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LECT_COCGR
ID   LECT_COCGR              Reviewed;         157 AA.
AC   P0DSP5;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2019, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=Lectin {ECO:0000303|PubMed:29126937};
DE   AltName: Full=Agglutinin {ECO:0000303|PubMed:29126937};
DE            Short=CIA17 {ECO:0000303|PubMed:29126937};
OS   Coccinia grandis (Ivy gourd) (Coccinia indica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Coccinia.
OX   NCBI_TaxID=387127;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT,
RP   TISSUE SPECIFICITY, AND DISULFIDE BOND.
RC   TISSUE=Fruit;
RX   PubMed=29126937; DOI=10.1016/j.ijbiomac.2017.11.024;
RA   Bobbili K.B., Pohlentz G., Narahari A., Sharma K., Surolia A., Mormann M.,
RA   Swamy M.J.;
RT   "Coccinia indica agglutinin, a 17kDa PP2 like phloem lectin: Affinity
RT   purification, primary structure and formation of self-assembled
RT   filaments.";
RL   Int. J. Biol. Macromol. 108:1227-1236(2018).
CC   -!- FUNCTION: Binds with high affinity specifically to chito-
CC       oligosaccharides. May play a role in plant defense against pathogens by
CC       directly binding with the chitin cell wall. Forms filamentous
CC       structures at higher concentrations and may promote wound healing by
CC       forming filaments with phloem proteins like PP1.
CC       {ECO:0000269|PubMed:29126937}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:29126937}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29126937}.
CC       Note=Detected in phloem exudate. {ECO:0000269|PubMed:29126937}.
CC   -!- TISSUE SPECIFICITY: Detected in fruits (at protein level).
CC       {ECO:0000269|PubMed:29126937}.
CC   -!- MASS SPECTROMETRY: Mass=17495; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:29126937};
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DR   AlphaFoldDB; P0DSP5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   InterPro; IPR025886; PP2-like.
DR   Pfam; PF14299; PP2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Lectin; Plant defense; Secreted.
FT   CHAIN           1..157
FT                   /note="Lectin"
FT                   /evidence="ECO:0000269|PubMed:29126937"
FT                   /id="PRO_0000447999"
FT   DISULFID        37..54
FT                   /evidence="ECO:0000269|PubMed:29126937"
SQ   SEQUENCE   157 AA;  18017 MW;  059FABA743C278E5 CRC64;
     LNQEKLSSTH FLLFPRAATL TWSDDTRYWS WNPVDFCGYQ LEEAQLSRVS WFDCRWTVNT
     TDLKTNVWYN VFLKVQMGSG ASGWNTPLNL ELEMPNGSKQ ASQVVLNDRP RDVWFKLQMG
     NLMVSDSETC GALRMSLYNH QTNWKMGATL GPLALEA
 
 
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