LEC_PARPC
ID LEC_PARPC Reviewed; 447 AA.
AC P83304;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Mannose/glucose-specific lectin;
DE Flags: Fragment;
OS Parkia platycephala.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Caesalpinioideae; mimosoid clade;
OC Mimoseae; Parkia.
OX NCBI_TaxID=185447 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, SUBUNIT, MASS SPECTROMETRY, AND VARIANTS VAL-70; ARG-227
RP AND ASN-296.
RC TISSUE=Seed;
RX PubMed=11502201; DOI=10.1046/j.1432-1327.2001.02368.x;
RA Mann K., Farias C.M.S.A., Del Sol F.G., Santos C.F., Grangeiro T.B.,
RA Nagano C.S., Cavada B.S., Calvete J.J.;
RT "The amino-acid sequence of the glucose/mannose-specific lectin isolated
RT from Parkia platycephala seeds reveals three tandemly arranged jacalin-
RT related domains.";
RL Eur. J. Biochem. 268:4414-4422(2001).
RN [2] {ECO:0000305}
RP FUNCTION.
RA Ramos M.V., Cavada B.S., Bomfim L.R., Debray H., Mazard A.-M.,
RA Calvete J.J., Grangeiro T.B., Rouge P.;
RT "Interaction of the seed lectin from Parkia platycephala (Mimosoideae) with
RT carbohydrates and complex glycans.";
RL Protein Pept. Lett. 6:215-222(1999).
CC -!- FUNCTION: Mannose/glucose specific lectin. Shows agglutinating activity
CC against rabbit erythrocytes. {ECO:0000269|Ref.2}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11502201}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MASS SPECTROMETRY: Mass=47946; Mass_error=6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11502201};
CC -!- MASS SPECTROMETRY: Mass=47951; Mass_error=9; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11502201};
CC -!- MISCELLANEOUS: PubMed:11502201 authors report the absence of the
CC blocked N-terminal residue, together with 3 to 5 amino acids from the
CC N-terminal part of the protein.
CC -!- SIMILARITY: Belongs to the jacalin lectin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01088, ECO:0000305}.
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DR PDB; 1ZGR; X-ray; 2.50 A; A/B=1-447.
DR PDB; 1ZGS; X-ray; 2.50 A; A/B=1-447.
DR PDBsum; 1ZGR; -.
DR PDBsum; 1ZGS; -.
DR AlphaFoldDB; P83304; -.
DR SMR; P83304; -.
DR UniLectin; P83304; -.
DR EvolutionaryTrace; P83304; -.
DR GO; GO:0005536; F:glucose binding; IDA:UniProtKB.
DR GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:UniProtKB.
DR CDD; cd09612; Jacalin; 3.
DR Gene3D; 2.100.10.30; -; 3.
DR InterPro; IPR001229; Jacalin-like_lectin_dom.
DR InterPro; IPR033734; Jacalin-like_lectin_dom_plant.
DR InterPro; IPR036404; Jacalin-like_lectin_dom_sf.
DR Pfam; PF01419; Jacalin; 3.
DR SMART; SM00915; Jacalin; 3.
DR SUPFAM; SSF51101; SSF51101; 3.
DR PROSITE; PS51752; JACALIN_LECTIN; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lectin; Mannose-binding; Repeat.
FT CHAIN <1..447
FT /note="Mannose/glucose-specific lectin"
FT /id="PRO_0000072804"
FT REPEAT 1..149
FT /note="1"
FT /evidence="ECO:0000269|PubMed:11502201"
FT DOMAIN 5..148
FT /note="Jacalin-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT REPEAT 150..295
FT /note="2"
FT /evidence="ECO:0000269|PubMed:11502201"
FT DOMAIN 153..294
FT /note="Jacalin-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT REPEAT 296..447
FT /note="3"
FT /evidence="ECO:0000269|PubMed:11502201"
FT DOMAIN 300..443
FT /note="Jacalin-type lectin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT REGION 1..447
FT /note="3 X approximate tandem repeats"
FT VARIANT 70
FT /note="I -> V"
FT /evidence="ECO:0000269|PubMed:11502201"
FT VARIANT 227
FT /note="K -> R"
FT /evidence="ECO:0000269|PubMed:11502201"
FT VARIANT 296
FT /note="D -> N"
FT /evidence="ECO:0000269|PubMed:11502201"
FT NON_TER 1
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 27..45
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1ZGR"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 79..89
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 92..104
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 123..148
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 176..194
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:1ZGR"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 226..236
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 239..251
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 269..294
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 311..317
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 322..340
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:1ZGR"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 372..400
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:1ZGR"
FT STRAND 418..443
FT /evidence="ECO:0007829|PDB:1ZGR"
SQ SEQUENCE 447 AA; 47521 MW; 8F14ED460874BBB2 CRC64;
SLKGMISVGP WGGSGGNYWS FKANHAITEI VIHVKDNIKS ISFKDASGDI SGTFGGKDPR
ENEKGDEKKI KIHWPTEYLK SISGSYGDYN GVLVIRSLSF ITNLTTYGPF GSTSGGESFS
IPIADSVVVG FHGRAGYYLD ALGIFVQPVP HGTISFGPWG GPAGDDAFNF KVGSWIKDII
IYADAAINSI AFKDANGHCY GKFGGQDPND IGVEKKVEID GNLEHLKSIS GTYGNYKGFE
VVTSLSFITN VTKHGPFGIA SGTSFSIPIE GSLVTGFHGK SGYYLDSIGI YVKPRDVEGS
ISIGPWGGSG GDPWSYTANE GINQIIIYAG SNIKSVAFKD TSGLDSATFG GVNPKDTGEK
NTVSINWPSE YLTSISGTYG QYKFKDVFTT ITSLSFTTNL ATYGPFGKAS ATSFSIPIHN
NMVVGFHGRA GDYLDAIGIF VKPDTAV
