ID   LECC_POLMI              Reviewed;         125 AA.
AC   P16108;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Lectin;
OS   Polyandrocarpa misakiensis (Tunicate).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC   Styelidae; Polyandrocarpa.
OX   NCBI_TaxID=7723;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2295629; DOI=10.1016/s0021-9258(19)40009-4;
RA   Suzuki T., Takagi T., Furukohri T., Kawamura K., Nakauchi M.;
RT   "A calcium-dependent galactose-binding lectin from the tunicate
RT   Polyandrocarpa misakiensis. Isolation, characterization, and amino acid
RT   sequence.";
RL   J. Biol. Chem. 265:1274-1281(1990).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=10398588; DOI=10.1006/jmbi.1999.2910;
RA   Poget S.F., Legge G.B., Proctor M.R., Butler P.J., Bycroft M.,
RA   Williams R.L.;
RT   "The structure of a tunicate C-type lectin from Polyandrocarpa misakiensis
RT   complexed with D-galactose.";
RL   J. Mol. Biol. 290:867-879(1999).
CC   -!- FUNCTION: Role in the defense system of the organism against
CC       microorganisms. This calcium-binding lectin binds galactose.
CC   -!- SUBUNIT: Homodimer.
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DR   PIR; A35003; A35003.
DR   PDB; 1BYF; X-ray; 2.00 A; A/B=1-125.
DR   PDB; 1TLG; X-ray; 2.20 A; A/B=1-125.
DR   PDBsum; 1BYF; -.
DR   PDBsum; 1TLG; -.
DR   AlphaFoldDB; P16108; -.
DR   SMR; P16108; -.
DR   UniLectin; P16108; -.
DR   EvolutionaryTrace; P16108; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   CDD; cd03601; CLECT_TC14_like; 1.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR034008; TC14-like_CTLD.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Direct protein sequencing; Disulfide bond; Lectin.
FT   CHAIN           1..125
FT                   /note="Lectin"
FT                   /id="PRO_0000046646"
FT   DOMAIN          1..120
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        21..119
FT   DISULFID        96..111
FT   STRAND          3..12
FT                   /evidence="ECO:0007829|PDB:1BYF"
FT   HELIX           14..22
FT                   /evidence="ECO:0007829|PDB:1BYF"
FT   TURN            23..25
FT                   /evidence="ECO:0007829|PDB:1BYF"
FT   STRAND          27..29
FT                   /evidence="ECO:0007829|PDB:1BYF"
FT   HELIX           31..34
FT                   /evidence="ECO:0007829|PDB:1BYF"
FT   HELIX           36..49
FT                   /evidence="ECO:0007829|PDB:1BYF"
FT   STRAND          53..59
FT                   /evidence="ECO:0007829|PDB:1BYF"
FT   TURN            60..62
FT                   /evidence="ECO:0007829|PDB:1BYF"
FT   STRAND          96..99
FT                   /evidence="ECO:0007829|PDB:1BYF"
FT   TURN            101..103
FT                   /evidence="ECO:0007829|PDB:1BYF"
FT   STRAND          104..109
FT                   /evidence="ECO:0007829|PDB:1BYF"
FT   STRAND          115..122
FT                   /evidence="ECO:0007829|PDB:1BYF"
SQ   SEQUENCE   125 AA;  14034 MW;  5C9B98F6F8B00C4A CRC64;
     MDYEILFSDE TMNYADAGTY CQSRGMALVS SAMRDSTMVK AILAFTEVKG HDYWVGADNL
     QDGAYNFLWN DGVSLPTDSD LWSPNEPSNP QSWQLCVQIW SKYNLLDDVG CGGARRVICE
     KELDD