ID   LEC1_PLAAG              Reviewed;         132 AA.
AC   P84330;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Lectin OAA;
OS   Planktothrix agardhii (Oscillatoria agardhii).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Planktothrix.
OX   NCBI_TaxID=1160;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   STRAIN=NIES-204 / IAM M-244 / CCAP 1460/5 / PCC 10704;
RX   PubMed=17314091; DOI=10.1074/jbc.m701252200;
RA   Sato Y., Okuyama S., Hori K.;
RT   "Primary structure and carbohydrate binding specificity of a potent anti-
RT   HIV lectin isolated from the filamentous cyanobacterium Oscillatoria
RT   agardhii.";
RL   J. Biol. Chem. 282:11021-11029(2007).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-20, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RC   STRAIN=NIES-204 / IAM M-244 / CCAP 1460/5 / PCC 10704;
RX   PubMed=10817903; DOI=10.1016/s0305-0491(99)00164-9;
RA   Sato Y., Murakami M., Miyazawa K., Hori K.;
RT   "Purification and characterization of a novel lectin from a freshwater
RT   cyanobacterium, Oscillatoria agardhii.";
RL   Comp. Biochem. Physiol. 125B:169-177(2000).
CC   -!- FUNCTION: Lectin specific for high mannose N-glycans, recognizes the
CC       branched moiety of these glycans. Does not recognize other types of N-
CC       glycans or monosaccharides. Agglutinates trypsin-treated rabbit
CC       erythrocytes. Does not require divalent cations for activity. Inhibits
CC       HIV replication in MT4 cells with an EC(50) of 45 nM. Binds to the HIV
CC       envelope glycoprotein gp120. {ECO:0000269|PubMed:10817903,
CC       ECO:0000269|PubMed:17314091}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Stable over a wide pH range, activity is unaffected after incubation
CC         at pH 4.0-11.0. {ECO:0000269|PubMed:10817903};
CC       Temperature dependence:
CC         Thermostable. Activity is unaffected by heating at 80 degrees Celsius
CC         for 30 minutes, half of the original activity is retained after
CC         heating at 100 degrees Celsius for 30 minutes.
CC         {ECO:0000269|PubMed:10817903};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10817903}.
CC   -!- MASS SPECTROMETRY: Mass=13924.1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17314091};
CC   -!- SIMILARITY: Belongs to the bacterial lectin family. {ECO:0000305}.
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DR   PDB; 2MWH; NMR; -; A=1-130.
DR   PDB; 3S5V; X-ray; 1.55 A; A=1-130.
DR   PDB; 3S5X; X-ray; 1.65 A; A=1-130.
DR   PDB; 3S60; X-ray; 1.60 A; A=1-130.
DR   PDBsum; 2MWH; -.
DR   PDBsum; 3S5V; -.
DR   PDBsum; 3S5X; -.
DR   PDBsum; 3S60; -.
DR   AlphaFoldDB; P84330; -.
DR   BMRB; P84330; -.
DR   SMR; P84330; -.
DR   UniLectin; P84330; -.
DR   GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR   InterPro; IPR040964; SBD.
DR   Pfam; PF17882; SBD; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Hemagglutinin; Lectin;
KW   Mannose-binding; Repeat.
FT   CHAIN           1..132
FT                   /note="Lectin OAA"
FT                   /id="PRO_0000282941"
FT   REPEAT          1..66
FT                   /note="1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          67..132
FT                   /note="2"
FT                   /evidence="ECO:0000255"
FT   REGION          1..132
FT                   /note="2 X approximate tandem repeats"
FT                   /evidence="ECO:0000255"
FT   STRAND          2..8
FT                   /evidence="ECO:0007829|PDB:3S5V"
FT   STRAND          16..23
FT                   /evidence="ECO:0007829|PDB:3S5V"
FT   STRAND          32..38
FT                   /evidence="ECO:0007829|PDB:3S5V"
FT   STRAND          44..52
FT                   /evidence="ECO:0007829|PDB:3S5V"
FT   STRAND          57..66
FT                   /evidence="ECO:0007829|PDB:3S5V"
FT   STRAND          69..75
FT                   /evidence="ECO:0007829|PDB:3S5V"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:3S60"
FT   STRAND          84..90
FT                   /evidence="ECO:0007829|PDB:3S5V"
FT   STRAND          93..96
FT                   /evidence="ECO:0007829|PDB:2MWH"
FT   STRAND          99..105
FT                   /evidence="ECO:0007829|PDB:3S5V"
FT   STRAND          111..119
FT                   /evidence="ECO:0007829|PDB:3S5V"
FT   STRAND          124..130
FT                   /evidence="ECO:0007829|PDB:3S5V"
SQ   SEQUENCE   132 AA;  13926 MW;  534D4720E4FCAF40 CRC64;
     ALYNVENQWG GSSAPWNEGG QWEIGSRSDQ NVVAINVESG DDGQTLNGTM TYAGEGPIGF
     RATLLGNNSY EVENQWGGDS APWHSGGNWI LGSRENQNVV AINVESGDDG QTLNGTMTYA
     GEGPIGFKGT TL