CRAM_CRAAB
ID CRAM_CRAAB Reviewed; 46 AA.
AC P01542;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Crambin;
GN Name=THI2;
OS Crambe hispanica subsp. abyssinica (Abyssinian kale) (Crambe abyssinica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Crambe.
OX NCBI_TaxID=3721;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=6895315; DOI=10.1021/bi00522a013;
RA Teeter M.M., Mazer J.A., L'Italien J.J.;
RT "Primary structure of the hydrophobic plant protein crambin.";
RL Biochemistry 20:5437-5443(1981).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), AND DISULFIDE BONDS.
RA Hendrickson W.A., Teeter M.M.;
RT "Structure of the hydrophobic protein crambin determined directly from the
RT anomalous scattering of sulphur.";
RL Nature 290:107-113(1981).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
RX PubMed=8188676; DOI=10.1016/s0021-9258(17)36741-8;
RA Yamano A., Teeter M.M.;
RT "Correlated disorder of the pure Pro22/Leu25 form of crambin at 150 K
RT refined to 1.05-A resolution.";
RL J. Biol. Chem. 269:13956-13965(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (0.89 ANGSTROMS).
RX PubMed=9092482; DOI=10.1074/jbc.272.15.9597;
RA Yamano A., Heo N.-H., Teeter M.M.;
RT "Crystal structure of Ser-22/Ile-25 form crambin confirms solvent, side
RT chain substate correlations.";
RL J. Biol. Chem. 272:9597-9600(1997).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=3338468; DOI=10.1111/j.1432-1033.1988.tb13791.x;
RA Lamerichs R.M.J.N., Berliner L.J., Boelens R., de Marco A., Llinas M.,
RA Kaptein R.;
RT "Secondary structure and hydrogen bonding of crambin in solution. A two-
RT dimensional NMR study.";
RL Eur. J. Biochem. 171:307-312(1988).
CC -!- FUNCTION: The function of this hydrophobic plant seed protein is not
CC known.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MISCELLANEOUS: Two isoforms exists, a major form PL (shown here) and a
CC minor form SI.
CC -!- SIMILARITY: Belongs to the plant thionin (TC 1.C.44) family.
CC {ECO:0000305}.
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DR PIR; A01805; KECX.
DR PDB; 1AB1; X-ray; 0.89 A; A=1-46.
DR PDB; 1CBN; X-ray; 0.83 A; A=1-46.
DR PDB; 1CCM; NMR; -; A=1-46.
DR PDB; 1CCN; NMR; -; A=1-46.
DR PDB; 1CNR; X-ray; 1.05 A; A=1-46.
DR PDB; 1CRN; X-ray; 1.50 A; A=1-46.
DR PDB; 1CXR; NMR; -; A=1-46.
DR PDB; 1EJG; X-ray; 0.54 A; A=1-46.
DR PDB; 1JXT; X-ray; 0.89 A; A=1-46.
DR PDB; 1JXU; X-ray; 0.99 A; A=1-46.
DR PDB; 1JXW; X-ray; 0.89 A; A=1-46.
DR PDB; 1JXX; X-ray; 0.89 A; A=1-46.
DR PDB; 1JXY; X-ray; 0.89 A; A=1-46.
DR PDB; 1YV8; NMR; -; A=1-46.
DR PDB; 1YVA; NMR; -; A=1-46.
DR PDB; 2EYA; NMR; -; A=1-46.
DR PDB; 2EYB; NMR; -; A=1-46.
DR PDB; 2EYC; NMR; -; A=1-46.
DR PDB; 2EYD; NMR; -; A=1-46.
DR PDB; 2FD7; X-ray; 1.75 A; A=1-46.
DR PDB; 2FD9; X-ray; 1.60 A; A=1-46.
DR PDB; 3NIR; X-ray; 0.48 A; A=1-46.
DR PDB; 3U7T; X-ray; 0.85 A; A=1-46.
DR PDB; 3UE7; X-ray; 1.08 A; B=1-46.
DR PDB; 4FC1; Neutron; 1.10 A; A=1-46.
DR PDBsum; 1AB1; -.
DR PDBsum; 1CBN; -.
DR PDBsum; 1CCM; -.
DR PDBsum; 1CCN; -.
DR PDBsum; 1CNR; -.
DR PDBsum; 1CRN; -.
DR PDBsum; 1CXR; -.
DR PDBsum; 1EJG; -.
DR PDBsum; 1JXT; -.
DR PDBsum; 1JXU; -.
DR PDBsum; 1JXW; -.
DR PDBsum; 1JXX; -.
DR PDBsum; 1JXY; -.
DR PDBsum; 1YV8; -.
DR PDBsum; 1YVA; -.
DR PDBsum; 2EYA; -.
DR PDBsum; 2EYB; -.
DR PDBsum; 2EYC; -.
DR PDBsum; 2EYD; -.
DR PDBsum; 2FD7; -.
DR PDBsum; 2FD9; -.
DR PDBsum; 3NIR; -.
DR PDBsum; 3U7T; -.
DR PDBsum; 3UE7; -.
DR PDBsum; 4FC1; -.
DR AlphaFoldDB; P01542; -.
DR BMRB; P01542; -.
DR SMR; P01542; -.
DR EvolutionaryTrace; P01542; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1350.10; -; 1.
DR InterPro; IPR001010; Thionin.
DR InterPro; IPR036391; Thionin-like_sf.
DR Pfam; PF00321; Thionin; 1.
DR PRINTS; PR00287; THIONIN.
DR SUPFAM; SSF57429; SSF57429; 1.
DR PROSITE; PS00271; THIONIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Plant defense;
KW Secreted.
FT CHAIN 1..46
FT /note="Crambin"
FT /id="PRO_0000221479"
FT DISULFID 3..40
FT /evidence="ECO:0000269|Ref.2"
FT DISULFID 4..32
FT /evidence="ECO:0000269|Ref.2"
FT DISULFID 16..26
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 22
FT /note="P -> S (in isoform SI)"
FT VARIANT 25
FT /note="L -> I (in isoform SI)"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1AB1"
FT HELIX 7..17
FT /evidence="ECO:0007829|PDB:1AB1"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:1AB1"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:1AB1"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1AB1"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1CNR"
SQ SEQUENCE 46 AA; 4736 MW; 919E68AF159EF722 CRC64;
TTCCPSIVAR SNFNVCRLPG TPEALCATYT GCIIIPGATC PGDYAN
