HEVE_HEVBR
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 25-MAY-2022, entry version 135.
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:ribonuclease 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 Gene3D; 2.40.40.10; -; 1.
DR Gene3D; 3.30.60.10; -; 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; PTHR46351; 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; SSF50685; 1.
DR SUPFAM; SSF57016; SSF57016; 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
