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P01542

- CRAM_CRAAB

UniProt

P01542 - CRAM_CRAAB

Protein

Crambin

Gene

THI2

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

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

    GO - Biological processi

    1. defense response Source: UniProtKB-KW

    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

    1. extracellular region Source: UniProtKB-SubCell

    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 – 65
    Helixi7 – 1711
    Turni18 – 225
    Helixi26 – 305
    Beta strandi36 – 383
    Helixi42 – 443

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    TTCCPSIVAR SNFNVCRLPG TPEALCATYT GCIIIPGATC PGDYAN       46
    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

    PIRi A01805. KECX.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AB1 X-ray 0.89 A 1-46 [» ]
    1CBN X-ray 0.83 A 1-46 [» ]
    1CCM NMR - A 1-46 [» ]
    1CCN NMR - A 1-46 [» ]
    1CNR X-ray 1.05 A 1-46 [» ]
    1CRN X-ray 1.50 A 1-46 [» ]
    1CXR NMR - A 1-46 [» ]
    1EJG X-ray 0.54 A 1-46 [» ]
    1JXT X-ray 0.89 A 1-46 [» ]
    1JXU X-ray 0.99 A 1-46 [» ]
    1JXW X-ray 0.89 A 1-46 [» ]
    1JXX X-ray 0.89 A 1-46 [» ]
    1JXY X-ray 0.89 A 1-46 [» ]
    1YV8 NMR - A 1-46 [» ]
    1YVA NMR - A 1-46 [» ]
    2EYA NMR - A 1-46 [» ]
    2EYB NMR - A 1-46 [» ]
    2EYC NMR - A 1-46 [» ]
    2EYD NMR - A 1-46 [» ]
    2FD7 X-ray 1.75 A 1-46 [» ]
    2FD9 X-ray 1.60 A 1-46 [» ]
    3NIR X-ray 0.48 A 1-46 [» ]
    3U7T X-ray 0.85 A 1-46 [» ]
    3UE7 X-ray 1.08 B 1-46 [» ]
    4FC1 neutron diffraction 1.10 A 1-46 [» ]
    ProteinModelPortali P01542.
    SMRi P01542. Positions 1-46.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P01542.

    Family and domain databases

    Gene3Di 3.30.1350.10. 1 hit.
    InterProi IPR001010. Thionin.
    [Graphical view ]
    Pfami PF00321. Thionin. 1 hit.
    [Graphical view ]
    PRINTSi PR00287. THIONIN.
    SUPFAMi SSF57429. SSF57429. 1 hit.
    PROSITEi PS00271. THIONIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 91 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