IPO_IPOBA
ID IPO_IPOBA Reviewed; 154 AA.
AC P93193;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Ipomoelin {ECO:0000303|PubMed:22808208, ECO:0000303|PubMed:30824008, ECO:0000303|PubMed:9249986, ECO:0000312|EMBL:BAA14024.1};
DE AltName: Full=Jacalin related lectin {ECO:0000303|PubMed:22808208};
DE Short=JRL {ECO:0000303|PubMed:22808208};
GN Name=IPO {ECO:0000303|PubMed:12746543, ECO:0000303|PubMed:17971062,
GN ECO:0000303|PubMed:25063862, ECO:0000303|PubMed:26924170,
GN ECO:0000303|Ref.2, ECO:0000303|Ref.4};
OS Ipomoea batatas (Sweet potato) (Convolvulus batatas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX NCBI_TaxID=4120 {ECO:0000312|EMBL:BAA14024.1};
RN [1] {ECO:0000312|EMBL:BAA14024.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-51; 77-105 AND 110-134,
RP TISSUE SPECIFICITY, INDUCTION, AND PTM.
RC STRAIN=cv. Kokei No. 14 {ECO:0000303|PubMed:9249986,
RC ECO:0000312|EMBL:BAA14024.1};
RC TISSUE=Leaf {ECO:0000303|PubMed:9249986, ECO:0000312|EMBL:BAA14024.1};
RX PubMed=9249986; DOI=10.1093/oxfordjournals.pcp.a029216;
RA Imanishi S., Kito-Nakamura K., Matsuoka K., Morikami A., Nakamura K.;
RT "A major jasmonate-inducible protein of sweet potato, ipomoelin, is an ABA-
RT independent wound-inducible protein.";
RL Plant Cell Physiol. 38:643-652(1997).
RN [2]
RP INDUCTION.
RX DOI=10.1046/j.0016-8025.2003.01062.x;
RA Chen Y.C., Tseng B.W., Huang Y.L., Liu Y.C., Jeng S.T.;
RT "Expression of the ipomoelin gene from sweet potato is regulated by
RT dephosphorylated proteins, calcium ion and ethylene.";
RL Plant Cell Environ. 26:1373-1383(2003).
RN [3]
RP INDUCTION.
RX PubMed=12746543; DOI=10.1104/pp.102.015701;
RA Jih P.J., Chen Y.C., Jeng S.T.;
RT "Involvement of hydrogen peroxide and nitric oxide in expression of the
RT ipomoelin gene from sweet potato.";
RL Plant Physiol. 132:381-389(2003).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, TISSUE SPECIFICITY, AND INDUCTION.
RX DOI=10.1111/j.1365-3040.2005.01271.x;
RA Chen Y.C., Chang H.S., Lai H.M., Jeng S.T.;
RT "Characterization of the wound-inducible protein ipomoelin from sweet
RT potato.";
RL Plant Cell Environ. 28:251-259(2005).
RN [5]
RP INDUCTION.
RX PubMed=17971062; DOI=10.1111/j.1365-3040.2007.01742.x;
RA Chen Y.C., Lin H.H., Jeng S.T.;
RT "Calcium influxes and mitogen-activated protein kinase kinase activation
RT mediate ethylene inducing ipomoelin gene expression in sweet potato.";
RL Plant Cell Environ. 31:62-72(2008).
RN [6]
RP INDUCTION.
RX PubMed=25063862; DOI=10.1093/jxb/eru291;
RA Lin J.S., Lin H.H., Li Y.C., King Y.C., Sung R.J., Kuo Y.W., Lin C.C.,
RA Shen Y.H., Jeng S.T.;
RT "Carbon monoxide regulates the expression of the wound-inducible gene
RT ipomoelin through antioxidation and MAPK phosphorylation in sweet potato.";
RL J. Exp. Bot. 65:5279-5290(2014).
RN [7]
RP INDUCTION.
RX PubMed=26924170; DOI=10.1111/pce.12729;
RA Li Y.C., Wan W.L., Lin J.S., Kuo Y.W., King Y.C., Chen Y.C., Jeng S.T.;
RT "Signal transduction and regulation of IbpreproHypSys in sweet potato.";
RL Plant Cell Environ. 39:1576-1587(2016).
RN [8]
RP INDUCTION.
RX PubMed=30824008; DOI=10.1016/j.plantsci.2018.12.011;
RA Lin H.H., King Y.C., Li Y.C., Lin C.C., Chen Y.C., Lin J.S., Jeng S.T.;
RT "The p38-like MAP kinase modulated H2O2 accumulation in wounding signaling
RT pathways of sweet potato.";
RL Plant Sci. 280:305-313(2019).
RN [9] {ECO:0007744|PDB:3R50, ECO:0007744|PDB:3R51, ECO:0007744|PDB:3R52, ECO:0007744|PDB:4DDN}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) AND IN COMPLEX WITH CARBOHYDRATES,
RP SUBUNIT, REGION, AND MUTAGENESIS OF 1-MET--ASP-10.
RX PubMed=22808208; DOI=10.1371/journal.pone.0040618;
RA Chang W.C., Liu K.L., Hsu F.C., Jeng S.T., Cheng Y.S.;
RT "Ipomoelin, a jacalin-related lectin with a compact tetrameric association
RT and versatile carbohydrate binding properties regulated by its N
RT terminus.";
RL PLoS ONE 7:e40618-e40618(2012).
CC -!- FUNCTION: Lectin involved in defense reactions of the leaves in
CC response to wounding by herbivorous insects and pathogens (Probable).
CC Retards the growth and development of silkworm thus reducing their
CC survival rates. Has hemagglutinating activity against human
CC erythrocytes (Ref.4). {ECO:0000269|Ref.4}.
CC -!- ACTIVITY REGULATION: Hemagglutinating activity is completely inhibited
CC by methyl alpha-D-glucopyranoside or methyl alpha-D-mannopyranoside.
CC The activity is also inhibited by maltose, glucose, galactose, mannose
CC and lactose, but not by polygalacturonic acid, mannitol, sorbitol or
CC sucrose. {ECO:0000269|Ref.4}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:22808208}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves (at protein level)
CC (PubMed:9249986, Ref.4). Expressed in leaves and to a lesser extent in
CC petioles. Not expressed in stems or tuberous roots (PubMed:9249986).
CC {ECO:0000269|PubMed:9249986, ECO:0000269|Ref.4}.
CC -!- INDUCTION: By wounding of the leaves (at protein level). Expressed in
CC unwounded leaves on day 7, indicating factors in senescence may up-
CC regulate the expression (at protein level) (Ref.4). By plant hormone
CC methyl jasmonate (MJ) in leaves and to a lesser extent in petioles, but
CC not in stems or roots (at protein level) (PubMed:9249986). In leaves,
CC both local and systemic expression is induced by mechanical wounding.
CC Increased expression is detected in wounded local leaves after 6 hours,
CC but expression decreases at 12 hours after wounding (PubMed:9249986,
CC Ref.2, PubMed:12746543). An increased expression is also detected in
CC the opposite non-wounded half of the main vein of leaves and in
CC neighboring non-wounded leaves. Not induced by treatment of leaves with
CC 20 uM abscisic acid (ABA), 1% NaCl or 6% sucrose (PubMed:9249986). In
CC response to wounding in leaves, up-regulated by MJ, ethylene (ET) and
CC hydrogen peroxide (H(2)O(2)), via activation of the MAPK signaling
CC cascades (Ref.2, PubMed:12746543, PubMed:17971062, PubMed:25063862,
CC PubMed:30824008). Up-regulated by synthetic plant peptide hormone
CC hydroxyproline-rich glycopeptide (HypSys IV) upon wounding through the
CC action of jasmonate and H(2)O(2) (PubMed:26924170). Down-regulated by
CC nitric oxide (NO) produced by the NO synthase (PubMed:12746543).
CC {ECO:0000269|PubMed:12746543, ECO:0000269|PubMed:17971062,
CC ECO:0000269|PubMed:25063862, ECO:0000269|PubMed:26924170,
CC ECO:0000269|PubMed:30824008, ECO:0000269|PubMed:9249986,
CC ECO:0000269|Ref.2, ECO:0000269|Ref.4}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:9249986}.
CC -!- SIMILARITY: Belongs to the jacalin lectin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01088}.
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DR EMBL; D89823; BAA14024.1; -; mRNA.
DR PIR; T10940; T10940.
DR PDB; 3R50; X-ray; 2.27 A; A/B/C/D/E=1-154.
DR PDB; 3R51; X-ray; 2.10 A; A/B=1-154.
DR PDB; 3R52; X-ray; 2.10 A; A/B/C/D=1-154.
DR PDB; 4DDN; X-ray; 1.90 A; A/B/C/D=1-154.
DR PDBsum; 3R50; -.
DR PDBsum; 3R51; -.
DR PDBsum; 3R52; -.
DR PDBsum; 4DDN; -.
DR AlphaFoldDB; P93193; -.
DR SMR; P93193; -.
DR UniLectin; P93193; -.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0002213; P:defense response to insect; IDA:UniProtKB.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IEP:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR CDD; cd09612; Jacalin; 1.
DR Gene3D; 2.100.10.30; -; 1.
DR InterPro; IPR001229; Jacalin-like_lectin_dom.
DR InterPro; IPR033734; Jacalin-like_lectin_dom_plant.
DR InterPro; IPR036404; Jacalin-like_lectin_dom_sf.
DR Pfam; PF01419; Jacalin; 1.
DR SMART; SM00915; Jacalin; 1.
DR SUPFAM; SSF51101; SSF51101; 1.
DR PROSITE; PS51752; JACALIN_LECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lectin.
FT CHAIN 1..154
FT /note="Ipomoelin"
FT /id="PRO_0000450440"
FT DOMAIN 10..153
FT /note="Jacalin-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT REGION 1..10
FT /note="Involved in regulating the binding affinity to
FT carbohydrates"
FT /evidence="ECO:0000269|PubMed:22808208"
FT BINDING 21
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:22808208,
FT ECO:0007744|PDB:3R51, ECO:0007744|PDB:3R52,
FT ECO:0007744|PDB:4DDN"
FT BINDING 97
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:22808208,
FT ECO:0007744|PDB:3R51, ECO:0007744|PDB:3R52,
FT ECO:0007744|PDB:4DDN"
FT BINDING 141..145
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:22808208,
FT ECO:0007744|PDB:3R51, ECO:0007744|PDB:3R52,
FT ECO:0007744|PDB:4DDN"
FT MUTAGEN 1..10
FT /note="Missing: Loss of homotetramerization."
FT /evidence="ECO:0000269|PubMed:22808208"
FT STRAND 11..18
FT /evidence="ECO:0007829|PDB:4DDN"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:4DDN"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:4DDN"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:3R51"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:4DDN"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:4DDN"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:4DDN"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:3R50"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:4DDN"
FT STRAND 84..94
FT /evidence="ECO:0007829|PDB:4DDN"
FT STRAND 97..109
FT /evidence="ECO:0007829|PDB:4DDN"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:4DDN"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:4DDN"
FT STRAND 131..153
FT /evidence="ECO:0007829|PDB:4DDN"
SQ SEQUENCE 154 AA; 16504 MW; CEE3D50C7FFC3E08 CRC64;
MALQLAAHSD ARSGPVGSNG GQFWSFRPVR PLNKIVLSFS GSPDQTLNLI SITFSSNPTD
IITVGGVGPE PLTYTETVNI DGDIIEISGM IANYKGYNVI RSIKFTTNKK EYGPYGANAG
TPFNIKIPDG NKIVGFFGNS GWYVDAIGAY YTAK
