ID   LEC_VACFA               Reviewed;         225 AA.
AC   P84849;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Lectin {ECO:0000303|PubMed:18568300};
DE            Short=AFAL;
OS   Vachellia farnesiana (Sweet acacia) (Acacia farnesiana).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Caesalpinioideae; mimosoid clade;
OC   Acacieae; Vachellia.
OX   NCBI_TaxID=72368;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC   TISSUE=Seed {ECO:0000269|PubMed:18568300};
RX   PubMed=18568300; DOI=10.1007/s12010-008-8144-0;
RA   Santi-Gadelha T., Rocha B.A.M., Oliveira C.C., Aragao K.S., Marinho E.S.,
RA   Gadelha C.A.A., Toyama M.H., Pinto V.P.T., Nagano C.S., Delatorre P.,
RA   Martins J.L., Galvani F.R., Sampaio A.H., Debray H., Cavada B.S.;
RT   "Purification of a PHA-like chitin-binding protein from Acacia farnesiana
RT   seeds: a time-dependent oligomerization protein.";
RL   Appl. Biochem. Biotechnol. 150:97-111(2008).
CC   -!- FUNCTION: Chitin-binding lectin. Agglutinates rabbit erythrocytes, but
CC       not human erythrocytes. {ECO:0000269|PubMed:18568300}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:18568300}.
CC   -!- MASS SPECTROMETRY: Mass=24257.84; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18568300};
CC   -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P84849; -.
DR   SMR; P84849; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR016363; L-lectin.
DR   InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR   InterPro; IPR001220; Legume_lectin_dom.
DR   Pfam; PF00139; Lectin_legB; 1.
DR   PIRSF; PIRSF002690; L-type_lectin_plant; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lectin.
FT   CHAIN           1..225
FT                   /note="Lectin"
FT                   /id="PRO_0000309556"
SQ   SEQUENCE   225 AA;  25063 MW;  A6B68B3D7A16BCDE CRC64;
     FKNLNFNEQS LILQGDATVS STGRLTNVVD NGEPRTSSLG RAFYSAPIWD KPTGRLASWR
     EKIQEPNKAG PADGMAFALV PVGSEPKDKG AGLLGLFDEY DSNRHPVAVE FDTCYNLEHD
     PKERHSIRSI ATPRWDFPNG ENAEVLITYD EELQLLVASL VYPGERPYYL PSDRVEIEDE
     LPEYVIPGFS ATRGLNEGET HDVLSWSFAS KMPDEQESEG LDLAE