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LCB2_ROBPS
ID   LCB2_ROBPS              Reviewed;         286 AA.
AC   Q42372;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Bark agglutinin I polypeptide B;
DE   AltName: Full=LECRPA2;
DE   AltName: Full=RPbAI;
DE   Flags: Precursor;
OS   Robinia pseudoacacia (Black locust).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; robinioid clade; Robinieae; Robinia.
OX   NCBI_TaxID=35938;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Bark;
RX   PubMed=7915553; DOI=10.1007/bf00028879;
RA   Yoshida K., Baba K., Yamamoto N., Tazaki K.;
RT   "Cloning of a lectin cDNA and seasonal changes in levels of the lectin and
RT   its mRNA in the inner bark of Robinia pseudoacacia.";
RL   Plant Mol. Biol. 25:845-853(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 32-49.
RX   PubMed=7716244; DOI=10.1104/pp.107.3.833;
RA   van Damme E.J.M., Barre A., Smeets K., Torrekens S., van Leuven F.,
RA   Rouge P., Peumans W.J.;
RT   "The bark of Robinia pseudoacacia contains a complex mixture of lectins.
RT   Characterization of the proteins and the cDNA clones.";
RL   Plant Physiol. 107:833-843(1995).
RN   [3]
RP   PROTEIN SEQUENCE OF 32-51.
RC   TISSUE=Bark;
RA   Tazaki K., Yoshida K.;
RT   "The bark lectin of Robinia pseudoacacia: purification and partial
RT   characterization.";
RL   Plant Cell Physiol. 33:125-129(1992).
CC   -!- FUNCTION: Bark lectins are storage proteins that probably maintain
CC       stocks of nitrogen during dormant period. Self-aggregatable molecules
CC       that can bind their own carbohydrate side chains. They could also play
CC       a role in the plant's defense against phytophagous invertebrates or
CC       herbivorous higher animals.
CC   -!- SUBUNIT: RPbAI is composed of two polypeptides, A and B, that associate
CC       into five different tetrameric isolectins. The A4 combination is the
CC       only one devoid of agglutination activity. Isoform B4 displays maximal
CC       agglutination activity.
CC   -!- TISSUE SPECIFICITY: Mostly in the axial and ray parenchymal cells of
CC       the inner bark. Fewer in the axial and ray parenchymal cells of the
CC       xylem. Strong expression in bark. The lectin accumulates in the inner
CC       bark in autumn and winter and disappears in may.
CC   -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR   EMBL; D17757; BAA04604.1; -; mRNA.
DR   EMBL; U12783; AAA80182.1; -; mRNA.
DR   PIR; S48033; S48033.
DR   AlphaFoldDB; Q42372; -.
DR   SMR; Q42372; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR016363; L-lectin.
DR   InterPro; IPR000985; Lectin_LegA_CS.
DR   InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR   InterPro; IPR001220; Legume_lectin_dom.
DR   Pfam; PF00139; Lectin_legB; 1.
DR   PIRSF; PIRSF002690; L-type_lectin_plant; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00308; LECTIN_LEGUME_ALPHA; 1.
DR   PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Glycoprotein; Lectin; Manganese;
KW   Metal-binding; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000269|PubMed:7716244, ECO:0000269|Ref.3"
FT   CHAIN           32..286
FT                   /note="Bark agglutinin I polypeptide B"
FT                   /id="PRO_0000017645"
FT   BINDING         157
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        43..46
FT                   /note="KHSQ -> MPNE (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        48
FT                   /note="D -> W (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   286 AA;  31211 MW;  467E37661D1DC1E6 CRC64;
     MASYKFKTQN SFLLLLSISF FFLLLLNKVN STGSLSFSFP KFKHSQPDLI FQSDALVTSK
     GVLQLTTVND GRPVYDSIGR VLYAAPFQIW DSTTGNVASF VTSFSFIIKA PNEGKTADGL
     VFFLAPVGST QPLKGGGLLG LFKDESYNKS NQIVAVEFDT FRNVAWDPNG IHMGIDVNSI
     QSVRTVRWDW ANGEVANVFI SYEASTKSLT ASLVYPSLEK SFILSAIVDL KKVLPEWVRV
     GFTATTGLSE DYVQTNDVLS WSFESNLPGG NSVASVKNAG LSTYAA
 
 
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