMA; LISGRCQ; -.
DR OrthoDB; EOG7GXPD6; -.
DR PhylomeDB; P31025; -.
DR ChiTaRS; LCN1; human.
DR EvolutionaryTrace; P31025; -.
DR GeneWiki; LCN1; -.
DR GenomeRNAi; 3933; -.
DR NextBio; 15447; -.
DR PRO; PR:P31025; -.
DR Bgee; P31025; -.
DR CleanEx; HS_LCN1; -.
DR Genevestigator; P31025; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0050909; P:sensory perception of taste; IEA:UniProtKB-KW.
DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR011038; Calycin-like.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR InterPro; IPR002450; von_Ebner_gland.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR01175; VNEBNERGLAND.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Reference proteome; Secreted; Sensory transduction;
KW Signal; Taste; Transport.
FT SIGNAL 1 18
FT CHAIN 19 176 Lipocalin-1.
FT /FTId=PRO_0000017974.
FT DISULFID 79 171
FT STRAND 33 42
FT STRAND 51 54
FT STRAND 57 61
FT STRAND 67 73
FT STRAND 80 88
FT STRAND 94 97
FT HELIX 98 100
FT STRAND 102 108
FT STRAND 114 121
FT STRAND 128 139
FT HELIX 145 154
FT STRAND 160 163
SQ SEQUENCE 176 AA; 19250 MW; 0DDBF124C8C78CB8 CRC64;
MKPLLLAVSL GLIAALQAHH LLASDEEIQD VSGTWYLKAM TVDREFPEMN LESVTPMTLT
TLEGGNLEAK VTMLISGRCQ EVKAVLEKTD EPGKYTADGG KHVAYIIRSH VKDHYIFYCE
GELHGKPVRG VKLVGRDPKN NLEALEDFEK AAGARGLSTE SILIPRQSET CSPGSD
//
ID LCN1_HUMAN Reviewed; 176 AA.
AC P31025; Q5T8A1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1993, sequence version 1.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=Lipocalin-1;
DE AltName: Full=Tear lipocalin;
DE Short=Tlc;
DE AltName: Full=Tear prealbumin;
DE Short=TP;
DE AltName: Full=Von Ebner gland protein;
DE Short=VEG protein;
DE Flags: Precursor;
GN Name=LCN1; Synonyms=VEGP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tongue;
RX PubMed=7679926;
RA Blaeker M., Kock K., Ahlers C., Buck F., Schmale H.;
RT "Molecular cloning of human von Ebner's gland protein, a member of the
RT lipocalin superfamily highly expressed in lingual salivary glands.";
RL Biochim. Biophys. Acta 1172:131-137(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tear;
RX PubMed=1400345;
RA Redl B., Holzfeind P., Lottspeich F.;
RT "cDNA cloning and sequencing reveals human tear prealbumin to be a
RT member of the lipophilic-ligand carrier protein superfamily.";
RL J. Biol. Chem. 267:20282-20287(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tear;
RX PubMed=8500570; DOI=10.1006/exer.1993.1075;
RA Lassagne H., Gachon A.-M.;
RT "Cloning of a human lacrimal lipocalin secreted in tears.";
RL Exp. Eye Res. 56:605-609(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8112601; DOI=10.1016/0378-1119(94)90752-8;
RA Holzfeind P., Redl B.;
RT "Structural organization of the gene encoding the human lipocalin tear
RT prealbumin and synthesis of the recombinant protein in Escherichia
RT coli.";
RL Gene 139:177-183(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 19-38.
RC TISSUE=Nasal mucus;
RA Scalfari F., Castagna M., Fattori B., Andreini I., Maremmani C.,
RA Pelosi P.;
RT "Expression of a lipocalin in human nasal mucosa.";
RL Comp. Biochem. Physiol. 118B:819-824(1997).
RN [9]
RP INTERACTION WITH LMBR1L.
RC TISSUE=Pituitary;
RX PubMed=11287427; DOI=10.1074/jbc.M101762200;
RA Wojnar P., Lechner M., Merschak P., Redl B.;
RT "Molecular cloning of a novel lipocalin-1 interacting human cell
RT membrane receptor using phage display.";
RL J. Biol. Chem. 276:20206-20212(2001).
RN [10]
RP INTERACTION WITH LMBR1L, AND ENDOCYTOSIS.
RX PubMed=12591932; DOI=10.1074/jbc.M210922200;
RA Wojnar P., Lechner M., Redl B.;
RT "Antisense down-regulation of lipocalin-interacting membrane receptor
RT expression inhibits cellular internalization of lipocalin-1 in human
RT NT2 cells.";
RL J. Biol. Chem. 278:16209-16215(2003).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 23-175.
RX PubMed=15489503; DOI=10.1074/jbc.M410466200;
RA Breustedt D.A., Korndorfer I.P., Redl B., Skerra A.;
RT "The 1.8-A crystal structure of human tear lipocalin reveals an
RT extended branched cavity with capacity for multiple ligands.";
RL J. Biol. Chem. 280:484-493(2005).
CC -!- FUNCTION: Could play a role in taste reception. Could be necessary
CC for the concentration and delivery of sapid molecules in the
CC gustatory system. Can bind various ligands, with chemical
CC structures ranging from lipids and retinoids to the macrocyclic
CC antibiotic rifampicin and even to microbial siderophores. Exhibits
CC an extremely wide ligand pocket.
CC -!- SUBUNIT: Homodimer (By similarity). Binds to LMBR1L which may
CC mediate its endocytosis.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Mainly expressed in lachrymal and salivary
CC glands. Also expressed in the prostate.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X62418; CAA44284.1; -; mRNA.
DR EMBL; M90424; AAA61845.1; -; mRNA.
DR EMBL; X67647; CAA47889.1; -; mRNA.
DR EMBL; L14927; AAA18633.1; -; Genomic_DNA.
DR EMBL; AL161452; CAI14045.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88156.1; -; Genomic_DNA.
DR EMBL; BC065721; AAH65721.1; -; mRNA.
DR EMBL; BC074925; AAH74925.1; -; mRNA.
DR EMBL; BC074926; AAH74926.1; -; mRNA.
DR PIR; A44029; LCHUL.
DR RefSeq; NP_001239546.1; NM_001252617.1.
DR RefSeq; NP_001239547.1; NM_001252618.1.
DR RefSeq; NP_001239548.1; NM_001252619.1.
DR RefSeq; NP_002288.1; NM_002297.3.
DR UniGene; Hs.530311; -.
DR PDB; 1XKI; X-ray; 1.80 A; A=23-175.
DR PDB; 3EYC; X-ray; 2.60 A; A/B/C/D=23-175.
DR PDBsum; 1XKI; -.
DR PDBsum; 3EYC; -.
DR DisProt; DP00647; -.
DR ProteinModelPortal; P31025; -.
DR SMR; P31025; 31-173.
DR IntAct; P31025; 1.
DR STRING; 9606.ENSP00000263598; -.
DR Allergome; 3990; Hom s TL.
DR PhosphoSite; P31025; -.
DR DMDM; 401346; -.
DR UCD-2DPAGE; P31025; -.
DR PeptideAtlas; P31025; -.
DR PRIDE; P31025; -.
DR Ensembl; ENST00000263598; ENSP00000263598; ENSG00000160349.
DR Ensembl; ENST00000371781; ENSP00000360846; ENSG00000160349.
DR GeneID; 3933; -.
DR KEGG; hsa:3933; -.
DR UCSC; uc004cfz.2; human.
DR CTD; 3933; -.
DR GeneCards; GC09P138413; -.
DR HGNC; HGNC:6525; LCN1.
DR MIM; 151675; gene.
DR neXtProt; NX_P31025; -.
DR PharmGKB; PA30308; -.
DR HOGENOM; HOG000231562; -.
DR HOVERGEN; HBG101411; -.
DR InParanoid; P31025; -.
DR OMA; LISGRCQ; -.
DR OrthoDB; EOG7GXPD6; -.
DR PhylomeDB; P31025; -.
DR ChiTaRS; LCN1; human.
DR EvolutionaryTrace; P31025; -.
DR GeneWiki; LCN1; -.
DR GenomeRNAi; 3933; -.
DR NextBio; 15447; -.
DR PRO; PR:P31025; -.
DR Bgee; P31025; -.
DR CleanEx; HS_LCN1; -.
DR Genevestigator; P31025; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0050909; P:sensory perception of taste; IEA:UniProtKB-KW.
DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR011038; Calycin-like.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR InterPro; IPR002450; von_Ebner_gland.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR01175; VNEBNERGLAND.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Reference proteome; Secreted; Sensory transduction;
KW Signal; Taste; Transport.
FT SIGNAL 1 18
FT CHAIN 19 176 Lipocalin-1.
FT /FTId=PRO_0000017974.
FT DISULFID 79 171
FT STRAND 33 42
FT STRAND 51 54
FT STRAND 57 61
FT STRAND 67 73
FT STRAND 80 88
FT STRAND 94 97
FT HELIX 98 100
FT STRAND 102 108
FT STRAND 114 121
FT STRAND 128 139
FT HELIX 145 154
FT STRAND 160 163
SQ SEQUENCE 176 AA; 19250 MW; 0DDBF124C8C78CB8 CRC64;
MKPLLLAVSL GLIAALQAHH LLASDEEIQD VSGTWYLKAM TVDREFPEMN LESVTPMTLT
TLEGGNLEAK VTMLISGRCQ EVKAVLEKTD EPGKYTADGG KHVAYIIRSH VKDHYIFYCE
GELHGKPVRG VKLVGRDPKN NLEALEDFEK AAGARGLSTE SILIPRQSET CSPGSD
//
MIM
151675
*RECORD*
*FIELD* NO
151675
*FIELD* TI
*151675 LIPOCALIN 1; LCN1
;;LIPOCALIN, TEAR;;
PREALBUMIN, TEAR;;
PROTEIN MIGRATING FASTER THAN ALBUMIN;;
read moreVON EBNER GLAND PROTEIN;;
VEG PROTEIN; VEGP
*FIELD* TX
GENE FAMILY
Lipocalins are a group of extracellular proteins, first described by
Pervaiz and Brew (1987), that are able to bind lipophiles by enclosure
within their structures, minimizing solvent contact. Based on the known
3-dimensional structure of 5 members of the lipocalin family, i.e.,
retinol binding protein (180250), beta-lactoglobulin (see 173310), bilin
binding protein, mouse major urinary protein, and rat urinary
alpha-2-globulin, the general architecture appears to be highly
appropriate for binding a variety of hydrophobic ligands. On the basis
of highly conserved amino acid sequences and of a size around 18 to 20
kD, about 20 proteins have been designated as lipocalins.
CLONING
In tear fluid, a group of 6 proteins with molecular weights ranging from
15 to 20 kD and various isoelectric points are abundant. The N-terminal
sequences of these proteins led Lassagne and Gachon (1993) to
hypothesize that they are isoforms and belong to the lipocalin family.
Redl et al. (1992) isolated and partially sequenced tear prealbumin.
Based on that sequence, the authors were able to clone a cDNA from a
lacrimal gland library predicted to encode a 176-amino acid protein that
shares 58% identity to the von Ebner gland protein of the rat and
significant homology with other lipocalins including beta lactoglobulin.
Northern blots probed with a radiolabeled N-terminal oligonucleotide
showed a 0.8-kb mRNA in human lacrimal gland mRNA. Redl et al. (1992)
predicted the tear prealbumin protein to be structurally similar to beta
lactoglobulin and showed it to bind radiolabeled retinol in vitro. From
genetic and biochemical data, they concluded that tear prealbumin is a
member of the lipophilic-ligand carrier protein superfamily. Though tear
prealbumin was originally described as a tear-specific protein, Redl et
al. (1992) showed that tear prealbumin-specific antiserum reacted with
human saliva, sweat, and nasal mucus proteins.
Von Ebner glands (VEG) are small lingual salivary glands. Their ducts
open into trenches of circumvallate and foliate papillae, and their
secretions influence the milieu where the interaction between taste
receptor cells and sapid molecules takes place. ('Sapid' means
'possessing taste.') The major secretion of human VEG is a protein with
a molecular mass of 18 kD. This VEG protein is identical to lipocalin-1.
Blaker et al. (1993) isolated a cDNA clone from a human VEG library and
showed that it contained an insert of 735 bp, including an open reading
frame that encodes the human VEG protein of 176 amino acids. The VEG
proteins are members of the lipocalin protein superfamily; together with
odorant-binding protein (164320), they constitute a new subfamily.
Sequence similarity to proteins such as retinol binding protein (e.g.,
180260) and odorant binding protein suggests a possible function for the
human VEG protein in taste perception.
Using Northern blotting and immunohistology, Holzfeind et al. (1996)
found that LCN1 is expressed in the human prostate. Cloning and
sequencing showed that the transcript is identical to that found in
tears. This finding suggested to Holzfeind et al. (1996) that the
lipocalin-1 protein is not specific to tears and saliva, as was
previously believed, but is multifunctional.
MAPPING
Using a clone from a cDNA library constructed from human lacrimal
glands, Lassagne et al. (1993) mapped the gene for tear lipocalin (LCN1)
to 9q34 by isotopic in situ hybridization. Five other members of the
lipocalin family mapped to the same region: orosomucoid (138600),
alpha-1-microglobulin (176870), progestagen-associated endometrial
protein (173310), the gamma chain of C8 (120930), and prostaglandin D2
synthase (176803). Chan et al. (1994) demonstrated by in situ
hybridization that the LCN1 gene, like several other genes in the
lipocalin superfamily, is located in 9q34. Chan et al. (1994) placed the
LCN1 gene close to the lipocalin-2 gene (600181). Since the locus
homologous to LCN2 is on mouse chromosome 2, the homolog of LCN1 may
also be located there. Contradictory results were obtained by
Baumgartner et al. (1994) who, using a genomic tear prealbumin probe,
mapped LCN1 to 8q24 by fluorescence in situ hybridization. The
contradictory results concerning localization of the LCN1 gene were
resolved by Herzog et al. (1995), who used hamster/human hybrid cells
for PCR experiments and demonstrated localization on chromosome 9.
Furthermore, Lassagne et al. (1995), using a panel of hybrid cell lines
that had been generated and characterized by Nguyen Van Cong et al.
(1986) and Glasgow et al. (1993), likewise assigned it to 9q34-qter by
somatic cell hybrid analysis.
Lacazette et al. (1997) reported a dinucleotide repeat microsatellite
marker (D9S1826) close to the LCN1 gene. Using the CEPH reference
families, they located the LCN1 gene within the 9q34 genetic map between
D9S23 and D9S158.
GENE FUNCTION
Van't Hof et al. (1997) showed that LCN1 inhibits the cysteine-protease
papain in vitro, similar to cystatins (see 123857). They suggested that
LCN1 plays a role in the nonimmunologic defense and in the control of
inflammatory processes in oral and ocular tissues.
Redl et al. (1998) found enhanced LCN1 secretion in the airways of
patients with cystic fibrosis (CF; 219700). Northern blot analysis of
RNA from normal trachea and RNA isolated from tracheal biopsies of
patients with CF indicated that the enhanced secretion was due to an
upregulated expression of the LCN1 gene. Thus, the investigations
presented the first clear evidence that LCN1 is induced in infection or
inflammation and supported the idea that this lipocalin functions as a
physiologic protection factor of epithelia in vivo.
*FIELD* RF
1. Baumgartner, M.; Holzfeind, P.; Redl, B.: Assignment of the gene
for human tear prealbumin (LCN1), a member of the lipocalin superfamily,
to chromosome 8q24. Cytogenet. Cell Genet. 65: 101-103, 1994.
2. 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 1172: 131-137, 1993.
3. Chan, P.; Simon-Chazottes, D.; Mattei, M. G.; Guenet, J. L.; Salier,
J. P.: Comparative mapping of lipocalin genes in human and mouse:
the four genes for complement C8 gamma chain, prostaglandin-D-synthase,
oncogene-24P3, and progestagen-associated endometrial protein map
to HSA9 and MMU2. Genomics 23: 145-150, 1994.
4. Glasgow, B. J.; Heinzmann, C.; Kojis, T.; Sparkes, R. S.; Mohandas,
T.; Bateman, J. B.: Assignment of tear lipocalin gene to human chromosome
9q34-9qter. Curr. Eye Res. 12: 1019-1023, 1993.
5. Herzog, H.; Baumgartner, M.; Holzfeind, P.; Redl, B.: Confirmation
of 9q34 as the chromosomal site of the human lipocalin LCN1 gene. Cytogenet.
Cell Genet. 69: 108-109, 1995.
6. Holzfeind, P.; Merschak, P.; Rogatsch, H.; Culig, Z.; Feichtinger,
H.; Klocker, H.; Redl, B.: Expression of the gene for tear lipocalin/von
Ebner's gland protein in human prostate. FEBS Lett. 395: 95-98,
1996.
7. Lacazette, E.; Pitiot, G.; Jobert, S.; Mallet, J.; Gachon, A. M.
F.: Fine genetic mapping of LCN1/D9S1826 within 9q34. Ann. Hum.
Genet. 61: 449-455, 1997.
8. Lassagne, H.; Gachon, A. M. F.: Cloning of a human lacrimal lipocalin
secreted in tears. Exp. Eye Res. 56: 605-609, 1993.
9. Lassagne, H.; Nguyen, V. C.; Mattei, M. G.; Gachon, A. M. F.:
Assignment of LCN1 to human chromosome 9 is confirmed. Cytogent.
Cell Genet. 71: 104, 1995.
10. Lassagne, H.; Ressot, C.; Mattei, M. G.; Gachon, A. M. F.: Assignment
of the human tear lipocalin gene (LCN1) to 9q34 by in situ hybridization. Genomics 18:
160-161, 1993.
11. Nguyen Van Cong; Weil, D.; Finaz, C.; Cohen-Haguenauer, O.; Gross,
M.-S.; Jegou-Foubert, C.; de Tand, M.-F.; Cochet, C.; de Grouchy,
J.; Frezal, J.: Panel of twenty-five independent man-rodent hybrids
for human genetic marker mapping. Ann. Genet. 29: 20-26, 1986.
12. Pervaiz, S.; Brew, K.: Homology and structure-function correlations
between alpha-1-acid glycoprotein and serum retinol-binding protein
and its relatives. FASEB J. 1: 209-214, 1987.
13. 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. 28: 20282-20287, 1992.
14. Redl, B.; Wojnar, P.; Ellemunter, H.; Feichtinger, H.: Identification
of a lipocalin in mucosal glands of the human tracheobronchial tree
and its enhanced secretion in cystic fibrosis. Lab. Invest. 78:
1121-1129, 1998.
15. van't Hof, W.; Blankenvoorde, M. F. J.; Veerman, E. C. I.; Nieuw
Amerongen, A. V.: The salivary lipocalin Von Ebner's Gland protein
is a cysteine proteinase inhibitor. J. Biol. Chem. 272: 1837-1841,
1997.
*FIELD* CN
Victor A. McKusick - updated: 9/15/1999
Rebekah S. Rasooly - updated: 4/7/1998
Victor A. McKusick - updated: 3/30/1998
Jennifer P. Macke - updated: 10/10/1997
Alan F. Scott - updated: 4/17/1996
*FIELD* CD
Victor A. McKusick: 10/15/1993
*FIELD* ED
carol: 08/09/2010
carol: 10/4/1999
jlewis: 9/28/1999
terry: 9/15/1999
psherman: 5/1/1998
psherman: 4/7/1998
alopez: 3/30/1998
terry: 3/25/1998
alopez: 10/10/1997
alopez: 10/3/1997
terry: 7/8/1997
alopez: 6/2/1997
mark: 4/17/1996
mark: 10/25/1995
pfoster: 3/3/1995
terry: 11/7/1994
jason: 7/14/1994
carol: 12/22/1993
carol: 12/16/1993
*RECORD*
*FIELD* NO
151675
*FIELD* TI
*151675 LIPOCALIN 1; LCN1
;;LIPOCALIN, TEAR;;
PREALBUMIN, TEAR;;
PROTEIN MIGRATING FASTER THAN ALBUMIN;;
read moreVON EBNER GLAND PROTEIN;;
VEG PROTEIN; VEGP
*FIELD* TX
GENE FAMILY
Lipocalins are a group of extracellular proteins, first described by
Pervaiz and Brew (1987), that are able to bind lipophiles by enclosure
within their structures, minimizing solvent contact. Based on the known
3-dimensional structure of 5 members of the lipocalin family, i.e.,
retinol binding protein (180250), beta-lactoglobulin (see 173310), bilin
binding protein, mouse major urinary protein, and rat urinary
alpha-2-globulin, the general architecture appears to be highly
appropriate for binding a variety of hydrophobic ligands. On the basis
of highly conserved amino acid sequences and of a size around 18 to 20
kD, about 20 proteins have been designated as lipocalins.
CLONING
In tear fluid, a group of 6 proteins with molecular weights ranging from
15 to 20 kD and various isoelectric points are abundant. The N-terminal
sequences of these proteins led Lassagne and Gachon (1993) to
hypothesize that they are isoforms and belong to the lipocalin family.
Redl et al. (1992) isolated and partially sequenced tear prealbumin.
Based on that sequence, the authors were able to clone a cDNA from a
lacrimal gland library predicted to encode a 176-amino acid protein that
shares 58% identity to the von Ebner gland protein of the rat and
significant homology with other lipocalins including beta lactoglobulin.
Northern blots probed with a radiolabeled N-terminal oligonucleotide
showed a 0.8-kb mRNA in human lacrimal gland mRNA. Redl et al. (1992)
predicted the tear prealbumin protein to be structurally similar to beta
lactoglobulin and showed it to bind radiolabeled retinol in vitro. From
genetic and biochemical data, they concluded that tear prealbumin is a
member of the lipophilic-ligand carrier protein superfamily. Though tear
prealbumin was originally described as a tear-specific protein, Redl et
al. (1992) showed that tear prealbumin-specific antiserum reacted with
human saliva, sweat, and nasal mucus proteins.
Von Ebner glands (VEG) are small lingual salivary glands. Their ducts
open into trenches of circumvallate and foliate papillae, and their
secretions influence the milieu where the interaction between taste
receptor cells and sapid molecules takes place. ('Sapid' means
'possessing taste.') The major secretion of human VEG is a protein with
a molecular mass of 18 kD. This VEG protein is identical to lipocalin-1.
Blaker et al. (1993) isolated a cDNA clone from a human VEG library and
showed that it contained an insert of 735 bp, including an open reading
frame that encodes the human VEG protein of 176 amino acids. The VEG
proteins are members of the lipocalin protein superfamily; together with
odorant-binding protein (164320), they constitute a new subfamily.
Sequence similarity to proteins such as retinol binding protein (e.g.,
180260) and odorant binding protein suggests a possible function for the
human VEG protein in taste perception.
Using Northern blotting and immunohistology, Holzfeind et al. (1996)
found that LCN1 is expressed in the human prostate. Cloning and
sequencing showed that the transcript is identical to that found in
tears. This finding suggested to Holzfeind et al. (1996) that the
lipocalin-1 protein is not specific to tears and saliva, as was
previously believed, but is multifunctional.
MAPPING
Using a clone from a cDNA library constructed from human lacrimal
glands, Lassagne et al. (1993) mapped the gene for tear lipocalin (LCN1)
to 9q34 by isotopic in situ hybridization. Five other members of the
lipocalin family mapped to the same region: orosomucoid (138600),
alpha-1-microglobulin (176870), progestagen-associated endometrial
protein (173310), the gamma chain of C8 (120930), and prostaglandin D2
synthase (176803). Chan et al. (1994) demonstrated by in situ
hybridization that the LCN1 gene, like several other genes in the
lipocalin superfamily, is located in 9q34. Chan et al. (1994) placed the
LCN1 gene close to the lipocalin-2 gene (600181). Since the locus
homologous to LCN2 is on mouse chromosome 2, the homolog of LCN1 may
also be located there. Contradictory results were obtained by
Baumgartner et al. (1994) who, using a genomic tear prealbumin probe,
mapped LCN1 to 8q24 by fluorescence in situ hybridization. The
contradictory results concerning localization of the LCN1 gene were
resolved by Herzog et al. (1995), who used hamster/human hybrid cells
for PCR experiments and demonstrated localization on chromosome 9.
Furthermore, Lassagne et al. (1995), using a panel of hybrid cell lines
that had been generated and characterized by Nguyen Van Cong et al.
(1986) and Glasgow et al. (1993), likewise assigned it to 9q34-qter by
somatic cell hybrid analysis.
Lacazette et al. (1997) reported a dinucleotide repeat microsatellite
marker (D9S1826) close to the LCN1 gene. Using the CEPH reference
families, they located the LCN1 gene within the 9q34 genetic map between
D9S23 and D9S158.
GENE FUNCTION
Van't Hof et al. (1997) showed that LCN1 inhibits the cysteine-protease
papain in vitro, similar to cystatins (see 123857). They suggested that
LCN1 plays a role in the nonimmunologic defense and in the control of
inflammatory processes in oral and ocular tissues.
Redl et al. (1998) found enhanced LCN1 secretion in the airways of
patients with cystic fibrosis (CF; 219700). Northern blot analysis of
RNA from normal trachea and RNA isolated from tracheal biopsies of
patients with CF indicated that the enhanced secretion was due to an
upregulated expression of the LCN1 gene. Thus, the investigations
presented the first clear evidence that LCN1 is induced in infection or
inflammation and supported the idea that this lipocalin functions as a
physiologic protection factor of epithelia in vivo.
*FIELD* RF
1. Baumgartner, M.; Holzfeind, P.; Redl, B.: Assignment of the gene
for human tear prealbumin (LCN1), a member of the lipocalin superfamily,
to chromosome 8q24. Cytogenet. Cell Genet. 65: 101-103, 1994.
2. 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 1172: 131-137, 1993.
3. Chan, P.; Simon-Chazottes, D.; Mattei, M. G.; Guenet, J. L.; Salier,
J. P.: Comparative mapping of lipocalin genes in human and mouse:
the four genes for complement C8 gamma chain, prostaglandin-D-synthase,
oncogene-24P3, and progestagen-associated endometrial protein map
to HSA9 and MMU2. Genomics 23: 145-150, 1994.
4. Glasgow, B. J.; Heinzmann, C.; Kojis, T.; Sparkes, R. S.; Mohandas,
T.; Bateman, J. B.: Assignment of tear lipocalin gene to human chromosome
9q34-9qter. Curr. Eye Res. 12: 1019-1023, 1993.
5. Herzog, H.; Baumgartner, M.; Holzfeind, P.; Redl, B.: Confirmation
of 9q34 as the chromosomal site of the human lipocalin LCN1 gene. Cytogenet.
Cell Genet. 69: 108-109, 1995.
6. Holzfeind, P.; Merschak, P.; Rogatsch, H.; Culig, Z.; Feichtinger,
H.; Klocker, H.; Redl, B.: Expression of the gene for tear lipocalin/von
Ebner's gland protein in human prostate. FEBS Lett. 395: 95-98,
1996.
7. Lacazette, E.; Pitiot, G.; Jobert, S.; Mallet, J.; Gachon, A. M.
F.: Fine genetic mapping of LCN1/D9S1826 within 9q34. Ann. Hum.
Genet. 61: 449-455, 1997.
8. Lassagne, H.; Gachon, A. M. F.: Cloning of a human lacrimal lipocalin
secreted in tears. Exp. Eye Res. 56: 605-609, 1993.
9. Lassagne, H.; Nguyen, V. C.; Mattei, M. G.; Gachon, A. M. F.:
Assignment of LCN1 to human chromosome 9 is confirmed. Cytogent.
Cell Genet. 71: 104, 1995.
10. Lassagne, H.; Ressot, C.; Mattei, M. G.; Gachon, A. M. F.: Assignment
of the human tear lipocalin gene (LCN1) to 9q34 by in situ hybridization. Genomics 18:
160-161, 1993.
11. Nguyen Van Cong; Weil, D.; Finaz, C.; Cohen-Haguenauer, O.; Gross,
M.-S.; Jegou-Foubert, C.; de Tand, M.-F.; Cochet, C.; de Grouchy,
J.; Frezal, J.: Panel of twenty-five independent man-rodent hybrids
for human genetic marker mapping. Ann. Genet. 29: 20-26, 1986.
12. Pervaiz, S.; Brew, K.: Homology and structure-function correlations
between alpha-1-acid glycoprotein and serum retinol-binding protein
and its relatives. FASEB J. 1: 209-214, 1987.
13. 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. 28: 20282-20287, 1992.
14. Redl, B.; Wojnar, P.; Ellemunter, H.; Feichtinger, H.: Identification
of a lipocalin in mucosal glands of the human tracheobronchial tree
and its enhanced secretion in cystic fibrosis. Lab. Invest. 78:
1121-1129, 1998.
15. van't Hof, W.; Blankenvoorde, M. F. J.; Veerman, E. C. I.; Nieuw
Amerongen, A. V.: The salivary lipocalin Von Ebner's Gland protein
is a cysteine proteinase inhibitor. J. Biol. Chem. 272: 1837-1841,
1997.
*FIELD* CN
Victor A. McKusick - updated: 9/15/1999
Rebekah S. Rasooly - updated: 4/7/1998
Victor A. McKusick - updated: 3/30/1998
Jennifer P. Macke - updated: 10/10/1997
Alan F. Scott - updated: 4/17/1996
*FIELD* CD
Victor A. McKusick: 10/15/1993
*FIELD* ED
carol: 08/09/2010
carol: 10/4/1999
jlewis: 9/28/1999
terry: 9/15/1999
psherman: 5/1/1998
psherman: 4/7/1998
alopez: 3/30/1998
terry: 3/25/1998
alopez: 10/10/1997
alopez: 10/3/1997
terry: 7/8/1997
alopez: 6/2/1997
mark: 4/17/1996
mark: 10/25/1995
pfoster: 3/3/1995
terry: 11/7/1994
jason: 7/14/1994
carol: 12/22/1993
carol: 12/16/1993