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ALTA1_ALTAL
ID   ALTA1_ALTAL             Reviewed;         157 AA.
AC   P79085;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Major allergen Alt a 1;
DE   AltName: Allergen=Alt a 1;
DE   Flags: Precursor;
GN   Name=ALTA1;
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION,
RP   AND ALLERGEN.
RX   PubMed=8957113; DOI=10.1159/000237397;
RA   De Vouge M.W., Thaker A.J., Curran I.H., Zhang L., Muradia G., Rode H.,
RA   Vijay H.M.;
RT   "Isolation and expression of a cDNA clone encoding an Alternaria alternata
RT   Alt a 1 subunit.";
RL   Int. Arch. Allergy Immunol. 111:385-395(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=08-0203-Berlin;
RA   Unger A.M., Lechenauer E., Simon B., Oberkofler H., Probst G., Achatz G.,
RA   Breitenbach M.;
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SUBCELLULAR LOCATION, AND ALLERGEN.
RX   PubMed=22640235; DOI=10.1111/j.1574-6968.2012.02606.x;
RA   Morin M., Asturias J.A., Dominguez A.;
RT   "Expression of Alt a 1 allergen from Alternaria alternata in the yeast
RT   Yarrowia lipolytica.";
RL   FEMS Microbiol. Lett. 333:121-128(2012).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=22078468; DOI=10.1016/j.jaci.2011.10.008;
RA   Twaroch T.E., Arcalis E., Sterflinger K., Stoeger E., Swoboda I.,
RA   Valenta R.;
RT   "Predominant localization of the major Alternaria allergen Alt a 1 in the
RT   cell wall of airborne spores.";
RL   J. Allergy Clin. Immunol. 129:1148-1149(2012).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=24642375; DOI=10.1016/j.febslet.2014.02.044;
RA   Gomez-Casado C., Murua-Garcia A., Garrido-Arandia M., Gonzalez-Melendi P.,
RA   Sanchez-Monge R., Barber D., Pacios L.F., Diaz-Perales A.;
RT   "Alt a 1 from Alternaria interacts with PR5 thaumatin-like proteins.";
RL   FEBS Lett. 588:1501-1508(2014).
RN   [6]
RP   STRUCTURE BY NMR OF 26-157, AND SUBUNIT.
RX   PubMed=23715812; DOI=10.1007/s12104-013-9489-z;
RA   Wagner G.E., Gutfreund S., Fauland K., Keller W., Valenta R., Zangger K.;
RT   "Backbone resonance assignment of Alt a 1, a unique beta-barrel protein and
RT   the major allergen of Alternaria alternata.";
RL   Biomol. NMR. Assign. 8:229-231(2014).
RN   [7] {ECO:0007744|PDB:3V0R}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 26-157, AND SUBUNIT.
RX   PubMed=22664167; DOI=10.1016/j.jaci.2012.03.047;
RA   Chruszcz M., Chapman M.D., Osinski T., Solberg R., Demas M., Porebski P.J.,
RA   Majorek K.A., Pomes A., Minor W.;
RT   "Alternaria alternata allergen Alt a 1: a unique beta-barrel protein dimer
RT   found exclusively in fungi.";
RL   J. Allergy Clin. Immunol. 130:241-247(2012).
RN   [8] {ECO:0007744|PDB:4AUD}
RP   X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS) OF 29-157.
RA   Mechaly A.E., Ibanez De Opakua A., Bermejo I., Asturias J., Viguera A.R.;
RT   "Crystal Structure of Major Allergen of Alternaria Alternata Alt a 1.";
RL   Submitted (MAY-2012) to the PDB data bank.
CC   -!- FUNCTION: May bind and inhibit the beta-glucanase activity of host
CC       plant thaumatin-like proteins. {ECO:0000269|PubMed:24642375}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:22664167,
CC       ECO:0000269|PubMed:23715812}.
CC   -!- INTERACTION:
CC       P79085; P81370: tlp; Xeno; NbExp=3; IntAct=EBI-9212161, EBI-9212168;
CC   -!- SUBCELLULAR LOCATION: Spore wall {ECO:0000269|PubMed:22078468,
CC       ECO:0000269|PubMed:24642375}. Secreted {ECO:0000269|PubMed:22640235,
CC       ECO:0000269|PubMed:24642375, ECO:0000269|PubMed:8957113}.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC       {ECO:0000269|PubMed:8957113, ECO:0000305|PubMed:22640235}.
CC   -!- SIMILARITY: Belongs to the ALTA1 family. {ECO:0000305}.
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DR   EMBL; U86752; AAB47552.1; -; mRNA.
DR   EMBL; U82633; AAB40400.1; -; mRNA.
DR   RefSeq; XP_018383182.1; XM_018534774.1.
DR   PDB; 3V0R; X-ray; 1.90 A; A=26-157.
DR   PDB; 4AUD; X-ray; 2.67 A; A/B=29-157.
DR   PDBsum; 3V0R; -.
DR   PDBsum; 4AUD; -.
DR   AlphaFoldDB; P79085; -.
DR   BMRB; P79085; -.
DR   SMR; P79085; -.
DR   IntAct; P79085; 3.
DR   MINT; P79085; -.
DR   Allergome; 11; Alt a 1.0101.
DR   Allergome; 722; Alt a 1.
DR   GeneID; 29120368; -.
DR   KEGG; aalt:CC77DRAFT_941148; -.
DR   OMA; NDQVCET; -.
DR   GO; GO:0005619; C:ascospore wall; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   InterPro; IPR032382; AltA1.
DR   Pfam; PF16541; AltA1; 1.
DR   PROSITE; PS51895; AA1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Allergen; Direct protein sequencing; Disulfide bond;
KW   Secreted; Signal.
FT   SIGNAL          1..18
FT   CHAIN           19..157
FT                   /note="Major allergen Alt a 1"
FT                   /id="PRO_0000020699"
FT   DOMAIN          35..153
FT                   /note="AA1-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01243"
FT   DISULFID        30
FT                   /note="Interchain"
FT                   /evidence="ECO:0000269|PubMed:22664167,
FT                   ECO:0007744|PDB:3V0R"
FT   DISULFID        74..89
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01243,
FT                   ECO:0000269|PubMed:22664167, ECO:0007744|PDB:3V0R,
FT                   ECO:0007744|PDB:4AUD"
FT   DISULFID        128..140
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01243,
FT                   ECO:0000269|PubMed:22664167, ECO:0007744|PDB:3V0R,
FT                   ECO:0007744|PDB:4AUD"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:3V0R"
FT   STRAND          39..49
FT                   /evidence="ECO:0007829|PDB:3V0R"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:3V0R"
FT   STRAND          56..67
FT                   /evidence="ECO:0007829|PDB:3V0R"
FT   STRAND          71..77
FT                   /evidence="ECO:0007829|PDB:3V0R"
FT   STRAND          87..92
FT                   /evidence="ECO:0007829|PDB:3V0R"
FT   STRAND          96..100
FT                   /evidence="ECO:0007829|PDB:3V0R"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:3V0R"
FT   STRAND          105..111
FT                   /evidence="ECO:0007829|PDB:3V0R"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:3V0R"
FT   STRAND          117..123
FT                   /evidence="ECO:0007829|PDB:3V0R"
FT   STRAND          126..130
FT                   /evidence="ECO:0007829|PDB:3V0R"
FT   STRAND          132..134
FT                   /evidence="ECO:0007829|PDB:3V0R"
FT   STRAND          138..144
FT                   /evidence="ECO:0007829|PDB:3V0R"
FT   STRAND          146..149
FT                   /evidence="ECO:0007829|PDB:3V0R"
FT   STRAND          151..153
FT                   /evidence="ECO:0007829|PDB:4AUD"
SQ   SEQUENCE   157 AA;  16980 MW;  AAC20D0819198246 CRC64;
     MQFTTIASLF AAAGLAAAAP LESRQDTASC PVTTEGDYVW KISEFYGRKP EGTYYNSLGF
     NIKATNGGTL DFTCSAQADK LEDHKWYSCG ENSFMDFSFD SDRSGLLLKQ KVSDDITYVA
     TATLPNYCRA GGNGPKDFVC QGVADAYITL VTLPKSS
 
 
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