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Protein

Antimicrobial protein PN-AMP1

Gene
N/A
Organism
Ipomoea nil (Japanese morning glory) (Pharbitis nil)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Chitin-binding protein with a defensive function against numerous chitin containing fungal pathogens. It is also an inhibitor of Gram-positive bacteria such as B.subtilis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Fungicide

Keywords - Biological processi

Plant defense

Keywords - Ligandi

Chitin-binding

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Antimicrobial protein PN-AMP1
Cleaved into the following chain:
OrganismiIpomoea nil (Japanese morning glory) (Pharbitis nil)
Taxonomic identifieri35883 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesConvolvulaceaeIpomoeeaeIpomoea

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4141Antimicrobial protein PN-AMP1PRO_0000005278Add
BLAST
Chaini1 – 4040Antimicrobial protein PN-AMP2PRO_0000005279Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Pyrrolidone carboxylic acidCurated
Disulfide bondi3 ↔ 18PROSITE-ProRule annotation
Disulfide bondi12 ↔ 24PROSITE-ProRule annotation
Disulfide bondi17 ↔ 31PROSITE-ProRule annotation
Disulfide bondi35 ↔ 39PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 4141Chitin-binding type-1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 chitin-binding type-1 domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.30.60.10. 1 hit.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 1 hit.
[Graphical view]
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMiSSF57016. SSF57016. 1 hit.
PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P81591-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
QQCGRQASGR LCGNRLCCSQ WGYCGSTASY CGAGCQSQCR S
Length:41
Mass (Da):4,326
Last modified:January 1, 1999 - v1
Checksum:i326C9E2DA00724DB
GO

Mass spectrometryi

Molecular mass is 4299.72 Da from positions 1 - 41. Determined by ESI. 1 Publication
Molecular mass is 4213.17 Da from positions 1 - 40. Determined by ESI. 1 Publication

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.30.60.10. 1 hit.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 1 hit.
[Graphical view]
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMiSSF57016. SSF57016. 1 hit.
PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Two hevein homologs isolated from the seed of Pharbitis nil L. exhibit potent antifungal activity."
    Koo J.C., Lee S.Y., Chun H.J., Cheong Y.H., Choi J.S., Kawabata S., Miyagi M., Tsunasawa S., Ha K.S., Bae D.W., Han C.-D., Lee B.L., Cho M.J.
    Biochim. Biophys. Acta 1382:80-90(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, CHARACTERIZATION, MASS SPECTROMETRY.
    Tissue: Seed.

Entry informationi

Entry nameiAMP_IPONI
AccessioniPrimary (citable) accession number: P81591
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1999
Last modified: October 1, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Its antimicrobial activity is strongly inhibited by divalent cations.

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.