Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P32196 (PG3_PIG)

Last modified June 16, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Protegrin-3
      Short name=PG-3
Gene names
Name: NPG3
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Hide | Top

Protein attributes

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

Hide | Top

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.

Hide | Top

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionAntibiotic
Antimicrobial
   PTMAmidation
Disulfide bond
Pyrrolidone carboxylic acid
   Technical term3D-structure
Direct protein sequencing
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...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Amino acid modifications

Modified residue301Pyrrolidone carboxylic acid By similarity
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

1 ............. 149
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P32196-1 [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

Hide | Top

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: 8013647] [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: 7628604] [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: 8335113] [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: 12377122] [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: 14604526] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 30-130, DISULFIDE BONDS.

Hide | Top

Cross-references

Sequence databases

X83267 mRNA. Translation: CAA58240.1.
X84095 Genomic DNA. Translation: CAA58891.1.
PIRA53895. S66285.
RefSeqNP_001116622.1.
UniGeneSsc.70542

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1KWIX-ray2.19A30-130[»]
1LXEX-ray2.50A30-130[»]
1PFPX-ray2.30A30-130[»]
ModBaseSearch...

Genome annotation databases

GeneID100144484.
KEGGssc:100144484.

Phylogenomic databases

HOVERGENP32196.

Family and domain databases

InterProIPR001894. Cathelicidin.
IPR018216. Cathelicidin_CS.
[Graphical view]
PANTHERPTHR10206. Cathelicidin. 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...

Hide | Top

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: June 16, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents