CANA_CANEN
ID CANA_CANEN Reviewed; 445 AA.
AC P50477;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Canavalin;
DE Flags: Precursor;
OS Canavalia ensiformis (Jack bean) (Dolichos ensiformis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Canavalia.
OX NCBI_TaxID=3823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cotyledon;
RX PubMed=1731967; DOI=10.1007/bf00018469;
RA Ng J.D., Stinchcombe T., Ko T.-P., Alexander E., McPherson A.;
RT "PCR cloning of the full-length cDNA for the seed protein canavalin from
RT the jack bean plant, Canavalis ensiformis.";
RL Plant Mol. Biol. 18:147-149(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cotyledon;
RX PubMed=8310055; DOI=10.1104/pp.101.3.713;
RA Ng J.D., Ko T.-P., McPherson A.;
RT "Cloning, expression, and crystallization of jack bean (Canavalia
RT ensiformis) canavalin.";
RL Plant Physiol. 101:713-728(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=8310056; DOI=10.1104/pp.101.3.729;
RA Ko T.-P., Ng J.D., McPherson A.;
RT "The three-dimensional structure of canavalin from jack bean (Canavalia
RT ensiformis).";
RL Plant Physiol. 101:729-744(1993).
CC -!- FUNCTION: Seed storage protein.
CC -!- SUBUNIT: Homotrimer.
CC -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC {ECO:0000305}.
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DR EMBL; X59467; CAA42075.1; -; mRNA.
DR PIR; JQ2264; JQ2264.
DR PDB; 1CAU; X-ray; 2.30 A; A=44-224, B=241-424.
DR PDB; 1CAV; X-ray; 2.60 A; A=44-224, B=241-424.
DR PDB; 1CAW; X-ray; 2.60 A; A=44-224, B=241-424.
DR PDB; 1CAX; X-ray; 2.60 A; A/C/E=44-224, B/D/F=241-424.
DR PDB; 1DGR; X-ray; 2.60 A; A/B/C=46-223, M/W/Y=331-423, N/V/X=246-324.
DR PDB; 1DGW; X-ray; 1.70 A; A=46-223, X=246-324, Y=331-423.
DR PDB; 2CAU; X-ray; 2.10 A; A=1-445.
DR PDB; 2CAV; X-ray; 2.00 A; A=1-445.
DR PDB; 6V7G; X-ray; 1.40 A; A=1-445.
DR PDB; 6V7J; X-ray; 2.00 A; A/B/C=1-445.
DR PDB; 6V7L; X-ray; 2.80 A; A/B/C=1-445.
DR PDBsum; 1CAU; -.
DR PDBsum; 1CAV; -.
DR PDBsum; 1CAW; -.
DR PDBsum; 1CAX; -.
DR PDBsum; 1DGR; -.
DR PDBsum; 1DGW; -.
DR PDBsum; 2CAU; -.
DR PDBsum; 2CAV; -.
DR PDBsum; 6V7G; -.
DR PDBsum; 6V7J; -.
DR PDBsum; 6V7L; -.
DR AlphaFoldDB; P50477; -.
DR SMR; P50477; -.
DR PRIDE; P50477; -.
DR EvolutionaryTrace; P50477; -.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR GO; GO:0045735; F:nutrient reservoir activity; IDA:CAFA.
DR DisProt; DP00436; -.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF00190; Cupin_1; 2.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; SSF51182; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Seed storage protein; Signal; Storage protein.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..445
FT /note="Canavalin"
FT /id="PRO_0000032174"
FT DOMAIN 49..207
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 249..407
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1CAV"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1CAU"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 95..115
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1DGW"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1CAU"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1CAU"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:6V7G"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:6V7G"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:6V7G"
FT TURN 242..246
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 257..268
FT /evidence="ECO:0007829|PDB:6V7G"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:6V7G"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 281..288
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 292..301
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 303..311
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 313..320
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:1CAV"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:1CAX"
FT STRAND 333..340
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 354..370
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:6V7G"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:6V7G"
FT HELIX 392..398
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:6V7G"
FT HELIX 403..411
FT /evidence="ECO:0007829|PDB:6V7G"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:6V7G"
SQ SEQUENCE 445 AA; 50327 MW; 30383C5F83A1E9B7 CRC64;
MAFSARFPLW LLLGVVLLAS VSASFAHSGH SGGEAEDESE ESRAQNNPYL FRSNKFLTLF
KNQHGSLRLL QRFNEDTEKL ENLRDYRVLE YCSKPNTLLL PHHSDSDLLV LVLEGQAILV
LVNPDGRDTY KLDQGDAIKI QAGTPFYLIN PDNNQNLRIL KFAITFRRPG TVEDFFLSST
KRLPSYLSAF SKNFLEASYD SPYDEIEQTL LQEEQEGVIV KMPKDQIQEI SKHAQSSSRK
TLSSQDKPFN LRSRDPIYSN NYGKLYEITP EKNSQLRDLD ILLNCLQMNE GALFVPHYNS
RATVILVANE GRAEVELVGL EQQQQQGLES MQLRRYAATL SEGDIIVIPS SFPVALKAAS
DLNMVGIGVN AENNERNFLA GHKENVIRQI PRQVSDLTFP GSGEEVEELL ENQKESYFVD
GQPRHIDAGG KARRAHLPNL FRTFY
