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P11006

- MAGA_XENLA

UniProt

P11006 - MAGA_XENLA

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Protein

Magainins

Gene

magainins

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Biological processi

  1. defense response to bacterium Source: UniProtKB-KW
  2. defense response to fungus Source: UniProtKB-KW
  3. hemolysis in other organism Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Amphibian defense peptide, Antibiotic, Antimicrobial, Fungicide

Keywords - Biological processi

Cytolysis, Hemolysis

Protein family/group databases

TCDBi1.C.16.1.1. the magainin (magainin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Magainins
Cleaved into the following 5 chains:
Alternative name(s):
Magainin I
Alternative name(s):
Magainin II
Gene namesi
Name:magainins
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6252596. magainins.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Propeptidei19 – 268PRO_0000010677
Peptidei27 – 326Small acidic peptide 1PRO_0000010678
Propeptidei33 – 364PRO_0000010679
Peptidei37 – 5923Magainin-1PRO_0000010680Add
BLAST
Propeptidei62 – 7211PRO_0000010681Add
BLAST
Peptidei73 – 786Small acidic peptide 2PRO_0000010682
Propeptidei79 – 824PRO_0000010683
Peptidei83 – 10523Magainin-2PRO_0000010684Add
BLAST
Propeptidei108 – 11811PRO_0000010685Add
BLAST
Peptidei119 – 1246Small acidic peptide 2PRO_0000010686
Propeptidei125 – 1284PRO_0000010687
Peptidei129 – 15123Magainin-2PRO_0000010688Add
BLAST
Propeptidei154 – 16411PRO_0000010689Add
BLAST
Peptidei165 – 1706Small acidic peptide 2PRO_0000010690
Propeptidei171 – 1744PRO_0000010691
Peptidei175 – 19723Magainin-2PRO_0000010692Add
BLAST
Propeptidei200 – 21011PRO_0000010693Add
BLAST
Peptidei211 – 2166Small acidic peptide 3PRO_0000010694
Propeptidei217 – 2204PRO_0000010695
Peptidei221 – 24323Magainin-2PRO_0000010696Add
BLAST
Propeptidei246 – 25611PRO_0000010697Add
BLAST
Peptidei257 – 2626Small acidic peptide 2PRO_0000010698
Propeptidei263 – 2664PRO_0000010699
Peptidei267 – 28923Magainin-2PRO_0000010700Add
BLAST
Propeptidei292 – 30312PRO_0000010701Add
BLAST

Keywords - PTMi

Cleavage on pair of basic residues

Expressioni

Tissue specificityi

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.

Structurei

Secondary structure

1
303
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi268 – 28619Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D9JNMR-A267-278[»]
1D9LNMR-A270-278[»]
1D9MNMR-A270-278[»]
1D9ONMR-A267-278[»]
1D9PNMR-A267-278[»]
1DUMNMR-A/B267-289[»]
1F0DNMR-A267-278[»]
1F0ENMR-A269-278[»]
1F0FNMR-A270-278[»]
1F0GNMR-A267-278[»]
1F0HNMR-A267-278[»]
2LSANMR-A267-289[»]
2MAGNMR-A267-289[»]
4MGPX-ray1.75A267-289[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11006.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11006-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFKGLFICSL IAVICANALP QPEASADEDM DEREVRGIGK FLHSAGKFGK
60 70 80 90 100
AFVGEIMKSK RDAEAVGPEA FADEDLDERE VRGIGKFLHS AKKFGKAFVG
110 120 130 140 150
EIMNSKRDAE AVGPEAFADE DLDEREVRGI GKFLHSAKKF GKAFVGEIMN
160 170 180 190 200
SKRDAEAVGP EAFADEDLDE REVRGIGKFL HSAKKFGKAF VGEIMNSKRD
210 220 230 240 250
AEAVGPEAFA DEDFDEREVR GIGKFLHSAK KFGKAFVGEI MNSKRDAEAV
260 270 280 290 300
GPEAFADEDL DEREVRGIGK FLHSAKKFGK AFVGEIMNSK RDAEAVDDRR

WVE
Length:303
Mass (Da):33,380
Last modified:July 1, 1989 - v1
Checksum:iE369B0DBB033EA80
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741E → Q AA sequence (PubMed:3299384)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03193 mRNA. Translation: AAA49930.1.
PIRiA28620.
RefSeqiNP_001081306.1. NM_001087837.1.
UniGeneiXl.843.

Genome annotation databases

GeneIDi397766.
KEGGixla:397766.

Cross-referencesi

Web resourcesi

Protein Spotlight

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03193 mRNA. Translation: AAA49930.1 .
PIRi A28620.
RefSeqi NP_001081306.1. NM_001087837.1.
UniGenei Xl.843.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D9J NMR - A 267-278 [» ]
1D9L NMR - A 270-278 [» ]
1D9M NMR - A 270-278 [» ]
1D9O NMR - A 267-278 [» ]
1D9P NMR - A 267-278 [» ]
1DUM NMR - A/B 267-289 [» ]
1F0D NMR - A 267-278 [» ]
1F0E NMR - A 269-278 [» ]
1F0F NMR - A 270-278 [» ]
1F0G NMR - A 267-278 [» ]
1F0H NMR - A 267-278 [» ]
2LSA NMR - A 267-289 [» ]
2MAG NMR - A 267-289 [» ]
4MGP X-ray 1.75 A 267-289 [» ]
ModBasei Search...
MobiDBi Search...

Protein family/group databases

TCDBi 1.C.16.1.1. the magainin (magainin) family.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 397766.
KEGGi xla:397766.

Organism-specific databases

Xenbasei XB-GENE-6252596. magainins.

Miscellaneous databases

EvolutionaryTracei P11006.

Family and domain databases

ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiMAGA_XENLA
AccessioniPrimary (citable) accession number: P11006
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 26, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3