ID   LEC1_HYPCE              Reviewed;          90 AA.
AC   P84870;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Lectin-1;
DE   AltName: Full=HCA;
DE   Contains:
DE     RecName: Full=Lectin-1 N-terminal subunit;
DE   Contains:
DE     RecName: Full=Lectin-1 C-terminal subunit;
OS   Hypnea cervicornis (Brazilian red alga).
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC   Hypneaceae; Hypnea.
OX   NCBI_TaxID=387623;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1, FUNCTION, CLEAVAGE,
RP   DISULFIDE BONDS, AND MASS SPECTROMETRY.
RX   PubMed=16046632; DOI=10.1110/ps.051498505;
RA   Nagano C.S., Debray H., Nascimento K.S., Pinto V.P.T., Cavada B.S.,
RA   Saker-Sampaio S., Farias W.R.L., Sampaio A.H., Calvete J.J.;
RT   "HCA and HML isolated from the red marine algae Hypnea cervicornis and
RT   Hypnea musciformis define a novel lectin family.";
RL   Protein Sci. 14:2167-2176(2005).
CC   -!- FUNCTION: Lectin with specificity for complex N-linked glycans and O-
CC       linked glycans. Has hemagglutinating activity towards rabbit
CC       erythrocytes that is inhibited by N-acetyl-D-galactosamine.
CC       {ECO:0000269|PubMed:16046632}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:16046632}.
CC   -!- PTM: Contains seven disulfide bonds. {ECO:0000269|PubMed:16046632,
CC       ECO:0000305}.
CC   -!- PTM: Proteolytically cleaved. Major form may consist of cleaved,
CC       disulfide-bonded subunits. {ECO:0000269|PubMed:16046632}.
CC   -!- MASS SPECTROMETRY: [Lectin-1]: Mass=9193; Mass_error=3; Method=MALDI;
CC       Note=The measured mass is that of the native single chain.;
CC       Evidence={ECO:0000269|PubMed:16046632};
CC   -!- MASS SPECTROMETRY: [Lectin-1]: Mass=9990; Method=MALDI; Note=The
CC       measured mass is that of the reduced and carbamidomethylated single
CC       chain.; Evidence={ECO:0000269|PubMed:16046632};
CC   -!- MASS SPECTROMETRY: [Lectin-1 N-terminal subunit]: Mass=5643;
CC       Method=MALDI; Note=The measured mass is that of the reduced and
CC       carbamidomethylated N-terminal subunit.;
CC       Evidence={ECO:0000269|PubMed:16046632};
CC   -!- MASS SPECTROMETRY: [Lectin-1 C-terminal subunit]: Mass=4380;
CC       Method=MALDI; Note=The measured mass is that of the reduced and
CC       carbamidomethylated C-terminal subunit.;
CC       Evidence={ECO:0000269|PubMed:16046632};
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DR   AlphaFoldDB; P84870; -.
DR   GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hemagglutinin; Lectin;
KW   Pyrrolidone carboxylic acid.
FT   CHAIN           1..90
FT                   /note="Lectin-1"
FT                   /id="PRO_0000245158"
FT   CHAIN           1..50
FT                   /note="Lectin-1 N-terminal subunit"
FT                   /id="PRO_0000245159"
FT   CHAIN           51..90
FT                   /note="Lectin-1 C-terminal subunit"
FT                   /id="PRO_0000245160"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:16046632"
FT   DISULFID        46..71
FT                   /note="Interchain (between N-terminal and C-terminal
FT                   subunits)"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:16046632"
SQ   SEQUENCE   90 AA;  9194 MW;  DACFF313ACA32D4E CRC64;
     QKACTMDYFP VCCQIVLGGG AYTAGNPCSC QGFVASKGTC DNPYPCPCTT EAQFPVCCTT
     QWGLVSATGN CACGCMGGVP VSDGPCPEVY