ALL2_BOVIN
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 03-AUG-2022, entry version 132.
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; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC 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., Pelkonen J.,
RA Rautiainen J., Virtanen T.;
RT "Complementary DNA cloning of the predominant allergen of bovine dander: a
RT 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 of the
RT bovine lipocalin allergen Bos d 2.";
RL J. Biol. Chem. 274:2337-2343(1999).
RN [4]
RP CHARACTERIZATION, CRYSTALLIZATION, AND PYROGLUTAMATE FORMATION AT 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 the
RT 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 glands
CC and transported to the skin surface. {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}.
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DR EMBL; L42867; AAB08720.1; -; mRNA.
DR PIR; A59225; A59225.
DR PIR; B59225; B59225.
DR RefSeq; NP_777186.1; NM_174761.2.
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 AlphaFoldDB; 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 Ensembl; ENSBTAT00000073049; ENSBTAP00000070507; ENSBTAG00000016820.
DR GeneID; 286791; -.
DR KEGG; bta:286791; -.
DR CTD; 286791; -.
DR VEuPathDB; HostDB:ENSBTAG00000016820; -.
DR eggNOG; ENOG502TDZD; Eukaryota.
DR GeneTree; ENSGT01050000244868; -.
DR HOGENOM; CLU_094061_4_2_1; -.
DR InParanoid; Q28133; -.
DR OMA; RVECIND; -.
DR OrthoDB; 1357921at2759; -.
DR TreeFam; TF338197; -.
DR EvolutionaryTrace; Q28133; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000016820; Expressed in zone of skin and 31 other tissues.
DR ExpressionAtlas; Q28133; baseline and differential.
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 Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR002345; Lipocalin.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Disulfide bond; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..16
FT CHAIN 17..172
FT /note="Allergen Bos d 2"
FT /id="PRO_0000017983"
FT MOD_RES 17
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:9647765"
FT DISULFID 60..64
FT DISULFID 79..170
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:4WFV"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1BJ7"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:4WFV"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:4WFV"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:4WFV"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:4WFV"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:4WFV"
FT STRAND 78..90
FT /evidence="ECO:0007829|PDB:4WFV"
FT STRAND 93..109
FT /evidence="ECO:0007829|PDB:4WFV"
FT STRAND 111..121
FT /evidence="ECO:0007829|PDB:4WFV"
FT STRAND 126..138
FT /evidence="ECO:0007829|PDB:4WFV"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:4WFV"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:4WFV"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4WFU"
FT HELIX 165..167
FT /evidence="ECO:0007829|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
