ALL1_HORSE
ID ALL1_HORSE Reviewed; 187 AA.
AC Q95182;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Major allergen Equ c 1;
DE AltName: Allergen=Equ c 1;
DE Flags: Precursor;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND ALLERGEN.
RC TISSUE=Hair, and Sublingual gland;
RX PubMed=8955138; DOI=10.1074/jbc.271.51.32951;
RA Gregoire C., Rosinski-Chupin I., Rabillon J., Alzari P.M., David B.,
RA Dandeu J.-P.;
RT "cDNA cloning and sequencing reveal the major horse allergen Equ c1 to be a
RT glycoprotein member of the lipocalin superfamily.";
RL J. Biol. Chem. 271:32951-32959(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-181.
RC TISSUE=Salivary gland;
RX PubMed=10787420; DOI=10.1074/jbc.m002854200;
RA Lascombe M.-B., Gregoire C., Poncet P., Tavares G.A., Rosinski-Chupin I.,
RA Rabillon J., Goubran-Botros H., Mazie J.-C., David B., Alzari P.M.;
RT "Crystal structure of the allergen Equ c 1: a dimeric lipocalin with
RT restricted IgE-reactive epitopes.";
RL J. Biol. Chem. 275:21572-21577(2000).
RN [3]
RP MASS SPECTROMETRY.
RC TISSUE=Dander;
RX PubMed=11358533; DOI=10.1046/j.1432-1327.2001.02217.x;
RA Goubran Botros H., Poncet P., Rabillon J., Fontaine T., Laval J.-M.,
RA David B.;
RT "Biochemical characterization and surfactant properties of horse
RT allergens.";
RL Eur. J. Biochem. 268:3126-3136(2001).
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in liver and in sublingual and
CC submaxillary salivary glands. Highly concentrated in secretory fluid
CC such as saliva and urine as well as in hair dandruff extract.
CC -!- PTM: Several N-terminal ends may be due to cleavage by signal peptidase
CC at different sites or may be generated by proteolytic processing of the
CC secreted protein.
CC -!- PTM: Analysis of the sugar composition shows the presence of GalNAc,
CC Gal, NeuAc, GlcNAc, and Man. May be also O-glycosylated.
CC -!- MASS SPECTROMETRY: Mass=22000; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11358533};
CC -!- ALLERGEN: Causes an allergic reaction in human. Potent allergen
CC responsible for about 80% of anti-horse IgE antibody response in
CC patients who are chronically exposed to horse allergens.
CC {ECO:0000269|PubMed:8955138}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; U70823; AAC48691.1; -; mRNA.
DR RefSeq; NP_001075966.1; NM_001082497.2.
DR PDB; 1EW3; X-ray; 2.30 A; A=23-181.
DR PDBsum; 1EW3; -.
DR AlphaFoldDB; Q95182; -.
DR SMR; Q95182; -.
DR STRING; 9796.ENSECAP00000049682; -.
DR Allergome; 3306; Equ c 1.0101.
DR Allergome; 331; Equ c 1.
DR PaxDb; Q95182; -.
DR Ensembl; ENSECAT00000000508; ENSECAP00000000397; ENSECAG00000034517.
DR GeneID; 100034197; -.
DR KEGG; ecb:100034197; -.
DR GeneTree; ENSGT01050000244868; -.
DR HOGENOM; CLU_094061_4_0_1; -.
DR OMA; FHTKVNG; -.
DR OrthoDB; 1475169at2759; -.
DR EvolutionaryTrace; Q95182; -.
DR Proteomes; UP000002281; Chromosome 25.
DR Bgee; ENSECAG00000034517; Expressed in zone of skin and 10 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; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..15
FT /note="Or 16, or 21"
FT CHAIN 16..187
FT /note="Major allergen Equ c 1"
FT /id="PRO_0000017982"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..176
FT VARIANT 62
FT /note="V -> L"
FT VARIANT 90
FT /note="F -> A"
FT VARIANT 136
FT /note="F -> L"
FT VARIANT 146
FT /note="S -> D"
FT VARIANT 172..173
FT /note="KI -> QT"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1EW3"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:1EW3"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:1EW3"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1EW3"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:1EW3"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:1EW3"
FT STRAND 82..92
FT /evidence="ECO:0007829|PDB:1EW3"
FT STRAND 98..116
FT /evidence="ECO:0007829|PDB:1EW3"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:1EW3"
FT STRAND 133..144
FT /evidence="ECO:0007829|PDB:1EW3"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:1EW3"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1EW3"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1EW3"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:1EW3"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:1EW3"
SQ SEQUENCE 187 AA; 21696 MW; 28898F744732FF71 CRC64;
MKLLLLCLGL ILVCAQQEEN SDVAIRNFDI SKISGEWYSI FLASDVKEKI EENGSMRVFV
DVIRALDNSS LYAEYQTKVN GECTEFPMVF DKTEEDGVYS LNYDGYNVFR ISEFENDEHI
ILYLVNFDKD RPFQLFEFYA REPDVSPEIK EEFVKIVQKR GIVKENIIDL TKIDRCFQLR
GNGVAQA
