LEC1_REMVI
ID LEC1_REMVI Reviewed; 256 AA.
AC B5LYJ9;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Mannose-specific lectin 1 {ECO:0000305};
DE AltName: Full=Agglutinin {ECO:0000305};
DE Contains:
DE RecName: Full=Mannose-specific lectin 1 chain 1 {ECO:0000305};
DE Contains:
DE RecName: Full=Mannose-specific lectin 1 chain 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=L1 {ECO:0000303|Ref.1}; Synonyms=RVL {ECO:0000303|PubMed:21788359};
OS Remusatia vivipara (Hitchhiker elephant ear) (Arum viviparum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Araceae; Aroideae; Colocasieae;
OC Remusatia.
OX NCBI_TaxID=189456;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Neekhra V., Bhat R.S., Chandrashekar T.M., Bhat G., Basingi S.M.,
RA Udikeri S.S., Swamy B.M., Kuruvinashetti M.S.;
RT "Cloning and expression of a novel mannose-binding lectin gene from
RT Remusatia vivipara.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 24-132 AND 140-249, DISULFIDE
RP BONDS, PROTEIN SEQUENCE OF 24-31 AND 140-147, AND SUBUNIT.
RX PubMed=21788359; DOI=10.1093/glycob/cwr100;
RA Shetty K.N., Bhat G.G., Inamdar S.R., Swamy B.M., Suguna K.;
RT "Crystal structure of a beta-prism II lectin from Remusatia vivipara.";
RL Glycobiology 22:56-69(2012).
CC -!- FUNCTION: Mannose-specific lectin. Shows agglutinating activity towards
CC erythrocytes from rabbit. {ECO:0000250|UniProtKB:R9RL27}.
CC -!- SUBUNIT: Forms heterodimers. {ECO:0000269|PubMed:21788359}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR EMBL; EU924066; ACH41914.1; -; Genomic_DNA.
DR PDB; 3R0E; X-ray; 2.40 A; A/C=24-132, B/D=140-249.
DR PDBsum; 3R0E; -.
DR AlphaFoldDB; B5LYJ9; -.
DR SMR; B5LYJ9; -.
DR UniLectin; B5LYJ9; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR CDD; cd00028; B_lectin; 2.
DR Gene3D; 2.90.10.10; -; 2.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR SMART; SM00108; B_lectin; 2.
DR SUPFAM; SSF51110; SSF51110; 2.
DR PROSITE; PS50927; BULB_LECTIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hemagglutinin;
KW Lectin; Mannose-binding; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:21788359"
FT CHAIN 24..139
FT /note="Mannose-specific lectin 1 chain 1"
FT /id="PRO_5002836532"
FT CHAIN 140..256
FT /note="Mannose-specific lectin 1 chain 2"
FT /id="PRO_0000450782"
FT DOMAIN 26..131
FT /note="Bulb-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DOMAIN 145..252
FT /note="Bulb-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT MOTIF 51..59
FT /note="Carbohydrate-binding motif 1"
FT /evidence="ECO:0000305|PubMed:21788359"
FT MOTIF 170..178
FT /note="Carbohydrate-binding motif 2"
FT /evidence="ECO:0000305|PubMed:21788359"
FT BINDING 51..55
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:A5HMM7"
FT BINDING 59
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:A5HMM7"
FT BINDING 63
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:R9RL27"
FT BINDING 64
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:A5HMM7"
FT BINDING 170..174
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:R9RL27"
FT BINDING 178
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:Q39487"
FT BINDING 182..185
FT /ligand="beta-D-mannose"
FT /ligand_id="ChEBI:CHEBI:28563"
FT /evidence="ECO:0000250|UniProtKB:Q39487"
FT DISULFID 54..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038,
FT ECO:0000269|PubMed:21788359, ECO:0007744|PDB:3R0E"
FT DISULFID 173..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038,
FT ECO:0000269|PubMed:21788359, ECO:0007744|PDB:3R0E"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:3R0E"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:3R0E"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:3R0E"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:3R0E"
SQ SEQUENCE 256 AA; 28100 MW; A6388CF15EDA62D3 CRC64;
MAKLLLFLLP AILGLLVPRS AVALGTNYLL SGQTLDTEGH LKNGDFDLVM QDDCNLVLYN
GNWQSNTANN GRDCKLTLTD YGELVIKNGD GSTVWKSGAQ SVKGNYAAVV HPDGRLVVLG
PSVFKIDPWV RGLNSLRFRN IPFTNNLLFS GQVLYGDGRL TAKNHQLVMQ GDCNLVLYGG
KYGWQSNTHG NGEHCFLRLN HKGELIIKDD DFKTIWSSRS SSKQGEYVLI LQDDGFGVIY
GPAIFETSSK RSIAAS
