P35904 (ACH1_ACHFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Achatin-1 Alternative name(s): Achatin-I
Organism	Achatina fulica (Giant African snail)
Taxonomic identifier	6530 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Mollusca › Gastropoda › Heterobranchia › Euthyneura › Panpulmonata › Eupulmonata › Stylommatophora › Sigmurethra › Achatinoidea › Achatinidae › Achatina

Protein attributes

Sequence length	4 AA.
Sequence status	Complete.
Protein existence	Evidence 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 function	Hormone
PTM	D-amino acid
Technical term	Direct protein sequencing
Gene Ontology (GO)
Molecular function	hormone activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Peptide	1 – 4	4	Achatin-1		PRO_0000044101
Amino acid modifications
	Modified residue	2	1	D-phenylalanine Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P35904 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 6AADD9C810000000	FASTA	4	408
	GFAD

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
PIR	A32480.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

ACH1_ACHFU

Accession

Primary (citable) accession number: P35904

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	March 8, 2011
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)