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Reviewed, UniProtKB/Swiss-Prot P35904 (ACH1_ACHFU)

Last modified November 4, 2008. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | 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

Names and origin

Protein namesRecommended name:
    Achatin-1
Alternative name(s):
    Achatin-I
OrganismAchatina fulica (Giant African snail)
Taxonomic identifier6530 [NCBI]
Taxonomic lineageEukaryotaMetazoaMolluscaGastropodaPulmonataStylommatophoraSigmurethraAchatinoideaAchatinidaeAchatina

Protein attributes

Sequence length4 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Neuroexcitatory peptide; increases the impulse frequency and produces a spike broadening of the identified heart excitatory neuron (PON); also enhances the amplitude and frequency of the heart beat. Has also an effect on several other muscles.

Ontologies

Keywords
   Molecular functionHormone
   PTMD-amino acid
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular functionhormone activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Peptide1 – 44Achatin-1
PRO_0000044101

Amino acid modifications

Modified residue21D-phenylalanine Ref.1

Sequences

Sequence LengthMass (Da)Tools
P35904-1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 6AADD9C810000000

FASTA4408
GFAD 

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References

[1]"Achatin-I, an endogenous neuroexcitatory tetrapeptide from Achatina fulica Ferussac containing a D-amino acid residue."
Kamatani Y., Minakata H., Kenny P.T.M., Iwashita T., Watanabe K., Funase K., Sun X.P., Yongsiri A., Kim K.H., Novales-Li P., Novales E.T., Kanapi C.G., Takeuchi H., Nomoto K.
Biochem. Biophys. Res. Commun. 160:1015-1020(1989) [PubMed: 2597281] [Abstract]
Cited for: PROTEIN SEQUENCE, D-AMINO ACID AT PHE-2, CHARACTERIZATION, SYNTHESIS.
Strain: Ferussac.
Tissue: Ganglion.
[2]"Purification of achatin-I from the atria of the African giant snail, Achatina fulica, and its possible function."
Fujimoto K., Kubota I., Yasuda-Kamatani Y., Minakata H., Nomoto K., Yoshida M., Harada A., Muneoka Y., Kobayashi M.
Biochem. Biophys. Res. Commun. 177:847-853(1991) [PubMed: 1675568] [Abstract]
Cited for: CHARACTERIZATION.
Strain: Ferussac.
Tissue: Heart atrium.
[3]"Crystal structure and molecular conformation of achatin-I (H-Gly-D-Phe-Ala-Asp-OH), an endogenous neuropeptide containing a D-amino acid residue."
Ishida T., In Y., Doi M., Inoue M., Yasuda-Kamatani Y., Minakata H., Iwashita T., Nomoto K.
Int. J. Pept. Protein Res. 39:258-264(1992) [PubMed: 1399265] [Abstract]
Cited for: CRYSTALLIZATION.

Cross-references

Sequence databases

PIRA32480.

3D structure databases

ModBaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameACH1_ACHFU
AccessionPrimary (citable) accession number: P35904
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 4, 2008
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information