LCN1_PIG
ID LCN1_PIG Reviewed; 176 AA.
AC P53715; O19136;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 100.
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;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7796060; DOI=10.1093/chemse/20.1.69;
RA Garibotti M., Christiansen H., Schmale H., Pelosi P.;
RT "Porcine VEG proteins and tear prealbumins.";
RL Chem. Senses 20:69-76(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=9427546; DOI=10.1016/s0378-1119(97)00454-x;
RA Holzfeind P., Merschak P., Wojnar P., Redl B.;
RT "Structure and organization of the porcine LCN1 gene encoding tear
RT lipocalin/von Ebner's gland protein.";
RL Gene 202:61-67(1997).
CC -!- FUNCTION: Could play a role in taste reception. Could be necessary for
CC the concentration and delivery of sapid molecules in the gustatory
CC system. Can bind various ligands, with chemical structures ranging from
CC lipids and retinoids to the macrocyclic antibiotic rifampicin and even
CC to microbial siderophores. Exhibits an extremely wide ligand pocket (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Predominantly monomer (By similarity). May form homodimer (By
CC similarity). Interacts with LMBR1L; this interaction mediates the
CC endocytosis of LCN1 (By similarity). {ECO:0000250|UniProtKB:P31025}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S77587; AAB34720.1; -; mRNA.
DR EMBL; U96150; AAC39166.1; -; Genomic_DNA.
DR PIR; JC6503; JC6503.
DR RefSeq; NP_999021.2; NM_213856.2.
DR AlphaFoldDB; P53715; -.
DR SMR; P53715; -.
DR iPTMnet; P53715; -.
DR PeptideAtlas; P53715; -.
DR Ensembl; ENSSSCT00045055016; ENSSSCP00045038345; ENSSSCG00045032182.
DR Ensembl; ENSSSCT00070010794; ENSSSCP00070008883; ENSSSCG00070005682.
DR GeneID; 396861; -.
DR KEGG; ssc:396861; -.
DR CTD; 29989; -.
DR InParanoid; P53715; -.
DR OrthoDB; 1450978at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0050909; P:sensory perception of taste; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR002345; Lipocalin.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR InterPro; IPR002450; von_Ebner_gland.
DR PANTHER; PTHR11430; PTHR11430; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR01175; VNEBNERGLAND.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Reference proteome; Secreted;
KW Sensory transduction; Signal; Taste; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..176
FT /note="Lipocalin-1"
FT /id="PRO_0000017975"
FT DISULFID 80..171
FT /evidence="ECO:0000250"
FT CONFLICT 136
FT /note="G -> A (in Ref. 2; AAC39166)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 176 AA; 19352 MW; BB7D6D750D4AC4AB CRC64;
MMRALLLAIG LGLVAALQAQ EFPAVGQPLQ DLLGRWYLKA MTSDPEIPGK KPESVTPLIL
KALEGGDLEA QITFLIDGQC QDVTLVLKKT NQPFTFTAYD GKRVVYILPS KVKDHYILYC
EGELDGQEVR MAKLVGRDPE NNPEALEEFK EVARAKGLNP DIVRPQQSET CSPGGN
