ID   OBP_BOVIN               Reviewed;         159 AA.
AC   P07435;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 2.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Odorant-binding protein;
DE            Short=OBP;
DE   AltName: Full=Olfactory mucosa pyrazine-binding protein;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2512125; DOI=10.1111/j.1432-1033.1989.tb15151.x;
RA   Tirindelli R., Keen J.N., Cavaggioni A., Eliopoulos E.E., Findlay J.B.C.;
RT   "Complete amino acid sequence of pyrazine-binding protein from cow nasal
RT   mucosa.";
RL   Eur. J. Biochem. 185:569-572(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-63.
RX   PubMed=3817156; DOI=10.1016/0014-5793(87)81349-2;
RA   Cavaggioni A., Sorbi R.T., Keen J.N., Pappin D.J.C., Findlay J.B.C.;
RT   "Homology between the pyrazine-binding protein from nasal mucosa and major
RT   urinary proteins.";
RL   FEBS Lett. 212:225-228(1987).
RN   [3]
RP   COMPARISON OF X-RAY STRUCTURES.
RX   PubMed=1623143; DOI=10.1002/bip.360320425;
RA   Monaco H.L., Zanotti G.;
RT   "Three-dimensional structure and active site of three hydrophobic molecule-
RT   binding proteins with significant amino acid sequence similarity.";
RL   Biopolymers 32:457-465(1992).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=8901871; DOI=10.1038/nsb1196-934;
RA   Bianchet M.A., Bains G., Pelosi P., Pevsner J., Snyder S.H., Monaco H.L.,
RA   Amzel L.M.;
RT   "The three-dimensional structure of bovine odorant binding protein and its
RT   mechanism of odor recognition.";
RL   Nat. Struct. Biol. 3:934-939(1996).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=8836103; DOI=10.1038/nsb1096-863;
RA   Tegoni M., Ramoni R., Bignetti E., Spinelli S., Cambillau C.;
RT   "Domain swapping creates a third putative combining site in bovine odorant
RT   binding protein dimer.";
RL   Nat. Struct. Biol. 3:863-867(1996).
CC   -!- FUNCTION: This protein binds a wide variety of chemical odorants.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
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DR   PIR; S06843; S06843.
DR   PDB; 1G85; X-ray; 1.80 A; A/B=1-159.
DR   PDB; 1GT1; X-ray; 1.71 A; A/B=1-159.
DR   PDB; 1GT3; X-ray; 1.80 A; A/B=1-159.
DR   PDB; 1GT4; X-ray; 2.10 A; A/B=1-159.
DR   PDB; 1GT5; X-ray; 2.08 A; A/B=1-159.
DR   PDB; 1HN2; X-ray; 1.80 A; A/B=1-159.
DR   PDB; 1OBP; X-ray; 2.00 A; A/B=1-159.
DR   PDB; 1PBO; X-ray; 2.20 A; A/B=1-159.
DR   PDB; 2HLV; X-ray; 1.65 A; A=1-159.
DR   PDBsum; 1G85; -.
DR   PDBsum; 1GT1; -.
DR   PDBsum; 1GT3; -.
DR   PDBsum; 1GT4; -.
DR   PDBsum; 1GT5; -.
DR   PDBsum; 1HN2; -.
DR   PDBsum; 1OBP; -.
DR   PDBsum; 1PBO; -.
DR   PDBsum; 2HLV; -.
DR   AlphaFoldDB; P07435; -.
DR   SMR; P07435; -.
DR   STRING; 9913.ENSBTAP00000022593; -.
DR   PaxDb; P07435; -.
DR   eggNOG; ENOG502TDZD; Eukaryota.
DR   EvolutionaryTrace; P07435; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005549; F:odorant binding; IBA:GO_Central.
DR   GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR002345; Lipocalin.
DR   InterPro; IPR022272; Lipocalin_CS.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   InterPro; IPR002448; OBP-like.
DR   PANTHER; PTHR11430; PTHR11430; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR01173; ODORANTBNDNG.
DR   SUPFAM; SSF50814; SSF50814; 1.
DR   PROSITE; PS00213; LIPOCALIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Olfaction; Reference proteome;
KW   Secreted; Sensory transduction; Transport.
FT   CHAIN           1..159
FT                   /note="Odorant-binding protein"
FT                   /id="PRO_0000201024"
FT   HELIX           11..13
FT                   /evidence="ECO:0007829|PDB:1GT1"
FT   STRAND          18..26
FT                   /evidence="ECO:0007829|PDB:2HLV"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:2HLV"
FT   STRAND          39..46
FT                   /evidence="ECO:0007829|PDB:2HLV"
FT   TURN            47..50
FT                   /evidence="ECO:0007829|PDB:2HLV"
FT   STRAND          51..60
FT                   /evidence="ECO:0007829|PDB:2HLV"
FT   STRAND          63..73
FT                   /evidence="ECO:0007829|PDB:2HLV"
FT   STRAND          79..94
FT                   /evidence="ECO:0007829|PDB:2HLV"
FT   STRAND          96..106
FT                   /evidence="ECO:0007829|PDB:2HLV"
FT   STRAND          112..120
FT                   /evidence="ECO:0007829|PDB:2HLV"
FT   HELIX           126..138
FT                   /evidence="ECO:0007829|PDB:2HLV"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:2HLV"
FT   STRAND          146..148
FT                   /evidence="ECO:0007829|PDB:2HLV"
FT   HELIX           149..154
FT                   /evidence="ECO:0007829|PDB:1PBO"
SQ   SEQUENCE   159 AA;  18503 MW;  338F5EBF1D03D4A8 CRC64;
     AQEEEAEQNL SELSGPWRTV YIGSTNPEKI QENGPFRTYF RELVFDDEKG TVDFYFSVKR
     DGKWKNVHVK ATKQDDGTYV ADYEGQNVFK IVSLSRTHLV AHNINVDKHG QTTELTELFV
     KLNVEDEDLE KFWKLTEDKG IDKKNVVNFL ENEDHPHPE