ID   LCN1_HUMAN              Reviewed;         176 AA.
AC   P31025; Q5T8A1;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   09-JUL-2014, entry version 140.
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.
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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   CCDS; CCDS6991.1; -.
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=23-176.
DR   PDB; 3EYC; X-ray; 2.60 A; A/B/C/D=23-176.
DR   PDBsum; 1XKI; -.
DR   PDBsum; 3EYC; -.
DR   DisProt; DP00647; -.
DR   ProteinModelPortal; P31025; -.
DR   SMR; P31025; 31-173.
DR   BioGrid; 110125; 5.
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   MaxQB; 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; SGRCQEV; -.
DR   OrthoDB; EOG7GXPD6; -.
DR   PhylomeDB; P31025; -.
DR   TreeFam; TF338197; -.
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:0005615; C:extracellular space; IDA:UniProt.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; TAS:ProtInc.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; TAS:GOC.
DR   GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0001895; P:retina homeostasis; IEP:UniProt.
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.
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
//