ID   FEL_CYPCA               Reviewed;         238 AA.
AC   P68512;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Fish-egg lectin;
DE            Short=FEL;
OS   Cyprinus carpio (Common carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=7962;
RN   [1]
RP   PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-27, FUNCTION,
RP   SUBUNIT, AND TISSUE SPECIFICITY.
RC   TISSUE=Egg;
RX   PubMed=12956625; DOI=10.1042/bj20030413;
RA   Galliano M., Minchiotti L., Campagnoli M., Sala A., Visai L., Amoresano A.,
RA   Pucci P., Casbarra A., Cauci M., Perduca M., Monaco H.L.;
RT   "Structural and biochemical characterization of a new type of lectin
RT   isolated from carp eggs.";
RL   Biochem. J. 376:433-440(2003).
CC   -!- FUNCTION: Lipopolysaccharide-binding protein with a very low
CC       agglutinating activity for human A-type erythrocytes and interacts with
CC       both Gram-positive and Gram-negative bacteria.
CC       {ECO:0000269|PubMed:12956625}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in the eggs.
CC       {ECO:0000269|PubMed:12956625}.
CC   -!- SIMILARITY: Belongs to the tectonin family. {ECO:0000305}.
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DR   PDB; 4RUQ; X-ray; 1.35 A; A/B=1-238.
DR   PDB; 4RUS; X-ray; 1.70 A; A/B/C/D/E/F=1-238.
DR   PDBsum; 4RUQ; -.
DR   PDBsum; 4RUS; -.
DR   AlphaFoldDB; P68512; -.
DR   SMR; P68512; -.
DR   UniLectin; P68512; -.
DR   iPTMnet; P68512; -.
DR   Proteomes; UP000694384; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   InterPro; IPR006624; Beta-propeller_rpt_TECPR.
DR   Pfam; PF19193; Tectonin; 1.
DR   SMART; SM00706; TECPR; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Lectin; Reference proteome; Repeat; Secreted.
FT   CHAIN           1..238
FT                   /note="Fish-egg lectin"
FT                   /id="PRO_0000221478"
FT   REPEAT          1..34
FT                   /note="1"
FT   REPEAT          35..68
FT                   /note="2"
FT   REPEAT          69..106
FT                   /note="3"
FT   REPEAT          107..156
FT                   /note="4"
FT   REPEAT          157..199
FT                   /note="5"
FT   REGION          1..199
FT                   /note="5 X approximate tandem repeats"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12956625"
FT   DISULFID        3..234
FT                   /evidence="ECO:0000269|PubMed:12956625"
FT   DISULFID        100..153
FT                   /evidence="ECO:0000269|PubMed:12956625"
FT   DISULFID        128..133
FT                   /evidence="ECO:0000269|PubMed:12956625"
FT   DISULFID        208..226
FT                   /evidence="ECO:0000269|PubMed:12956625"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          11..16
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          19..23
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          28..33
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          36..43
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          45..50
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          62..67
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          70..77
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          79..82
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          89..92
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          98..101
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   HELIX           103..106
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          117..121
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          124..128
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          133..136
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          141..145
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   TURN            153..156
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          160..165
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          167..171
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          177..180
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          186..191
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          194..196
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          200..205
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          208..210
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          212..218
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          221..226
FT                   /evidence="ECO:0007829|PDB:4RUQ"
FT   STRAND          231..235
FT                   /evidence="ECO:0007829|PDB:4RUQ"
SQ   SEQUENCE   238 AA;  25478 MW;  B4E10F1E02A9CA93 CRC64;
     LDCTVIDGNL KQIDAGSGSV VGVNNLNETF VLIDNVFTKI SGSLKHFSVG PAGQLGVNTA
     NNIFKYQSGG FVQLAGLLKQ VDAGGDQIIA GVNMYDDIYC LNMDANNKWP SSNTPWVQIN
     GKLKYYSCGP YSCWGVNSND QIFIMKDVSS NVCSGSGSFI NIPGLLSMIE VATDGSVFGV
     NSQGNLYQRT GVTRSKPDGT DWISMVACPN GHKHVSFDLG VLWLVCVDGS IRKCILTD