ID   LEC1_EUCSE              Reviewed;         268 AA.
AC   P84331;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Lectin ESA-2;
OS   Eucheuma serra (Marine red alga) (Sphaerococcus serra).
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC   Solieriaceae; Eucheuma.
OX   NCBI_TaxID=38516;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RX   PubMed=17259190; DOI=10.1093/glycob/cwm007;
RA   Hori K., Sato Y., Ito K., Fujiwara Y., Iwamoto Y., Makino H., Kawakubo A.;
RT   "Strict specificity for high-mannose type N-glycans and primary structure
RT   of a red alga Eucheuma serra lectin.";
RL   Glycobiology 17:479-491(2007).
RN   [2] {ECO:0000305}
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RA   Kawakubo A., Makino H., Ohnishi J., Hirohara H., Hori K.;
RT   "The marine red alga Eucheuma serra J. Agardh, a high yielding source of
RT   two isolectins.";
RL   J. Appl. Phycol. 9:331-338(1997).
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 sheep and
CC       rabbit erythrocytes and untreated sheep erythrocytes. Has mitogenic
CC       activity on mouse lymphocytes. Does not require metal ions for
CC       activity. {ECO:0000269|PubMed:17259190, ECO:0000269|Ref.2}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Stable over a wide pH range, activity is unaffected after incubation
CC         at pH 2.5-10.5. {ECO:0000269|Ref.2};
CC       Temperature dependence:
CC         Activity is unaffected by heating at 60 degrees Celsius for 1 hour.
CC         Activity gradually decreases after incubation at higher temperatures.
CC         {ECO:0000269|Ref.2};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|Ref.2}.
CC   -!- MASS SPECTROMETRY: Mass=27949; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17259190};
CC   -!- SIMILARITY: Belongs to the bacterial lectin family. {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   AlphaFoldDB; P84331; -.
DR   SMR; P84331; -.
DR   GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR   InterPro; IPR040964; SBD.
DR   Pfam; PF17882; SBD; 4.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hemagglutinin; Lectin; Mannose-binding; Repeat.
FT   CHAIN           1..268
FT                   /note="Lectin ESA-2"
FT                   /id="PRO_0000282940"
FT   REPEAT          1..67
FT                   /note="1"
FT                   /evidence="ECO:0000269|PubMed:17259190"
FT   REPEAT          68..135
FT                   /note="2"
FT                   /evidence="ECO:0000269|PubMed:17259190"
FT   REPEAT          136..202
FT                   /note="3"
FT                   /evidence="ECO:0000269|PubMed:17259190"
FT   REPEAT          203..268
FT                   /note="4"
FT                   /evidence="ECO:0000269|PubMed:17259190"
FT   REGION          1..268
FT                   /note="4 X approximate tandem repeats"
FT                   /evidence="ECO:0000269|PubMed:17259190"
SQ   SEQUENCE   268 AA;  27950 MW;  06524906F5262746 CRC64;
     GRYTVQNQWG GSSAPWNDAG LWILGSRGNQ NVMAVDVNSS DGGANLNGTM TYSGEGPIGF
     KGARRGESNV YDVENQWGGS SAPWHAGGQF VIGSRSGQGV LAVNITSSDG GKTLTGTMTY
     EREGPIGFKG TQSGGDTYNV ENQWGGSSAP WNKAGIWALG DRSGQAMIAM DVSSSDGGKT
     LEGTMQYKGE GPIGFRGKLS GANNYSVENQ WGGSSAPWNA AGDWLIGDRH NQNITAVKVS
     SDNDGKNLDG TCTYEREGPI GFKGVATS