ALL1_CANLF
ID ALL1_CANLF Reviewed; 174 AA.
AC O18873;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Major allergen Can f 1;
DE AltName: Full=Allergen Dog 1;
DE AltName: Allergen=Can f 1;
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).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Tongue epithelial tissue.
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}.
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; AF027177; AAC48794.1; -; mRNA.
DR RefSeq; NP_001003190.1; NM_001003190.1.
DR PDB; 7DRU; X-ray; 2.50 A; A/B/C/D/E/F/G=19-174.
DR PDBsum; 7DRU; -.
DR AlphaFoldDB; O18873; -.
DR SMR; O18873; -.
DR STRING; 9615.ENSCAFP00000038987; -.
DR Allergome; 174; Can f 1.
DR Allergome; 3169; Can f 1.0101.
DR PaxDb; O18873; -.
DR PRIDE; O18873; -.
DR ABCD; O18873; 1 sequenced antibody.
DR GeneID; 403830; -.
DR KEGG; cfa:403830; -.
DR CTD; 29989; -.
DR eggNOG; ENOG502S22P; Eukaryota.
DR OrthoDB; 1450978at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005615; C:extracellular space; 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; 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 3D-structure; Allergen; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..174
FT /note="Major allergen Can f 1"
FT /id="PRO_0000017980"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..169
FT /evidence="ECO:0000250"
FT STRAND 33..44
FT /evidence="ECO:0007829|PDB:7DRU"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:7DRU"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:7DRU"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:7DRU"
FT STRAND 65..74
FT /evidence="ECO:0007829|PDB:7DRU"
FT STRAND 77..87
FT /evidence="ECO:0007829|PDB:7DRU"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:7DRU"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:7DRU"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:7DRU"
FT STRAND 127..136
FT /evidence="ECO:0007829|PDB:7DRU"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:7DRU"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:7DRU"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:7DRU"
SQ SEQUENCE 174 AA; 19248 MW; 091A3025660806D5 CRC64;
MKTLLLTIGF SLIAILQAQD TPALGKDTVA VSGKWYLKAM TADQEVPEKP DSVTPMILKA
QKGGNLEAKI TMLTNGQCQN ITVVLHKTSE PGKYTAYEGQ RVVFIQPSPV RDHYILYCEG
ELHGRQIRMA KLLGRDPEQS QEALEDFREF SRAKGLNQEI LELAQSETCS PGGQ