BARW_HORVU
ID BARW_HORVU Reviewed; 125 AA.
AC P28814;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Barwin;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1, AND DISULFIDE BONDS.
RC STRAIN=cv. Hiproly; TISSUE=Seed;
RX PubMed=1390663; DOI=10.1021/bi00152a012;
RA Svensson B., Svendsen I., Hoejrup P., Roepstorff P., Ludvigsen S.,
RA Poulsen F.M.;
RT "Primary structure of barwin: a barley seed protein closely related to the
RT C-terminal domain of proteins encoded by wound-induced plant genes.";
RL Biochemistry 31:8767-8770(1992).
RN [2]
RP STRUCTURE BY NMR.
RC STRAIN=cv. Hiproly; TISSUE=Seed;
RX PubMed=1390664; DOI=10.1021/bi00152a013;
RA Ludvigsen S., Poulsen F.M.;
RT "Secondary structure in solution of barwin from barley seed using 1H
RT nuclear magnetic resonance spectroscopy.";
RL Biochemistry 31:8771-8782(1992).
CC -!- FUNCTION: May be involved in a defense mechanism. Probable plant
CC lectin. Binds weakly a chitin analog.
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DR PIR; A43474; A43474.
DR PDB; 1BW3; NMR; -; A=2-125.
DR PDB; 1BW4; NMR; -; A=2-125.
DR PDBsum; 1BW3; -.
DR PDBsum; 1BW4; -.
DR AlphaFoldDB; P28814; -.
DR SMR; P28814; -.
DR PRIDE; P28814; -.
DR EvolutionaryTrace; P28814; -.
DR ExpressionAtlas; P28814; baseline and differential.
DR GO; GO:0030246; F:carbohydrate 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 InterPro; IPR018226; Barwin_CS.
DR InterPro; IPR001153; Barwin_dom.
DR InterPro; IPR044301; PR4.
DR InterPro; IPR036908; RlpA-like_sf.
DR PANTHER; PTHR46351; PTHR46351; 1.
DR Pfam; PF00967; Barwin; 1.
DR PRINTS; PR00602; BARWIN.
DR SUPFAM; SSF50685; SSF50685; 1.
DR PROSITE; PS00771; BARWIN_1; 1.
DR PROSITE; PS00772; BARWIN_2; 1.
DR PROSITE; PS51174; BARWIN_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Lectin;
KW Plant defense; Pyrrolidone carboxylic acid.
FT CHAIN 1..125
FT /note="Barwin"
FT /id="PRO_0000164261"
FT DOMAIN 1..125
FT /note="Barwin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00527"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:1390663"
FT DISULFID 31..63
FT /evidence="ECO:0000269|PubMed:1390663"
FT DISULFID 52..86
FT /evidence="ECO:0000269|PubMed:1390663"
FT DISULFID 66..123
FT /evidence="ECO:0000269|PubMed:1390663"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1BW3"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:1BW3"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1BW3"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:1BW3"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:1BW3"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1BW3"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1BW4"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1BW3"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1BW3"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1BW3"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:1BW3"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1BW3"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1BW4"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1BW3"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:1BW3"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:1BW3"
FT STRAND 112..121
FT /evidence="ECO:0007829|PDB:1BW3"
SQ SEQUENCE 125 AA; 13737 MW; AA4227B7DCD070B4 CRC64;
QQANDVRATY HYYRPAQNNW DLGAPAVSAY CATWDASKPL SWRSKYGWTA FCGPAGPRGQ
AACGKCLRVT NPATGAQITA RIVDQCANGG LDLDWDTVFT KIDTNGIGYQ QGHLNVNYQF
VDCRD