ID   TAR1_COLES              Reviewed;         229 AA.
AC   Q43418;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 2.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Mannose-specific lectin TAR1 {ECO:0000305};
DE   AltName: Full=Agglutinin {ECO:0000305};
DE   AltName: Full=Tarin {ECO:0000303|PubMed:7787178};
DE   Contains:
DE     RecName: Full=Mannose-specific lectin TAR1 chain 1 {ECO:0000305};
DE   Contains:
DE     RecName: Full=Mannose-specific lectin TAR1 chain 2 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=TAR1 {ECO:0000303|PubMed:7787178};
OS   Colocasia esculenta (Wild taro) (Arum esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Araceae; Aroideae; Colocasieae;
OC   Colocasia.
OX   NCBI_TaxID=4460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 24-48 AND
RP   140-170.
RC   TISSUE=Stem;
RX   PubMed=7787178; DOI=10.1007/bf00042045;
RA   Bezerra I.C., Castro L.A., Neshich G., de Almeida E.R., de Sa M.F.,
RA   Mello L.V., Monte-Neshich D.C.;
RT   "A corm-specific gene encodes tarin, a major globulin of taro (Colocasia
RT   esculenta L. Schott).";
RL   Plant Mol. Biol. 28:137-144(1995).
CC   -!- FUNCTION: Mannose-specific lectin. Shows agglutinating activity towards
CC       erythrocytes from rabbit. {ECO:0000250|UniProtKB:R9RL27}.
CC   -!- SUBUNIT: Forms heterotetramer of 2 chains 1 and 2 chains 2 arranged as
CC       a dimer of chain 1 and chain 2 heterodimers.
CC       {ECO:0000250|UniProtKB:R9RL27}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA53717.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X76111; CAA53717.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q43418; -.
DR   SMR; Q43418; -.
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; 1.
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; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hemagglutinin; Lectin;
KW   Mannose-binding; Repeat; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:7787178"
FT   CHAIN           24..139
FT                   /note="Mannose-specific lectin TAR1 chain 1"
FT                   /id="PRO_5004231857"
FT   CHAIN           140..229
FT                   /note="Mannose-specific lectin TAR1 chain 2"
FT                   /id="PRO_0000450781"
FT   DOMAIN          26..131
FT                   /note="Bulb-type lectin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   DOMAIN          145..229
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"
FT   MOTIF           170..178
FT                   /note="Carbohydrate-binding motif 2"
FT                   /evidence="ECO:0000305"
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   DISULFID        173..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
SQ   SEQUENCE   229 AA;  25348 MW;  BEE83C4FCAF50CA1 CRC64;
     MAKLLLFLLP AILGLLIPRS AVALGTNYLL SGQTLNTDGH LKNGDFDLVM QNDCNLVLYN
     GNWQSNTANN GRDCKLTLTD YGDLVIKNRD GSTVWRSRAK SVKGNYAAVL HPDGRLVVFG
     PSVFKNDPWV PGLNSLAFRN IPFTDNLLFS PQVLYGDGRL TAKNHQLVMQ GDCNLVLYGG
     KYGWQSNTHG NGEHCFLRLN HKGELIIKDD DFKTIWSSSS SSKQGDYVL