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P19802 (FMRF_LYMST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

FMRFamide induces contractions in visceral and somatic musculature as well as in the heart. May play a role as cotransmitters or modulators in a number of significant neuronal systems.

Subcellular location

Secreted.

Tissue specificity

Expressed in 280 cells of the CNS including the EGP heart excitatory motoneurons.

Sequence similarities

Belongs to the FARP (FMRFamide related peptide) family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
   Molecular functionNeuropeptide
   PTMAmidation
Cleavage on pair of basic residues
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processneuropeptide signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Isoform 1 and isoform 2 only share the N-terminal signal sequence.
Isoform 1 (identifier: P19802-1)

Also known as: FMRFamide;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P42565-1)

Also known as: FMRFamide-related;

The sequence of this isoform can be found in the external entry P42565.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Isoform 3 (identifier: P19802-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MKTWSHVALLACLSIKWLTCVMADSIYCDDPDMCSM → MYSPTLIVCLSFFHSAVTKRFLRFGRALDTT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Propeptide36 – 372
PRO_0000009668
Peptide40 – 434FLRF-amide 1
PRO_0000009669
Propeptide46 – 5611
PRO_0000009670
Peptide59 – 635QFYRI-amide
PRO_0000009671
Propeptide66 – 738
PRO_0000009672
Peptide76 – 794FLRF-amide 2
PRO_0000009673
Peptide82 – 10322PN Ref.4
PRO_0000009674
Propeptide108 – 14942
PRO_0000009675
Peptide152 – 1554FMRF-amide 1
PRO_0000009676
Propeptide158 – 1636
PRO_0000009677
Peptide166 – 1694FMRF-amide 2
PRO_0000009678
Propeptide171 – 1722
PRO_0000009679
Peptide173 – 1764FMRF-amide 3
PRO_0000009680
Propeptide179 – 1846
PRO_0000009681
Peptide187 – 1904FMRF-amide 4
PRO_0000009682
Peptide194 – 1974FMRF-amide 5
PRO_0000009683
Propeptide200 – 2045
PRO_0000009684
Peptide207 – 2104FMRF-amide 6
PRO_0000009685
Propeptide213 – 2175
PRO_0000009686
Peptide220 – 2234FMRF-amide 7
PRO_0000009687
Propeptide226 – 25126
PRO_0000009688
Peptide254 – 2574FMRF-amide 8
PRO_0000009689
Propeptide260 – 2634
PRO_0000009690
Peptide266 – 2694FMRF-amide 9
PRO_0000009691
Propeptide272 – 2787
PRO_0000009692
Peptide281 – 2855EFLRI-amide
PRO_0000009693
Propeptide289 – 30618
PRO_0000009694

Amino acid modifications

Modified residue431Phenylalanine amide
Modified residue631Isoleucine amide
Modified residue791Phenylalanine amide
Modified residue1551Phenylalanine amide
Modified residue1691Phenylalanine amide
Modified residue1761Phenylalanine amide
Modified residue1901Phenylalanine amide
Modified residue1971Phenylalanine amide
Modified residue2101Phenylalanine amide
Modified residue2231Phenylalanine amide
Modified residue2571Phenylalanine amide
Modified residue2691Phenylalanine amide
Modified residue2851Isoleucine amide

Natural variations

Alternative sequence1 – 3636MKTWS…DMCSM → MYSPTLIVCLSFFHSAVTKR FLRFGRALDTT in isoform 3.
VSP_001564

Experimental info

Sequence conflict911L → P in AAA63280. Ref.1
Sequence conflict2731E → Q in AAA63280. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (FMRFamide) [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: AB2361EFF2C4EF18

FASTA30636,351
        10         20         30         40         50         60 
MKTWSHVALL ACLSIKWLTC VMADSIYCDD PDMCSMTKRF LRFGRALDTT DPFIRLRRQF 

        70         80         90        100        110        120 
YRIGRGGYQP YQDKRFLRFG RSEQPDVDDY LRDVVLQSEE PLYRKRRSTE AGGQSEEMTH 

       130        140        150        160        170        180 
RTARSAPEPA AENREIMKRE TGAEDLDEEK RFMRFGRGDE EAEKRFMRFG KSFMRFGRDM 

       190        200        210        220        230        240 
SDVDKRFMRF GKRFMRFGRE PGTDKRFMRF GREPGADKRF MRFGKSFDGE EENDDDLYYN 

       250        260        270        280        290        300 
ESDADSNDDV DKRFMRFGKS AEEKRFMRFG KSEDASRDKK EFLRIGKRES RSAEVENNIQ 


IAAKQS 

« Hide

Isoform 2 (FMRFamide-related) [UniParc].

See P42565.

Isoform 3 [UniParc].

Checksum: 43038865D26D9B20
Show »

FASTA30135,847

References

[1]"Cardioactive neuropeptide Phe-Met-Arg-Phe-NH2 (FMRFamide) and novel related peptides are encoded in multiple copies by a single gene in the snail Lymnaea stagnalis."
Linacre A., Kellett E., Saunders S., Bright K., Benjamin P.R., Burke J.F.
J. Neurosci. 10:412-419(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Genomic organization of the FMRFamide gene in Lymnaea: multiple exons encoding novel neuropeptides."
Kellett E., Saunders S.E., Li K.W., Staddon J.W., Benjamin P.R., Burke J.F.
J. Neurosci. 14:6564-6570(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]"Cell-specific alternative RNA splicing of an FMRFamide gene transcript in the brain."
Saunders S.E., Kellett E., Bright K., Benjamin P.R., Burke J.F.
J. Neurosci. 12:1033-1039(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: CNS.
[4]"Processing of the FMRFamide precursor protein in the snail Lymnaea stagnalis: characterization and neuronal localization of a novel peptide, 'SEEPLY'."
Santama N., Li K.W., Bright K.E., Yeoman M., Geraerts W.P.M., Benjamin P.R., Burke J.F.
Eur. J. Neurosci. 5:1003-1016(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 82-103 (PN).
Tissue: CNS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M37629 mRNA. Translation: AAA63280.1.
M87479 Genomic DNA. No translation available.
S38686 mRNA. Translation: AAB21767.1.
S94982 Genomic DNA. Translation: AAB21764.1.
PIRA37016.
F44840.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002544. FMRFamid-related_peptide-like.
[Graphical view]
PfamPF01581. FARP. 13 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFMRF_LYMST
AccessionPrimary (citable) accession number: P19802
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 1, 1995
Last modified: April 3, 2013
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families