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Protein

Crambin

Gene

THI2

Organism
Crambe hispanica subsp. abyssinica (Abyssinian kale) (Crambe abyssinica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

The function of this hydrophobic plant seed protein is not known.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Plant defense

Names & Taxonomyi

Protein namesi
Recommended name:
Crambin
Gene namesi
Name:THI2
OrganismiCrambe hispanica subsp. abyssinica (Abyssinian kale) (Crambe abyssinica)
Taxonomic identifieri3721 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeCrambe

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4646CrambinPRO_0000221479Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi3 ↔ 401 Publication
Disulfide bondi4 ↔ 321 Publication
Disulfide bondi16 ↔ 261 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
46
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi7 – 1711Combined sources
Turni18 – 225Combined sources
Helixi26 – 305Combined sources
Beta strandi36 – 383Combined sources
Helixi42 – 443Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AB1X-ray0.89A1-46[»]
1CBNX-ray0.83A1-46[»]
1CCMNMR-A1-46[»]
1CCNNMR-A1-46[»]
1CNRX-ray1.05A1-46[»]
1CRNX-ray1.50A1-46[»]
1CXRNMR-A1-46[»]
1EJGX-ray0.54A1-46[»]
1JXTX-ray0.89A1-46[»]
1JXUX-ray0.99A1-46[»]
1JXWX-ray0.89A1-46[»]
1JXXX-ray0.89A1-46[»]
1JXYX-ray0.89A1-46[»]
1YV8NMR-A1-46[»]
1YVANMR-A1-46[»]
2EYANMR-A1-46[»]
2EYBNMR-A1-46[»]
2EYCNMR-A1-46[»]
2EYDNMR-A1-46[»]
2FD7X-ray1.75A1-46[»]
2FD9X-ray1.60A1-46[»]
3NIRX-ray0.48A1-46[»]
3U7TX-ray0.85A1-46[»]
3UE7X-ray1.08B1-46[»]
4FC1neutron diffraction1.10A1-46[»]
ProteinModelPortaliP01542.
SMRiP01542. Positions 1-46.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01542.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.30.1350.10. 1 hit.
InterProiIPR001010. Thionin.
[Graphical view]
PfamiPF00321. Thionin. 1 hit.
[Graphical view]
PRINTSiPR00287. THIONIN.
SUPFAMiSSF57429. SSF57429. 1 hit.
PROSITEiPS00271. THIONIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P01542-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
TTCCPSIVAR SNFNVCRLPG TPEALCATYT GCIIIPGATC PGDYAN
Length:46
Mass (Da):4,736
Last modified:May 30, 2000 - v2
Checksum:i919E68AF159EF722
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221P → S in isoform SI.
Natural varianti25 – 251L → I in isoform SI.

Sequence databases

PIRiA01805. KECX.

Cross-referencesi

Sequence databases

PIRiA01805. KECX.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AB1X-ray0.89A1-46[»]
1CBNX-ray0.83A1-46[»]
1CCMNMR-A1-46[»]
1CCNNMR-A1-46[»]
1CNRX-ray1.05A1-46[»]
1CRNX-ray1.50A1-46[»]
1CXRNMR-A1-46[»]
1EJGX-ray0.54A1-46[»]
1JXTX-ray0.89A1-46[»]
1JXUX-ray0.99A1-46[»]
1JXWX-ray0.89A1-46[»]
1JXXX-ray0.89A1-46[»]
1JXYX-ray0.89A1-46[»]
1YV8NMR-A1-46[»]
1YVANMR-A1-46[»]
2EYANMR-A1-46[»]
2EYBNMR-A1-46[»]
2EYCNMR-A1-46[»]
2EYDNMR-A1-46[»]
2FD7X-ray1.75A1-46[»]
2FD9X-ray1.60A1-46[»]
3NIRX-ray0.48A1-46[»]
3U7TX-ray0.85A1-46[»]
3UE7X-ray1.08B1-46[»]
4FC1neutron diffraction1.10A1-46[»]
ProteinModelPortaliP01542.
SMRiP01542. Positions 1-46.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP01542.

Family and domain databases

Gene3Di3.30.1350.10. 1 hit.
InterProiIPR001010. Thionin.
[Graphical view]
PfamiPF00321. Thionin. 1 hit.
[Graphical view]
PRINTSiPR00287. THIONIN.
SUPFAMiSSF57429. SSF57429. 1 hit.
PROSITEiPS00271. THIONIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Primary structure of the hydrophobic plant protein crambin."
    Teeter M.M., Mazer J.A., L'Italien J.J.
    Biochemistry 20:5437-5443(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur."
    Hendrickson W.A., Teeter M.M.
    Nature 290:107-113(1981)
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), DISULFIDE BONDS.
  3. "Correlated disorder of the pure Pro22/Leu25 form of crambin at 150 K refined to 1.05-A resolution."
    Yamano A., Teeter M.M.
    J. Biol. Chem. 269:13956-13965(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
  4. "Crystal structure of Ser-22/Ile-25 form crambin confirms solvent, side chain substate correlations."
    Yamano A., Heo N.-H., Teeter M.M.
    J. Biol. Chem. 272:9597-9600(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (0.89 ANGSTROMS).
  5. "Secondary structure and hydrogen bonding of crambin in solution. A two-dimensional NMR study."
    Lamerichs R.M.J.N., Berliner L.J., Boelens R., de Marco A., Llinas M., Kaptein R.
    Eur. J. Biochem. 171:307-312(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiCRAM_CRAAB
AccessioniPrimary (citable) accession number: P01542
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 30, 2000
Last modified: January 7, 2015
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Two isoforms exists, a major form PL (shown here) and a minor form SI.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.