LEC3_CROVR
ID LEC3_CROVR Reviewed; 224 AA.
AC P86626;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 3.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Mannose-specific lectin 3;
DE Contains:
DE RecName: Full=Mannose-specific lectin 3 chain 1;
DE Contains:
DE RecName: Full=Mannose-specific lectin 3 chain 2;
OS Crocus vernus (Dutch crocus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Iridaceae;
OC Crocoideae; Croceae; Crocus.
OX NCBI_TaxID=87752;
RN [1] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), AND DISULFIDE BONDS.
RC TISSUE=Corm;
RA Akrem A., Meyer A., Perbandt M., Voelter W., Buck F., Betzel C.;
RL Submitted (MAY-2010) to UniProtKB.
CC -!- FUNCTION: Mannose-specific lectin. Has weak agglutinating activity
CC towards trypsin-treated erythrocytes from rabbit but not from human (By
CC similarity). {ECO:0000250|UniProtKB:Q9FVA1}.
CC -!- SUBUNIT: Heterotetramer of 2 domain 1 and 2 domain 2 chains arranged as
CC a dimer of domain 1/domain 2 heterodimers. {ECO:0000250}.
CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is:
CC 5.18, its MW is: 48 kDa.
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DR PDB; 3MEZ; X-ray; 1.94 A; A/C=1-110, B/D=112-223.
DR PDBsum; 3MEZ; -.
DR AlphaFoldDB; P86626; -.
DR SMR; P86626; -.
DR UniLectin; P86626; -.
DR EvolutionaryTrace; P86626; -.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR Gene3D; 2.90.10.10; -; 2.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR SMART; SM00108; B_lectin; 2.
DR SUPFAM; SSF51110; SSF51110; 2.
DR PROSITE; PS50927; BULB_LECTIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Hemagglutinin; Lectin; Mannose-binding;
KW Repeat.
FT CHAIN 1..111
FT /note="Mannose-specific lectin 3 chain 1"
FT /id="PRO_0000395438"
FT CHAIN 112..224
FT /note="Mannose-specific lectin 3 chain 2"
FT /id="PRO_0000395439"
FT DOMAIN 2..111
FT /note="Bulb-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038,
FT ECO:0000305"
FT DOMAIN 117..222
FT /note="Bulb-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DISULFID 30..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038,
FT ECO:0000269|Ref.1"
FT DISULFID 145..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038,
FT ECO:0000269|Ref.1"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:3MEZ"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:3MEZ"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:3MEZ"
SQ SEQUENCE 224 AA; 24454 MW; 94C963051247B7C6 CRC64;
DNNVLLTGDV IHTDNQLSYE SAAFVMQGDC NLVLYNEAGG FQSNTHGRGV DCTLRLNNRG
QLEIHSANSN TPVWVYPRSV NTVRGNYAAT LGPDQHVTIY GPAIWSTPAA ANIPRVRNVL
FSSQVMYDNA QLATRDYSLV MRDDCNLVLT KGSKTNIVWE SGTSGRGQHC FMRLGHSGEL
DITDDRLNTV FVSNTVGQEG DYVLILQING QAVVYGPAVW STAA