ID   DB3L_DIOPO              Reviewed;         272 AA.
AC   Q75N35;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Dioscorin DB3L {ECO:0000305};
DE   AltName: Full=Tuber storage protein DB3L {ECO:0000305};
DE   Flags: Precursor;
GN   Name=DB3L {ECO:0000312|EMBL:BAD18020.1};
OS   Dioscorea polystachya (Chinese yam).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Dioscoreales; Dioscoreaceae;
OC   Dioscorea.
OX   NCBI_TaxID=55575;
RN   [1] {ECO:0000312|EMBL:BAD18020.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-267, FUNCTION, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY,
RP   PTM, IDENTIFICATION BY MASS SPECTROMETRY, AND DISULFIDE BONDS.
RC   TISSUE=Tuber {ECO:0000303|PubMed:15047697, ECO:0000312|EMBL:BAD18020.1};
RX   PubMed=15047697; DOI=10.1074/jbc.m402139200;
RA   Gaidamashvili M., Ohizum Y., Iijima S., Takayama T., Ogawa T., Muramoto K.;
RT   "Characterization of the yam tuber storage proteins from Dioscorea batatas
RT   exhibiting unique lectin activities.";
RL   J. Biol. Chem. 279:26028-26035(2004).
CC   -!- FUNCTION: Maltose-binding lectin. No affinity is detected toward
CC       glucose. Has hemagglutinating activity against rabbit erythrocytes at
CC       3.9 ug/ml. No carbonate dehydratase or trypsin inhibitor activity
CC       detected by measuring the hydrolysis of 4-nitrophenyl acetate or the
CC       inhibition of bovine trypsin-catalyzed hydrolysis of N-benzoyl-L-
CC       arginine ethyl ester, respectively. {ECO:0000269|PubMed:15047697}.
CC   -!- ACTIVITY REGULATION: Loss of hemagglutinating activity by EDTA
CC       treatment. The activity is fully recovered by the addition of 5 mM
CC       Ca(2+) ions, but not with Mg(2+) and Mn 2(+). Hemagglutination activity
CC       is inhibited by maltose and its derivatives, with maltopentaose and
CC       maltohexaose being the best inhibitors followed by maltose and iso
CC       maltose. Not inhibited by glycoproteins. {ECO:0000269|PubMed:15047697}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Full hemagglutinating activity after 3 hours of incubation at pH 3-9
CC         at room temperature. {ECO:0000269|PubMed:15047697};
CC       Temperature dependence:
CC         The hemagglutinating activity is stable at 50 degrees Celsius up to
CC         40 min, but decreases to 50% after 80 min.
CC         {ECO:0000269|PubMed:15047697};
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:15047697}.
CC   -!- TISSUE SPECIFICITY: Expressed in tuber (at protein level).
CC       {ECO:0000269|PubMed:15047697}.
CC   -!- PTM: Not glycosylated. {ECO:0000269|PubMed:15047697}.
CC   -!- SIMILARITY: Belongs to the alpha-class carbonic anhydrase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Despite overall sequence similarity to the typical alpha class
CC       carbonic anhydrases, lacks one of the three conserved catalytic zinc-
CC       ligand histidines. {ECO:0000305}.
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   EMBL; AB178472; BAD18020.1; -; mRNA.
DR   AlphaFoldDB; Q75N35; -.
DR   SMR; Q75N35; -.
DR   GO; GO:0048030; F:disaccharide binding; IDA:UniProtKB.
DR   GO; GO:1901982; F:maltose binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd03124; alpha_CA_prokaryotic_like; 1.
DR   Gene3D; 3.10.200.10; -; 1.
DR   InterPro; IPR041891; Alpha_CA_prokaryot-like.
DR   InterPro; IPR001148; CA_dom.
DR   InterPro; IPR036398; CA_dom_sf.
DR   InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR   PANTHER; PTHR18952; PTHR18952; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; SSF51069; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Lectin; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:15047697"
FT   CHAIN           26..272
FT                   /note="Dioscorin DB3L"
FT                   /evidence="ECO:0000305|PubMed:15047697"
FT                   /id="PRO_5004286874"
FT   DOMAIN          28..263
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   DISULFID        53..213
FT                   /evidence="ECO:0000305|PubMed:15047697"
FT   DISULFID        65
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305|PubMed:15047697"
SQ   SEQUENCE   272 AA;  31023 MW;  0658ABBB71273951 CRC64;
     MSSSTLFHLF LLSSLLFSCL SNARPDEDDF SYIEGSPNGP ENWGNLNPEW KTCGNGMEQS
     PINLCDDRVI QTPALGKLRT SYQAARATLK NNGHDIMVNF KSDAGSQFIN QVRYQLKRIH
     FHSPSEHVLN GERFDLEVQM VHESQDQRRA VTAILFRFGR SDPFLSDLED FISQISKSEK
     NEVDAGVVDP RQLLQFDDPA YYRYMGSFTA PPCTEDITWT VIKKLGTVSP RQVLMLKQAV
     NENAINNARP LQPLKFRTIF FYPRQKSNHD AI