ID   LEC1_CROVR              Reviewed;         267 AA.
AC   Q9FVA1;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Mannose-specific lectin 1;
DE   AltName: Full=Agglutinin {ECO:0000303|PubMed:10931189};
DE            Short=CVA {ECO:0000303|PubMed:10931189};
DE   AltName: Full=Mannose-binding lectin {ECO:0000303|PubMed:10931189};
DE   Contains:
DE     RecName: Full=Mannose-specific lectin 1 chain 1;
DE     AltName: Full=CVA-DOM1 {ECO:0000303|PubMed:10931189};
DE   Contains:
DE     RecName: Full=Mannose-specific lectin 1 chain 2;
DE     AltName: Full=CVA-DOM2 {ECO:0000303|PubMed:10931189};
DE   Flags: Precursor;
GN   Name=LECCVA1 {ECO:0000312|EMBL:AAG10402.1};
OS   Crocus vernus (Dutch crocus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Iridaceae;
OC   Crocoideae; Croceae; Crocus.
OX   NCBI_TaxID=87752;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAG10402.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RC   TISSUE=Tuber {ECO:0000269|PubMed:10931189};
RX   PubMed=10931189; DOI=10.1046/j.1432-1327.2000.01563.x;
RA   Van Damme E.J., Astoul C.H., Barre A., Rouge P., Peumans W.J.;
RT   "Cloning and characterization of a monocot mannose-binding lectin from
RT   Crocus vernus (family Iridaceae).";
RL   Eur. J. Biochem. 267:5067-5077(2000).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 145-168, FUNCTION, AND SUBUNIT.
RC   TISSUE=Bulb {ECO:0000269|PubMed:9325257};
RX   PubMed=9325257; DOI=10.1074/jbc.272.41.25455;
RA   Misaki A., Kakuta M., Meah Y., Goldstein I.J.;
RT   "Purification and characterization of the alpha-1,3-mannosylmannose-
RT   recognizing lectin of Crocus vernus bulbs.";
RL   J. Biol. Chem. 272:25455-25461(1997).
CC   -!- FUNCTION: Mannose-specific lectin. Has weak agglutinating activity
CC       towards trypsin-treated erythrocytes from rabbit but not from human.
CC       {ECO:0000269|PubMed:10931189, ECO:0000269|PubMed:9325257}.
CC   -!- SUBUNIT: Heterotetramer of 2 domain 1 and 2 domain 2 chains arranged as
CC       a dimer of domain 1/domain 2 heterodimers.
CC       {ECO:0000269|PubMed:10931189, ECO:0000269|PubMed:9325257}.
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DR   EMBL; AF233283; AAG10402.1; -; mRNA.
DR   AlphaFoldDB; Q9FVA1; -.
DR   SMR; Q9FVA1; -.
DR   PRIDE; Q9FVA1; -.
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; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hemagglutinin; Lectin;
KW   Mannose-binding; Repeat; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..144
FT                   /note="Mannose-specific lectin 1 chain 1"
FT                   /evidence="ECO:0000269|PubMed:10931189"
FT                   /id="PRO_0000395434"
FT   CHAIN           145..267
FT                   /note="Mannose-specific lectin 1 chain 2"
FT                   /evidence="ECO:0000269|PubMed:9325257"
FT                   /id="PRO_0000395435"
FT   DOMAIN          26..136
FT                   /note="Bulb-type lectin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   DOMAIN          150..260
FT                   /note="Bulb-type lectin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   DISULFID        54..76
FT                   /evidence="ECO:0000250|UniProtKB:P86626,
FT                   ECO:0000255|PROSITE-ProRule:PRU00038"
FT   DISULFID        178..203
FT                   /evidence="ECO:0000250|UniProtKB:P86626,
FT                   ECO:0000255|PROSITE-ProRule:PRU00038"
FT   CONFLICT        148
FT                   /note="R -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        160
FT                   /note="S -> Y (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   267 AA;  28573 MW;  31E76812921A8A47 CRC64;
     MAKSLVLSSL LLALLLAAPL ASLADNNVLL TGDVLHTDNQ LSFESAAFVM QGDCNLVLYN
     EAGGFQSNTH GRGVGCTLRL NNFGQLEIHS ANSNTPVWVS LRNGIPVRGD YAAVLGPDQH
     VTIYGPAIWS TPAPNRHERG ATVSNIPRVR NVLFSSQVMS DNAQLATRDY SLVMRDDCNL
     ALTKGSKTNI VWESGTSGRG QHCFMRLGHT GLIEISDDRL NTVWRSNTVG QEGDYVLILQ
     INGQAVVYGP AVWSTASPAR GGASAAL