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P32196 (PG3_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified July 24, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protegrin-3

Short name=PG-3
Gene names
Name:NPG3
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length149 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Microbicidal activity. Active against E.coli, Listeria monocytogenes and C.albicans, in vitro.

Subcellular location

Secreted.

Sequence similarities

Belongs to the cathelicidin family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionAntibiotic
Antimicrobial
   PTMAmidation
Disulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Propeptide30 – 130101
PRO_0000004748
Peptide131 – 14818Protegrin-3 Ref.3
PRO_0000004749

Amino acid modifications

Modified residue1481Arginine amide
Disulfide bond85 ↔ 96 Ref.4 Ref.5
Disulfide bond107 ↔ 124 Ref.4 Ref.5
Disulfide bond136 ↔ 145 By similarity
Disulfide bond138 ↔ 143 By similarity

Secondary structure

............. 149
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32196 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 6F4BA98429CD6ED4

FASTA14916,578
        10         20         30         40         50         60 
METQRASLCL GRWSLWLLLL ALVVPSASAQ ALSYREAVLR AVDRLNEQSS EANLYRLLEL 

        70         80         90        100        110        120 
DQPPKADEDP GTPKPVSFTV KETVCPRPTR QPPELCDFKE NGRVKQCVGT VTLDQIKDPL 

       130        140 
DITCNEVQGV RGGGLCYCRR RFCVCVGRG 

« Hide

References

[1]"Identification of a new member of the protegrin family by cDNA cloning."
Zhao C., Liu L., Lehrer R.I.
FEBS Lett. 346:285-288(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Bone marrow.
[2]"The structure of porcine protegrin genes."
Zhao C., Ganz T., Lehrer R.I.
FEBS Lett. 368:197-202(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Red Duroc.
[3]"Protegrins: leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins."
Kokryakov V.N., Harwig S.S.L., Panyutich E.A., Shevchenko A.A., Aleshina G.M., Shamova O.V., Korneva H.A., Lehrer R.I.
FEBS Lett. 327:231-236(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 131-148.
Tissue: Leukocyte.
[4]"Structure of the cathelicidin motif of protegrin-3 precursor: structural insights into the activation mechanism of an antimicrobial protein."
Sanchez J.F., Hoh F., Strub M.-P., Aumelas A., Dumas C.
Structure 10:1363-1370(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 30-130, DISULFIDE BONDS.
[5]"Selenomethionine and selenocysteine double labeling strategy for crystallographic phasing."
Strub M.-P., Hoh F., Sanchez J.F., Strub J.-M., Bock A., Aumelas A., Dumas C.
Structure 11:1359-1367(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 30-130, DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83267 mRNA. Translation: CAA58240.1.
X84095 Genomic DNA. Translation: CAA58891.1.
PIRA53895. S66285.
RefSeqNP_001116622.1. NM_001123150.1.
UniGeneSsc.420.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KWIX-ray2.19A30-130[»]
1LXEX-ray2.50A30-130[»]
1PFPX-ray2.30A30-130[»]
ProteinModelPortalP32196.
SMRP32196. Positions 30-130.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100144484.
KEGGssc:100144484.

Organism-specific databases

CTD100144484.

Phylogenomic databases

HOVERGENHBG006116.

Family and domain databases

InterProIPR001894. Cathelicidin.
IPR018216. Cathelicidin_CS.
[Graphical view]
PANTHERPTHR10206. PTHR10206. 1 hit.
PfamPF00666. Cathelicidins. 1 hit.
[Graphical view]
ProDomPD001838. Cathelicidin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00946. CATHELICIDINS_1. 1 hit.
PS00947. CATHELICIDINS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32196.

Entry information

Entry namePG3_PIG
AccessionPrimary (citable) accession number: P32196
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: July 24, 2013
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references