ASAL_ALLSA
ID ASAL_ALLSA Reviewed; 181 AA.
AC P83886; P92930; P92931; Q19K88; Q5I1X6; Q679P1;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 3.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Mannose-specific lectin;
DE AltName: Full=ASAL;
DE AltName: Full=ASARI;
DE AltName: Full=Allimin;
DE AltName: Full=Leaf agglutinin;
DE AltName: Full=Root agglutinin;
DE Flags: Precursor;
GN Name=LECASAL {ECO:0000303|PubMed:9037141};
GN Synonyms=LECASARI {ECO:0000303|PubMed:9037141};
OS Allium sativum (Garlic).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC Allioideae; Allieae; Allium.
OX NCBI_TaxID=4682;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB64237.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 31-49; 56-70
RP AND 88-102, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC TISSUE=Leaf {ECO:0000269|PubMed:9037141}, and
RC Root {ECO:0000312|EMBL:AAB64237.1};
RX PubMed=9037141; DOI=10.1023/a:1005717020021;
RA Smeets K., Van Damme E.J.M., Verhaert P., Barre A., Rouge P.,
RA Van Leuven F., Peumans W.J.;
RT "Isolation, characterization and molecular cloning of the mannose-binding
RT lectins from leaves and roots of garlic (Allium sativum L.).";
RL Plant Mol. Biol. 33:223-234(1997).
RN [2] {ECO:0000305, ECO:0000312|EMBL:ABF70332.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Leaf {ECO:0000312|EMBL:ABF70332.1};
RA Khareedu V.R., Mendu V., Vudem D.R.;
RT "Insecticidal activity of garlic (Allium sativum) lectin.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAW48531.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-181 (ISOFORM 2).
RC TISSUE=Leaf {ECO:0000312|EMBL:AAW48531.1};
RX AGRICOLA=IND43762706; DOI=10.1016/j.plantsci.2005.05.016;
RA Dutta I., Majumder P., Saha P., Ray K., Das S.;
RT "Constitutive and phloem specific expression of Allium sativum leaf
RT agglutinin (ASAL) to engineer aphid (Lipaphis erysimi) resistance in
RT transgenic Indian mustard (Brassica juncea).";
RL Plant Sci. 169:996-1007(2005).
RN [4] {ECO:0000305, ECO:0000312|EMBL:ABF70332.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-148 (ISOFORM 1).
RC TISSUE=Leaf {ECO:0000312|EMBL:AAR23523.1};
RA Hossain M.A., Maiti M.K., Basu A., Sen S.K.;
RT "Mannose-binding lectin of onion is a potential biopesticide against plant
RT sap-sucking insects.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:ABF70332.1}
RP PROTEIN SEQUENCE OF 31-65.
RA Chakraborty K., Girish G.V., Mohapatra S., Kahn N.N., Sinha K.A.;
RT "Allimin.";
RL Submitted (APR-2004) to UniProtKB.
RN [6] {ECO:0000305}
RP PROTEIN SEQUENCE OF 47-56; 90-99 AND 125-141 (ISOFORM 1), AND FUNCTION.
RX PubMed=17265166; DOI=10.1007/s11248-007-9069-z;
RA Sadeghi A., Smagghe G., Broeders S., Hernalsteens J.-P., De Greve H.,
RA Peumans W.J., Van Damme E.J.M.;
RT "Ectopically expressed leaf and bulb lectins from garlic (Allium sativum
RT L.) protect transgenic tobacco plants against cotton leafworm (Spodoptera
RT littoralis).";
RL Transgenic Res. 17:9-18(2008).
RN [7] {ECO:0000305}
RP FUNCTION.
RC TISSUE=Leaf {ECO:0000269|PubMed:17147631};
RX PubMed=17147631; DOI=10.1111/j.1467-7652.2005.00151.x;
RA Dutta I., Saha P., Majumder P., Sarkar A., Chakraborti D., Banerjee S.,
RA Das S.;
RT "The efficacy of a novel insecticidal protein, Allium sativum leaf lectin
RT (ASAL), against homopteran insects monitored in transgenic tobacco.";
RL Plant Biotechnol. J. 3:601-611(2005).
CC -!- FUNCTION: Mannose-specific lectin. Shows agglutinating activity towards
CC rabbit erythrocytes, but not human erythrocytes. Has insecticidal
CC activity against the cotton leafworm S.littoralis and the peach potato
CC aphid M.persicae. {ECO:0000269|PubMed:17147631,
CC ECO:0000269|PubMed:17265166, ECO:0000269|PubMed:9037141}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9037141}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P49329}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:9037141};
CC IsoId=P83886-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|Ref.3};
CC IsoId=P83886-2; Sequence=VSP_030211, VSP_030212;
CC -!- MASS SPECTROMETRY: Mass=12382; Method=MALDI; Note=Leaf agglutinin.;
CC Evidence={ECO:0000269|PubMed:9037141};
CC -!- MASS SPECTROMETRY: Mass=15682; Method=MALDI; Note=Root agglutinin.;
CC Evidence={ECO:0000269|PubMed:9037141};
CC -!- MISCELLANEOUS: Controls hyperglycemia in diabetic mice. Also shows some
CC insulin mimetic effects in vitro, including activation of tyrosine
CC kinase, PI3 kinase and stimulation of nitric oxide synthesis.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW48531.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U58947; AAB64237.1; -; mRNA.
DR EMBL; U58948; AAB64238.1; -; mRNA.
DR EMBL; DQ525625; ABF70332.1; -; mRNA.
DR EMBL; AY866499; AAW48531.1; ALT_INIT; mRNA.
DR EMBL; AY376827; AAR23523.1; -; mRNA.
DR AlphaFoldDB; P83886; -.
DR SMR; P83886; -.
DR IntAct; P83886; 4.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005537; F:mannose binding; IMP:AgBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:AgBase.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:AgBase.
DR GO; GO:0002213; P:defense response to insect; TAS:AgBase.
DR CDD; cd00028; B_lectin; 1.
DR Gene3D; 2.90.10.10; -; 1.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR SMART; SM00108; B_lectin; 1.
DR SUPFAM; SSF51110; SSF51110; 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond; Lectin;
KW Mannose-binding; Plant defense; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:9037141, ECO:0000269|Ref.5"
FT CHAIN 31..181
FT /note="Mannose-specific lectin"
FT /evidence="ECO:0000269|PubMed:9037141"
FT /id="PRO_0000064564"
FT DOMAIN 31..140
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DISULFID 59..83
FT /evidence="ECO:0000250|UniProtKB:P49329,
FT ECO:0000255|PROSITE-ProRule:PRU00038"
FT VAR_SEQ 138..148
FT /note="YRRSVGGAVVM -> LLEHRVPTSFY (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_030211"
FT VAR_SEQ 149..181
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_030212"
FT CONFLICT 3
FT /note="R -> P (in Ref. 2; ABF70332)"
FT /evidence="ECO:0000305"
FT CONFLICT 32..34
FT /note="NVL -> MIP (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="V -> L (in Ref. 1; AAB64237, 3; AAW48531 and 4;
FT AAR23523)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="D -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 56..59
FT /note="QDDC -> RPDD (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="V -> R (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="N -> S (in Ref. 4; AAR23523)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="V -> L (in Ref. 1; AAB64237 and 4; AAR23523)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="K -> E (in Ref. 1; AAB64237 and 4; AAR23523)"
FT /evidence="ECO:0000305"
FT CONFLICT 168..169
FT /note="NV -> KD (in Ref. 2; ABF70332)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="T -> S (in Ref. 1; AAB64237)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 181 AA; 19282 MW; 4D89A957F75A753D CRC64;
MGRTTSSPKA MMRIATVAAI LTILASTCMA RNVLTNGEGL YAGQSLDVEQ YKFIMQDDCN
LVLYEYSTPI WASNTGVTGK NGCRAVMQRD GNFVVYDVNG RPVWASNSVR GNGNYILVLQ
KDRNVVIYGS DIWSTGTYRR SVGGAVVMAM NGTVDGGSVI GPVVVNQNVT AAIRKVGTGA
A
