ID   ADEL_APLDA              Reviewed;         217 AA.
AC   C0HK25;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Lectin ADEL {ECO:0000303|PubMed:28150103};
OS   Aplysia dactylomela (Spotted sea hare).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC   Aplysiidae; Aplysia.
OX   NCBI_TaxID=144766 {ECO:0000303|PubMed:28150103};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP   PRESENCE OF DISULFIDE BONDS, MASS SPECTROMETRY, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND GLYCOSYLATION AT ASN-30; ASN-102 AND ASN-126.
RC   TISSUE=Egg {ECO:0000303|PubMed:28150103};
RX   PubMed=28150103; DOI=10.1007/s10126-017-9728-x;
RA   Carneiro R.F., Torres R.C., Chaves R.P., de Vasconcelos M.A.,
RA   de Sousa B.L., Goveia A.C., Arruda F.V., Matos M.N., Matthews-Cascon H.,
RA   Freire V.N., Teixeira E.H., Nagano C.S., Sampaio A.H.;
RT   "Purification, biochemical characterization, and amino acid sequence of a
RT   novel type of lectin from Aplysia dactylomela eggs with
RT   antibacterial/antibiofilm potential.";
RL   Mar. Biotechnol. 19:49-64(2017).
CC   -!- FUNCTION: Binds in decreasing order of affinity: galacturonic acid, D-
CC       galactosamine, methyl-alpha-D-galactopyranoside and further galactose-
CC       containing carbohydrates. Has hemagglutinating activity against human
CC       and rabbit erythrocytes. {ECO:0000269|PubMed:28150103}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6-7. {ECO:0000269|PubMed:28150103};
CC       Temperature dependence:
CC         Activity is stable up to 60 degrees Celsius, then decreases and is
CC         lost at 80 degrees Celsius. {ECO:0000269|PubMed:28150103};
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:28150103}.
CC   -!- PTM: Contains disulfide bonds. {ECO:0000269|PubMed:28150103}.
CC   -!- MASS SPECTROMETRY: Mass=57228; Mass_error=2; Method=MALDI; Note=Dimer.;
CC       Evidence={ECO:0000269|PubMed:28150103};
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DR   AlphaFoldDB; C0HK25; -.
DR   iPTMnet; C0HK25; -.
DR   GO; GO:0005534; F:galactose binding; IDA:UniProtKB.
DR   GO; GO:0016936; F:galactoside binding; IDA:UniProtKB.
DR   GO; GO:0048032; F:galacturonate binding; IDA:UniProtKB.
DR   GO; GO:0030395; F:lactose binding; IDA:UniProtKB.
DR   GO; GO:1903777; F:melibiose binding; IDA:UniProtKB.
DR   GO; GO:0034120; P:positive regulation of erythrocyte aggregation; IDA:UniProtKB.
DR   InterPro; IPR021381; DUF3011.
DR   Pfam; PF11218; DUF3011; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hemagglutinin;
KW   Lectin.
FT   CHAIN           1..217
FT                   /note="Lectin ADEL"
FT                   /evidence="ECO:0000269|PubMed:28150103"
FT                   /id="PRO_0000439881"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:28150103"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:28150103"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:28150103"
FT   DISULFID        5..187
FT                   /evidence="ECO:0000303|PubMed:28150103"
FT   DISULFID        42..68
FT                   /evidence="ECO:0000303|PubMed:28150103"
FT   DISULFID        61..77
FT                   /evidence="ECO:0000303|PubMed:28150103"
FT   DISULFID        114..135
FT                   /evidence="ECO:0000303|PubMed:28150103"
FT   DISULFID        142..206
FT                   /evidence="ECO:0000303|PubMed:28150103"
FT   DISULFID        172
FT                   /note="Interchain"
FT                   /evidence="ECO:0000303|PubMed:28150103"
FT   VARIANT         4
FT                   /note="K -> M"
FT                   /evidence="ECO:0000269|PubMed:28150103"
FT   VARIANT         53
FT                   /note="A -> D"
FT                   /evidence="ECO:0000269|PubMed:28150103"
FT   VARIANT         199
FT                   /note="T -> A"
FT                   /evidence="ECO:0000269|PubMed:28150103"
SQ   SEQUENCE   217 AA;  24416 MW;  7C322DE7D920D91C CRC64;
     DPDKCKTIRV ESWSYKYAEK VVEDASYVLN MTVVDRQSAA ACTLGESFGY QKATLWVDHG
     CRADFKVCYL PVMPTECQTL RVESWNYKYA EKVVEGAALF INMTVEDRQS EASCDLDKSF
     GFYNQNSTVW VNHGCRADFN ICYLKGAVTT STINVSSWNY QYATKVLPAA SCIYSMRVVN
     QQSAAPCTLG TTYGFVANTM WVDDGCRADF KPSYYSP