ID   HEVE_HEVBR              Reviewed;         204 AA.
AC   P02877;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   28-JUN-2023, entry version 139.
DE   RecName: Full=Pro-hevein;
DE   AltName: Full=Major hevein;
DE   Contains:
DE     RecName: Full=Hevein;
DE     AltName: Allergen=Hev b 6;
DE   Contains:
DE     RecName: Full=Win-like protein;
DE   Flags: Precursor;
GN   Name=HEV1;
OS   Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC   Hevea.
OX   NCBI_TaxID=3981;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2217194; DOI=10.1073/pnas.87.19.7633;
RA   Broekaert W.F., Lee H.I., Kush A., Chua N.H., Raikhel N.;
RT   "Wound-induced accumulation of mRNA containing a hevein sequence in
RT   laticifers of rubber tree (Hevea brasiliensis).";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:7633-7637(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 18-60.
RC   TISSUE=Latex;
RA   Walujono K., Scholma R.A., Beintema J.J., Mariono A., Hahn A.M.;
RT   "Amino-acid sequence of hevein.";
RL   (In) Proceedings of the international rubber conference, pp.2:518-531,
RL   Rubber Research Institute of Malaysia, Kuala Lumpur (1975).
RN   [3]
RP   SEQUENCE REVISION TO 51-52.
RA   Beintema J.J.;
RL   Submitted (JUN-1977) to the PIR data bank.
RN   [4]
RP   PROTEIN SEQUENCE OF 18-26 AND 67-77, AND PROTEOLYTIC PROCESSING.
RC   TISSUE=Latex;
RX   PubMed=1874741; DOI=10.1016/s0021-9258(18)98499-1;
RA   Lee H.-I., Broekaert W.F., Raikhel N.V.;
RT   "Co- and post-translational processing of the hevein preproprotein of latex
RT   of the rubber tree (Hevea brasiliensis).";
RL   J. Biol. Chem. 266:15944-15948(1991).
RN   [5]
RP   PROTEIN SEQUENCE OF 18-35.
RC   TISSUE=Latex;
RX   PubMed=9845845; DOI=10.1007/bf02255930;
RA   Chen H.-D., Chen C.-L., Huang S.-W., Kung H.-F., Chen H.-C.;
RT   "Characterization of latex allergenic components by capillary zone
RT   electrophoresis and N-terminal sequence analysis.";
RL   J. Biomed. Sci. 5:421-427(1998).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-60.
RX   PubMed=1936279; DOI=10.1016/0014-5793(91)81308-u;
RA   Rodriguez-Romero A., Ravichandran K.G., Soriano-Garcia M.;
RT   "Crystal structure of hevein at 2.8-A resolution.";
RL   FEBS Lett. 291:307-309(1991).
RN   [7]
RP   STRUCTURE BY NMR OF 18-60, AND DISULFIDE BONDS.
RX   PubMed=8431421; DOI=10.1021/bi00057a004;
RA   Andersen N.H., Cao B., Rodriguez-Romero A., Arreguin B.;
RT   "Hevein: NMR assignment and assessment of solution-state folding for the
RT   agglutinin-toxin motif.";
RL   Biochemistry 32:1407-1422(1993).
CC   -!- FUNCTION: N-acetyl-D-glucosamine / N-acetyl-D-neuraminic acid binding
CC       lectin. Can inhibit fungal growth.
CC   -!- TISSUE SPECIFICITY: Laticifer.
CC   -!- PTM: Proteolytically processed to yield the two chains of the mature
CC       protein. {ECO:0000269|PubMed:1874741}.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
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DR   EMBL; M36986; AAA33357.1; -; mRNA.
DR   PIR; A38288; HVHV.
DR   PDB; 1HEV; NMR; -; A=18-60.
DR   PDB; 1Q9B; X-ray; 1.50 A; A=18-60.
DR   PDB; 1T0W; NMR; -; A=18-49.
DR   PDB; 1WKX; X-ray; 1.70 A; A=18-60.
DR   PDB; 4WP4; X-ray; 1.43 A; A=18-60.
DR   PDBsum; 1HEV; -.
DR   PDBsum; 1Q9B; -.
DR   PDBsum; 1T0W; -.
DR   PDBsum; 1WKX; -.
DR   PDBsum; 4WP4; -.
DR   AlphaFoldDB; P02877; -.
DR   BMRB; P02877; -.
DR   SMR; P02877; -.
DR   Allergome; 390; Hev b 6.
DR   Allergome; 391; Hev b 6.01.
DR   Allergome; 392; Hev b 6.02.
DR   Allergome; 393; Hev b 6.03.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   UniLectin; P02877; -.
DR   ABCD; P02877; 3 sequenced antibodies.
DR   EvolutionaryTrace; P02877; -.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:InterPro.
DR   GO; GO:0050832; P:defense response to fungus; IEA:InterPro.
DR   CDD; cd06921; ChtBD1_GH19_hevein; 1.
DR   CDD; cd22777; DPBB_barwin-like; 1.
DR   Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR   InterPro; IPR018226; Barwin_CS.
DR   InterPro; IPR001153; Barwin_dom.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR036861; Endochitinase-like_sf.
DR   InterPro; IPR044301; PR4.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR46351:SF7; HEVEIN-LIKE PREPROPROTEIN; 1.
DR   PANTHER; PTHR46351; WOUND-INDUCED PROTEIN WIN2; 1.
DR   Pfam; PF00967; Barwin; 1.
DR   Pfam; PF00187; Chitin_bind_1; 1.
DR   PRINTS; PR00602; BARWIN.
DR   PRINTS; PR00451; CHITINBINDNG.
DR   SMART; SM00270; ChtBD1; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR   SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR   PROSITE; PS00771; BARWIN_1; 1.
DR   PROSITE; PS00772; BARWIN_2; 1.
DR   PROSITE; PS51174; BARWIN_3; 1.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR   PROSITE; PS50941; CHIT_BIND_I_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Allergen; Chitin-binding; Direct protein sequencing;
KW   Disulfide bond; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:1874741,
FT                   ECO:0000269|PubMed:9845845, ECO:0000269|Ref.2"
FT   CHAIN           18..204
FT                   /note="Pro-hevein"
FT                   /id="PRO_0000005280"
FT   CHAIN           18..60
FT                   /note="Hevein"
FT                   /id="PRO_0000005281"
FT   PROPEP          61..66
FT                   /evidence="ECO:0000269|PubMed:1874741"
FT                   /id="PRO_0000005282"
FT   CHAIN           67..204
FT                   /note="Win-like protein"
FT                   /id="PRO_0000005283"
FT   DOMAIN          18..60
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DOMAIN          68..189
FT                   /note="Barwin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00527"
FT   DISULFID        20..35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:8431421"
FT   DISULFID        29..41
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:8431421"
FT   DISULFID        34..48
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:8431421"
FT   DISULFID        54..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT                   ECO:0000269|PubMed:8431421"
FT   DISULFID        96..128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        117..151
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        131..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   VARIANT         31
FT                   /note="N -> D (possible deamidation)"
FT   VARIANT         73
FT                   /note="V -> M"
FT   HELIX           22..24
FT                   /evidence="ECO:0007829|PDB:4WP4"
FT   HELIX           30..32
FT                   /evidence="ECO:0007829|PDB:4WP4"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:1T0W"
FT   STRAND          41..44
FT                   /evidence="ECO:0007829|PDB:4WP4"
FT   HELIX           45..48
FT                   /evidence="ECO:0007829|PDB:4WP4"
FT   HELIX           50..52
FT                   /evidence="ECO:0007829|PDB:4WP4"
SQ   SEQUENCE   204 AA;  21859 MW;  FBCEE57CDFC80569 CRC64;
     MNIFIVVLLC LTGVAIAEQC GRQAGGKLCP NNLCCSQWGW CGSTDEYCSP DHNCQSNCKD
     SGEGVGGGSA SNVLATYHLY NSQDHGWDLN AASAYCSTWD ANKPYSWRSK YGWTAFCGPV
     GAHGQSSCGK CLSVTNTGTG AKTTVRIVDQ CSNGGLDLDV NVFRQLDTDG KGYERGHITV
     NYQFVDCGDS FNPLFSVMKS SVIN
//