ID ALL2_BOVIN Reviewed; 172 AA. AC Q28133; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 25-OCT-2017, entry version 110. DE RecName: Full=Allergen Bos d 2; DE AltName: Full=Dander major allergen BDA20; DE AltName: Full=Dermal allergen BDA20; DE AltName: Allergen=Bos d 2; DE Flags: Precursor; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN. RC TISSUE=Skin; RX PubMed=8648026; DOI=10.1016/S0091-6749(96)70198-7; RA Maentyjaervi R., Parkkinen S., Rytkoenen M., Pentikaeinen J., RA Pelkonen J., Rautiainen J., Virtanen T.; RT "Complementary DNA cloning of the predominant allergen of bovine RT dander: a new member in the lipocalin family."; RL J. Allergy Clin. Immunol. 97:1297-1303(1996). RN [2] RP 3D-STRUCTURE MODELING. RX PubMed=9853680; DOI=10.1007/BF02780967; RA Santa H., Saarela J.T., Laatikainen R., Rautiainen J., Virtanen T., RA Rytkonen M., Maentyjaervi R.; RT "A bovine dander allergen, comparative modeling, and similarities and RT differences in folding with related proteins."; RL J. Protein Chem. 17:657-662(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX PubMed=9891000; DOI=10.1074/jbc.274.4.2337; RA Rouvinen J., Rautiainen J., Virtanen T., Zeiler T., Kauppinen J., RA Taivainen A., Maentyjaervi R.; RT "Probing the molecular basis of allergy. three-dimensional structure RT of the bovine lipocalin allergen Bos d 2."; RL J. Biol. Chem. 274:2337-2343(1999). RN [4] RP CHARACTERIZATION, CRYSTALLIZATION, AND PYROGLUTAMATE FORMATION AT RP GLN-17. RX PubMed=9647765; DOI=10.1006/bbrc.1998.8851; RA Rautiainen J., Auriola S., Rouvinen J., Kauppinen J., Zeiler T., RA Novikov D., Virtanen T., Maentyjaervi R.A.; RT "Molecular and crystal properties of Bos d 2, an allergenic protein of RT the lipocalin family."; RL Biochem. Biophys. Res. Commun. 247:746-750(1998). RN [5] RP TISSUE SPECIFICITY. RX PubMed=9525451; DOI=10.1016/S0091-6749(98)70247-7; RA Rautiainen J., Rytkoenen M., Syrjaenen K., Pentikaeinen J., Zeiler T., RA Virtanen T., Maentyjaervi R.; RT "Tissue localization of bovine dander allergen Bos d 2."; RL J. Allergy Clin. Immunol. 101:349-353(1998). CC -!- FUNCTION: Probable pheromone carrier. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Found exclusively in skin. Produced in sweat CC glands and transported to the skin surface. CC {ECO:0000269|PubMed:9525451}. CC -!- ALLERGEN: Causes an allergic reaction in human. Potent allergen of CC bovine dander. {ECO:0000269|PubMed:8648026}. 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; L42867; AAB08720.1; -; mRNA. DR PIR; A59225; A59225. DR PIR; B59225; B59225. DR RefSeq; NP_777186.1; NM_174761.2. DR UniGene; Bt.550; -. DR PDB; 1BJ7; X-ray; 1.80 A; A=17-172. DR PDB; 4WFU; X-ray; 1.75 A; A=17-172. DR PDB; 4WFV; X-ray; 1.40 A; A=17-172. DR PDBsum; 1BJ7; -. DR PDBsum; 4WFU; -. DR PDBsum; 4WFV; -. DR ProteinModelPortal; Q28133; -. DR SMR; Q28133; -. DR STRING; 9913.ENSBTAP00000022376; -. DR Allergome; 158; Bos d 2. DR Allergome; 159; Bos d 2.0101. DR Allergome; 160; Bos d 2.0102. DR Allergome; 161; Bos d 2.0103. DR PaxDb; Q28133; -. DR PRIDE; Q28133; -. DR Ensembl; ENSBTAT00000022376; ENSBTAP00000022376; ENSBTAG00000016820. DR GeneID; 286791; -. DR KEGG; bta:286791; -. DR CTD; 286791; -. DR eggNOG; ENOG410JFM0; Eukaryota. DR eggNOG; ENOG4111E4N; LUCA. DR GeneTree; ENSGT00730000111347; -. DR HOVERGEN; HBG098951; -. DR InParanoid; Q28133; -. DR OMA; YYRRIEC; -. DR OrthoDB; EOG091G0PVJ; -. DR TreeFam; TF338197; -. DR EvolutionaryTrace; Q28133; -. DR Proteomes; UP000009136; Chromosome X. DR Bgee; ENSBTAG00000016820; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005549; F:odorant binding; IEA:InterPro. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR Gene3D; 2.40.128.20; -; 1. DR InterPro; IPR012674; Calycin. DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom. DR InterPro; IPR002448; Odour-bd. DR Pfam; PF00061; Lipocalin; 1. DR PRINTS; PR01173; ODORANTBNDNG. DR SUPFAM; SSF50814; SSF50814; 1. PE 1: Evidence at protein level; KW 3D-structure; Allergen; Complete proteome; Disulfide bond; KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal; KW Transport. FT SIGNAL 1 16 FT CHAIN 17 172 Allergen Bos d 2. FT /FTId=PRO_0000017983. FT MOD_RES 17 17 Pyrrolidone carboxylic acid. FT {ECO:0000269|PubMed:9647765}. FT DISULFID 60 64 FT DISULFID 79 170 FT HELIX 25 27 {ECO:0000244|PDB:4WFV}. FT STRAND 28 31 {ECO:0000244|PDB:1BJ7}. FT STRAND 33 41 {ECO:0000244|PDB:4WFV}. FT HELIX 42 44 {ECO:0000244|PDB:4WFV}. FT STRAND 54 61 {ECO:0000244|PDB:4WFV}. FT TURN 62 65 {ECO:0000244|PDB:4WFV}. FT STRAND 66 75 {ECO:0000244|PDB:4WFV}. FT STRAND 78 90 {ECO:0000244|PDB:4WFV}. FT STRAND 93 109 {ECO:0000244|PDB:4WFV}. FT STRAND 111 121 {ECO:0000244|PDB:4WFV}. FT STRAND 126 138 {ECO:0000244|PDB:4WFV}. FT HELIX 141 153 {ECO:0000244|PDB:4WFV}. FT HELIX 158 160 {ECO:0000244|PDB:4WFV}. FT STRAND 161 163 {ECO:0000244|PDB:4WFU}. FT HELIX 165 167 {ECO:0000244|PDB:4WFV}. SQ SEQUENCE 172 AA; 19560 MW; C50F66F1B3D98156 CRC64; MKAVFLTLLF GLVCTAQETP AEIDPSKIPG EWRIIYAAAD NKDKIVEGGP LRNYYRRIEC INDCESLSIT FYLKDQGTCL LLTEVAKRQE GYVYVLEFYG TNTLEVIHVS ENMLVTYVEN YDGERITKMT EGLAKGTSFT PEELEKYQQL NSERGVPNEN IENLIKTDNC PP //