ALL2_CANLF
ID ALL2_CANLF Reviewed; 180 AA.
AC O18874;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Minor allergen Can f 2;
DE AltName: Full=Allergen Dog 2;
DE AltName: Allergen=Can f 2;
DE Flags: Precursor;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RX PubMed=9497502; DOI=10.1046/j.1365-2567.1997.00386.x;
RA Konieczny A., Morgenstern J.P., Bizinkauskas C.B., Lilley C.H.,
RA Brauer A.W., Bond J.F., Aalberse R.C., Wallner B.P., Kasaian M.T.;
RT "The major dog allergens, Can f 1 and Can f 2, are salivary lipocalin
RT proteins: cloning and immunological characterization of the recombinant
RT forms.";
RL Immunology 92:577-586(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 20-180, AND DISULFIDE BOND.
RX PubMed=20621650; DOI=10.1016/j.jmb.2010.05.043;
RA Madhurantakam C., Nilsson O.B., Uchtenhagen H., Konradsen J., Saarne T.,
RA Hogbom E., Sandalova T., Gronlund H., Achour A.;
RT "Crystal structure of the dog lipocalin allergen Can f 2: implications for
RT cross-reactivity to the cat allergen Fel d 4.";
RL J. Mol. Biol. 401:68-83(2010).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Tongue epithelial tissue and parotid gland.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC {ECO:0000269|PubMed:9497502}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; AF027178; AAC48795.1; -; mRNA.
DR RefSeq; NP_001003189.1; NM_001003189.2.
DR PDB; 3L4R; X-ray; 1.45 A; A=20-180.
DR PDBsum; 3L4R; -.
DR AlphaFoldDB; O18874; -.
DR SMR; O18874; -.
DR STRING; 9612.ENSCAFP00000029233; -.
DR Allergome; 175; Can f 2.
DR Allergome; 3170; Can f 2.0101.
DR PaxDb; O18874; -.
DR Ensembl; ENSCAFT00040001182; ENSCAFP00040001004; ENSCAFG00040000664.
DR Ensembl; ENSCAFT00845015896; ENSCAFP00845012369; ENSCAFG00845008996.
DR GeneID; 403829; -.
DR KEGG; cfa:403829; -.
DR CTD; 403829; -.
DR VEuPathDB; HostDB:ENSCAFG00845008996; -.
DR eggNOG; ENOG502TJKQ; Eukaryota.
DR GeneTree; ENSGT01050000244868; -.
DR HOGENOM; CLU_094061_4_0_1; -.
DR InParanoid; O18874; -.
DR OMA; NVTYFHR; -.
DR OrthoDB; 1553933at2759; -.
DR TreeFam; TF338197; -.
DR EvolutionaryTrace; O18874; -.
DR Proteomes; UP000002254; Chromosome 9.
DR Bgee; ENSCAFG00000019749; Expressed in saliva-secreting gland and 9 other tissues.
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; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR InterPro; IPR002971; Maj_urinary.
DR PANTHER; PTHR11430; PTHR11430; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR01221; MAJORURINARY.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..180
FT /note="Minor allergen Can f 2"
FT /id="PRO_0000017981"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 82..175
FT /evidence="ECO:0000269|PubMed:20621650"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:3L4R"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:3L4R"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3L4R"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:3L4R"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:3L4R"
FT STRAND 79..91
FT /evidence="ECO:0007829|PDB:3L4R"
FT STRAND 97..114
FT /evidence="ECO:0007829|PDB:3L4R"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:3L4R"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:3L4R"
FT STRAND 130..140
FT /evidence="ECO:0007829|PDB:3L4R"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3L4R"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:3L4R"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:3L4R"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:3L4R"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3L4R"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:3L4R"
SQ SEQUENCE 180 AA; 20230 MW; 2DE17BE496248E28 CRC64;
MQLLLLTVGL ALICGLQAQE GNHEEPQGGL EELSGRWHSV ALASNKSDLI KPWGHFRVFI
HSMSAKDGNL HGDILIPQDG QCEKVSLTAF KTATSNKFDL EYWGHNDLYL AEVDPKSYLI
LYMINQYNDD TSLVAHLMVR DLSRQQDFLP AFESVCEDIG LHKDQIVVLS DDDRCQGSRD
