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P11006 (MAGA_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Magainins

Cleaved into the following 5 chains:

  1. Small acidic peptide 1
  2. Small acidic peptide 2
  3. Small acidic peptide 3
  4. Magainin-1
    Alternative name(s):
    Magainin I
  5. Magainin-2
    Alternative name(s):
    Magainin II
Gene names
Name:magainins
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Antimicrobial peptides that inhibit the growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa. Magainins are membrane lytic agents.

Subcellular location

Secreted.

Tissue specificity

Synthesized in the stomach and stored in a novel granular multinucleated cell in the gastric mucosa. It is stored as active, processed peptides in large granules within the granular gland secretions of the skin.

Sequence similarities

Belongs to the gastrin/cholecystokinin family. Magainin subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 268
PRO_0000010677
Peptide27 – 326Small acidic peptide 1
PRO_0000010678
Propeptide33 – 364
PRO_0000010679
Peptide37 – 5923Magainin-1
PRO_0000010680
Propeptide62 – 7211
PRO_0000010681
Peptide73 – 786Small acidic peptide 2
PRO_0000010682
Propeptide79 – 824
PRO_0000010683
Peptide83 – 10523Magainin-2
PRO_0000010684
Propeptide108 – 11811
PRO_0000010685
Peptide119 – 1246Small acidic peptide 2
PRO_0000010686
Propeptide125 – 1284
PRO_0000010687
Peptide129 – 15123Magainin-2
PRO_0000010688
Propeptide154 – 16411
PRO_0000010689
Peptide165 – 1706Small acidic peptide 2
PRO_0000010690
Propeptide171 – 1744
PRO_0000010691
Peptide175 – 19723Magainin-2
PRO_0000010692
Propeptide200 – 21011
PRO_0000010693
Peptide211 – 2166Small acidic peptide 3
PRO_0000010694
Propeptide217 – 2204
PRO_0000010695
Peptide221 – 24323Magainin-2
PRO_0000010696
Propeptide246 – 25611
PRO_0000010697
Peptide257 – 2626Small acidic peptide 2
PRO_0000010698
Propeptide263 – 2664
PRO_0000010699
Peptide267 – 28923Magainin-2
PRO_0000010700
Propeptide292 – 30312
PRO_0000010701

Experimental info

Sequence conflict741E → Q AA sequence Ref.2

Secondary structure

1 .......... 303
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11006 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: E369B0DBB033EA80

FASTA30333,380
        10         20         30         40         50         60 
MFKGLFICSL IAVICANALP QPEASADEDM DEREVRGIGK FLHSAGKFGK AFVGEIMKSK 

        70         80         90        100        110        120 
RDAEAVGPEA FADEDLDERE VRGIGKFLHS AKKFGKAFVG EIMNSKRDAE AVGPEAFADE 

       130        140        150        160        170        180 
DLDEREVRGI GKFLHSAKKF GKAFVGEIMN SKRDAEAVGP EAFADEDLDE REVRGIGKFL 

       190        200        210        220        230        240 
HSAKKFGKAF VGEIMNSKRD AEAVGPEAFA DEDFDEREVR GIGKFLHSAK KFGKAFVGEI 

       250        260        270        280        290        300 
MNSKRDAEAV GPEAFADEDL DEREVRGIGK FLHSAKKFGK AFVGEIMNSK RDAEAVDDRR 


WVE

« Hide

References

[1]"The cDNA sequence coding for prepro-PGS (prepro-magainins) and aspects of the processing of this prepro-polypeptide."
Terry A.S., Poulter L., Williams D.H., Nutkins J.C., Giovannini M.G., Moore C.H., Gibson B.W.
J. Biol. Chem. 263:5745-5751(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor."
Zasloff M.
Proc. Natl. Acad. Sci. U.S.A. 84:5449-5453(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-158 AND 297-303, PARTIAL PROTEIN SEQUENCE.
Tissue: Skin and Skin secretion.
[3]"Antimicrobial peptides in the stomach of Xenopus laevis."
Moore K.S., Bevins C.L., Brasseur M.M., Tomassini N., Turner K., Eck H., Zasloff M.
J. Biol. Chem. 266:19851-19857(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE (MAGAININ-1 AND MAGAININ-2).
Tissue: Stomach.
[4]"Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy."
Bechinger B., Zasloff M., Opella S.J.
Protein Sci. 2:2077-2084(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF MAGAININ-2.
+Additional computationally mapped references.

Web resources

Protein Spotlight

When a frog swallows a fly - Issue 7 of February 2001

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J03193 mRNA. Translation: AAA49930.1.
PIRA28620.
RefSeqNP_001081306.1. NM_001087837.1.
UniGeneXl.843.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D9JNMR-A129-140[»]
1D9LNMR-A224-232[»]
1D9MNMR-A224-232[»]
1D9ONMR-A129-140[»]
1D9PNMR-A129-140[»]
1DUMNMR-A/B129-151[»]
1F0DNMR-A83-94[»]
1F0ENMR-A86-94[»]
1F0FNMR-A86-94[»]
1F0GNMR-A83-94[»]
1F0HNMR-A83-94[»]
2MAGNMR-A267-289[»]
ModBaseSearch...

Protein family/group databases

TCDB1.C.16.1.1. magainin family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397766.
KEGGxla:397766.

Organism-specific databases

XenbaseXB-GENE-6252596. magainins.

Family and domain databases

ProtoNetSearch...

Other

EvolutionaryTraceP11006.

Entry information

Entry nameMAGA_XENLA
AccessionPrimary (citable) accession number: P11006
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 3, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents