ID   FEL1A_FELCA             Reviewed;          92 AA.
AC   P30438; P30439;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   04-NOV-2026, entry version 133.
DE   RecName: Full=Major allergen I polypeptide chain 1;
DE   AltName: Full=AG4;
DE   AltName: Full=Allergen Cat-1;
DE   AltName: Full=Allergen Fel d I-A;
DE            Short=Allergen FdI;
DE            Short=Allergen Fel dI;
DE   AltName: Allergen=Fel d 1-A;
DE   Flags: Precursor;
GN   Name=CH1;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 23-92 (ISOFORMS 1 AND
RP   2).
RC   TISSUE=Salivary gland;
RX   PubMed=1946388; DOI=10.1073/pnas.88.21.9690;
RA   Morgenstern J.P., Griffith I.J., Brauer A.W., Rogers B.L., Bond J.F.,
RA   Chapman M.D., Kuo M.-C.;
RT   "Amino acid sequence of Fel dI, the major allergen of the domestic cat:
RT   protein sequence analysis and cDNA cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:9690-9694(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Liver;
RX   PubMed=1572548; DOI=10.1016/0378-1119(92)90405-e;
RA   Griffith I.J., Craig S., Pollock J., Yu X.-B., Morgenstern J.P.,
RA   Rogers B.L.;
RT   "Expression and genomic structure of the genes encoding FdI, the major
RT   allergen from the domestic cat.";
RL   Gene 113:263-268(1992).
RN   [3]
RP   PROTEIN SEQUENCE OF 23-62, AND CHARACTERIZATION.
RX   PubMed=1712068; DOI=10.1016/0161-5890(91)90141-6;
RA   Duffort O.A., Carreira J., Nitti G., Polo F., Lombardero M.;
RT   "Studies on the biochemical structure of the major cat allergen Felis
RT   domesticus I.";
RL   Mol. Immunol. 28:301-309(1991).
RN   [4]
RP   CHARACTERIZATION.
RX   PubMed=6747135; DOI=10.1016/0091-6749(84)90278-1;
RA   Leitermann K., Ohman J.L. Jr.;
RT   "Cat allergen 1: biochemical, antigenic, and allergenic properties.";
RL   J. Allergy Clin. Immunol. 74:147-153(1984).
RN   [5] {ECO:0007744|PDB:1PUO}
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH CH2, FUNCTION, SUBUNIT, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, ALLERGEN, AND DISULFIDE BOND.
RX   PubMed=12851385; DOI=10.1074/jbc.m304740200;
RA   Kaiser L., Gronlund H., Sandalova T., Ljunggren H.G., van Hage-Hamsten M.,
RA   Achour A., Schneider G.;
RT   "The crystal structure of the major cat allergen Fel d 1, a member of the
RT   secretoglobin family.";
RL   J. Biol. Chem. 278:37730-37735(2003).
RN   [6] {ECO:0007744|PDB:2EJN}
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH CH2 AND CA(2+), FUNCTION, SUBUNIT,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALLERGEN, AND DISULFIDE BOND.
RX   PubMed=17543334; DOI=10.1016/j.jmb.2007.04.074;
RA   Kaiser L., Velickovic T.C., Badia-Martinez D., Adedoyin J., Thunberg S.,
RA   Hallen D., Berndt K., Gronlund H., Gafvelin G., van Hage M., Achour A.;
RT   "Structural characterization of the tetrameric form of the major cat
RT   allergen Fel d 1.";
RL   J. Mol. Biol. 370:714-727(2007).
CC   -!- FUNCTION: Chelates calciums ions and may inhibit the activity of
CC       calcium-dependent phospholipase A2. {ECO:0000269|PubMed:12851385,
CC       ECO:0000269|PubMed:17543334}.
CC   -!- SUBUNIT: Heterotetramer composed of two non-covalently linked
CC       heterodimers of CH1/Fel d I-A and CH2/Fel d I-B; CH1 and CH2 are
CC       covalently linked by interchain disulfide bonds (PubMed:12851385,
CC       PubMed:17543334). Binds to at least three calcium ions as a tetrameric
CC       complex (PubMed:17543334). {ECO:0000269|PubMed:12851385,
CC       ECO:0000269|PubMed:17543334}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12851385,
CC       ECO:0000269|PubMed:17543334}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Leader A, Major;
CC         IsoId=P30438-1; Sequence=Displayed;
CC       Name=2; Synonyms=Leader B, Minor;
CC         IsoId=P30438-2; Sequence=VSP_015665;
CC   -!- TISSUE SPECIFICITY: Saliva and sebaceous glands.
CC       {ECO:0000269|PubMed:12851385, ECO:0000269|PubMed:17543334}.
CC   -!- ALLERGEN: Causes an allergic reaction in human (PubMed:12851385,
CC       PubMed:17543334). Binds to IgE (PubMed:12851385, PubMed:17543334).
CC       Major allergen produced by the domestic cat (PubMed:12851385,
CC       PubMed:17543334). Implicated as an asthma-inducing agent in human. This
CC       protein is sticky and easily adheres to walls, carpet, clothing,
CC       furniture and bedding. {ECO:0000269|PubMed:12851385,
CC       ECO:0000269|PubMed:17543334}.
CC   -!- SIMILARITY: Belongs to the secretoglobin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA44343.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA44344.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M74952; AAC37318.1; -; mRNA.
DR   EMBL; M74953; AAC41617.1; -; mRNA.
DR   EMBL; X62477; CAA44344.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X62477; CAA44343.1; ALT_INIT; Genomic_DNA.
DR   PIR; A56413; A56413.
DR   PIR; JC1136; JC1136.
DR   RefSeq; NP_001041618.1; NM_001048153.1.
DR   PDB; 1PUO; X-ray; 1.85 A; A/B=23-92.
DR   PDB; 1ZKR; X-ray; 1.64 A; A/B=23-92.
DR   PDB; 2EJN; X-ray; 1.64 A; A/B=23-92.
DR   PDB; 5VYF; X-ray; 2.90 A; C/F=23-92.
DR   AlphaFoldDB; P30438; -.
DR   SMR; P30438; -.
DR   Allergome; 3278; Fel d 1.0101.
DR   Allergome; 345; Fel d 1.
DR   ABCD; P30438; 4 sequenced antibodies.
DR   GeneID; 677877; -.
DR   KEGG; fca:677877; -.
DR   eggNOG; ENOG502RTYP; Eukaryota.
DR   InParanoid; P30438; -.
DR   OrthoDB; 9450650at2759; -.
DR   EvolutionaryTrace; P30438; -.
DR   PRO; PR:P30438; -.
DR   Proteomes; UP000823872; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0005496; F:steroid binding; IBA:GO_Central.
DR   CDD; cd00633; Secretoglobin; 1.
DR   FunFam; 1.20.920.50:FF:000001; Androgen-binding protein; 1.
DR   Gene3D; 1.20.920.50; -; 1.
DR   InterPro; IPR006178; CH1-like.
DR   InterPro; IPR016126; Secretoglobin.
DR   InterPro; IPR053723; Secretoglobin_Domain_sf.
DR   InterPro; IPR035960; Secretoglobin_sf.
DR   PANTHER; PTHR21226; ABPA10-RELATED; 1.
DR   PANTHER; PTHR21226:SF8; ABPA10-RELATED; 1.
DR   Pfam; PF01099; Uteroglobin; 1.
DR   PRINTS; PR00827; FELALLERGEN.
DR   SMART; SM00096; UTG; 1.
DR   SUPFAM; SSF48201; Uteroglobin-like; 1.
DR   PROSITE; PS51311; SCGB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Allergen; Alternative splicing; Direct protein sequencing;
KW   Disulfide bond; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:1712068"
FT   CHAIN           23..92
FT                   /note="Major allergen I polypeptide chain 1"
FT                   /id="PRO_0000036370"
FT   BINDING         68
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:17543334,
FT                   ECO:0007744|PDB:2EJN"
FT   BINDING         71
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:17543334,
FT                   ECO:0007744|PDB:2EJN"
FT   BINDING         74
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:17543334,
FT                   ECO:0007744|PDB:2EJN"
FT   DISULFID        25
FT                   /note="Interchain (with C-90 in CH2)"
FT                   /evidence="ECO:0000269|PubMed:12851385,
FT                   ECO:0000269|PubMed:17543334, ECO:0007744|PDB:1PUO,
FT                   ECO:0007744|PDB:2EJN"
FT   DISULFID        66
FT                   /note="Interchain (with C-65 in CH2)"
FT                   /evidence="ECO:0000269|PubMed:12851385,
FT                   ECO:0000269|PubMed:17543334, ECO:0007744|PDB:1PUO,
FT                   ECO:0007744|PDB:2EJN"
FT   DISULFID        92
FT                   /note="Interchain (with C-24 in CH2)"
FT                   /evidence="ECO:0000269|PubMed:12851385,
FT                   ECO:0000269|PubMed:17543334, ECO:0007744|PDB:1PUO,
FT                   ECO:0007744|PDB:2EJN"
FT   VAR_SEQ         1..21
FT                   /note="MKGACVLVLLWAALLLISGGN -> MLDAALPPCPTVAATAD (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_015665"
FT   VARIANT         51
FT                   /note="K -> N"
FT   CONFLICT        5
FT                   /note="C -> R (in Ref. 1; AAC37318)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        18
FT                   /note="S -> W (in Ref. 1; AAC37318)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82
FT                   /note="V -> L (in Ref. 1; AAC41617/AAC37318)"
FT                   /evidence="ECO:0000305"
FT   HELIX           26..37
FT                   /evidence="ECO:0007829|PDB:1ZKR"
FT   HELIX           40..50
FT                   /evidence="ECO:0007829|PDB:1ZKR"
FT   HELIX           54..70
FT                   /evidence="ECO:0007829|PDB:1ZKR"
FT   HELIX           73..87
FT                   /evidence="ECO:0007829|PDB:1ZKR"
SQ   SEQUENCE   92 AA;  10086 MW;  083145F55EE8AAB3 CRC64;
     MKGACVLVLL WAALLLISGG NCEICPAVKR DVDLFLTGTP DEYVEQVAQY KALPVVLENA
     RILKNCVDAK MTEEDKENAL SVLDKIYTSP LC
//