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P20481 (BUCC_APLCA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Modulatory neuropeptide, acting presynaptically on nerve terminals to inhibit acetylcholine release. Ref.3

Subcellular location

Secreted.

Tissue specificity

Cholinergic motor neuron B15 innervating buccal muscles in Aplysia.

Mass spectrometry

Molecular mass is 1059.1±0.4 Da from positions 93 - 102. Determined by MALDI. Ref.4

Molecular mass is 1101.6±0.0 Da from positions 106 - 116. Determined by MALDI. Ref.4

Molecular mass is 1052.8±0.3 Da from positions 133 - 143. Determined by MALDI. Buccalin-A. Ref.4

Molecular mass is 1053.6±0.1 Da from positions 258 - 267. Determined by MALDI. Ref.4

Molecular mass is 1151.9±0.3 Da from positions 311 - 321. Determined by MALDI. Buccalin-B. Ref.4

Molecular mass is 1150.6±0.1 Da from positions 325 - 335. Determined by MALDI. Ref.4

Molecular mass is 1112.9±0.4 Da from positions 353 - 363. Determined by MALDI. Ref.4

Molecular mass is 1251.6±0.0 Da from positions 409 - 419. Determined by MALDI. Ref.4

Molecular mass is 1096.7±0.2 Da from positions 424 - 433. Determined by MALDI. Ref.4

Molecular mass is 1168.7±0.2 Da from positions 437 - 447. Determined by MALDI. Buccalin-C. Ref.4

Molecular mass is 1274.9±0.2 Da from positions 465 - 475. Determined by MALDI. Ref.4

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionNeuropeptide
   PTMAmidation
Cleavage on pair of basic residues
Pyrrolidone carboxylic acid
   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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – 6237 Potential
PRO_0000001881
Peptide63 – 7412Buccalin-D
PRO_0000001882
Peptide78 – 8811Buccalin-E
PRO_0000001883
Peptide93 – 10210Buccalin-F
PRO_0000001884
Peptide106 – 11611Buccalin-G
PRO_0000001885
Peptide120 – 12910Buccalin-H Potential
PRO_0000001886
Peptide133 – 14311Buccalin-A Ref.2
PRO_0000001887
Peptide147 – 15711Buccalin-A
PRO_0000001888
Peptide161 – 17111Buccalin-A
PRO_0000001889
Peptide175 – 18511Buccalin-A
PRO_0000001890
Peptide189 – 19911Buccalin-A
PRO_0000001891
Peptide203 – 21311Buccalin-A
PRO_0000001892
Peptide217 – 22711Buccalin-I Potential
PRO_0000001893
Peptide231 – 24111Buccalin-J Potential
PRO_0000001894
Peptide245 – 25410Buccalin-K Potential
PRO_0000001895
Peptide258 – 26710Buccalin-L Potential
PRO_0000001896
Peptide271 – 28111Buccalin-J Potential
PRO_0000001897
Peptide285 – 29410Buccalin-L Potential
PRO_0000001898
Peptide298 – 30710Buccalin-L Potential
PRO_0000001899
Peptide311 – 32111Buccalin-B
PRO_0000001900
Peptide325 – 33511Buccalin-M
PRO_0000001901
Peptide339 – 34911Buccalin gene-predicted acidic peptide A Potential
PRO_0000001902
Peptide353 – 36311Buccalin-N
PRO_0000001903
Peptide367 – 37711Buccalin-B Ref.3
PRO_0000001904
Peptide381 – 39111Buccalin-O Potential
PRO_0000001905
Peptide396 – 40510Buccalin-P Potential
PRO_0000001906
Peptide409 – 41911Buccalin-Q
PRO_0000001907
Peptide424 – 43310Buccalin-R
PRO_0000001908
Peptide437 – 44711Buccalin-C Ref.1
PRO_0000001909
Peptide451 – 46111Buccalin-C
PRO_0000001910
Peptide465 – 47511Buccalin-S
PRO_0000001911
Peptide479 – 49214Buccalin gene-predicted acidic peptide B Potential
PRO_0000001912
Propeptide495 – 50511 Potential
PRO_0000001913

Amino acid modifications

Modified residue741Valine amide Potential
Modified residue881Leucine amide Potential
Modified residue1021Leucine amide
Modified residue1061Pyrrolidone carboxylic acid Potential
Modified residue1161Isoleucine amide
Modified residue1291Leucine amide Potential
Modified residue1431Leucine amide Ref.2
Modified residue1571Leucine amide Ref.2
Modified residue1711Leucine amide Ref.2
Modified residue1851Leucine amide Ref.2
Modified residue1991Leucine amide Ref.2
Modified residue2131Leucine amide Ref.2
Modified residue2271Leucine amide Potential
Modified residue2411Leucine amide Potential
Modified residue2541Leucine amide Potential
Modified residue2671Leucine amide
Modified residue2811Leucine amide Potential
Modified residue2941Leucine amide Potential
Modified residue3071Leucine amide Potential
Modified residue3211Leucine amide
Modified residue3351Leucine amide
Modified residue3491Glutamic acid 1-amide Potential
Modified residue3631Leucine amide
Modified residue3771Leucine amide
Modified residue3911Leucine amide Potential
Modified residue4051Leucine amide Potential
Modified residue4191Leucine amide
Modified residue4331Leucine amide
Modified residue4471Isoleucine amide
Modified residue4611Isoleucine amide
Modified residue4651Pyrrolidone carboxylic acid Potential
Modified residue4751Leucine amide

Sequences

Sequence LengthMass (Da)Tools
P20481 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: FC17DB022C818D51

FASTA50553,517
        10         20         30         40         50         60 
MAHHRGHRHI LLYVSLALSL GLALAEDATD PSDDTGSFDD VEAVSEEADL DPYSMSQELN 

        70         80         90        100        110        120 
KRPNVDPYSY LPSVGKRAFD HYGFTGGLGK RKIDHFGFVG GLGKRQIDPL GFSGGIGKRY 

       130        140        150        160        170        180 
DSFAYSAGLG KRGMDSLAFS GGLGKRGMDS LAFSGGLGKR GMDSLAFSGG LGKRGMDSLA 

       190        200        210        220        230        240 
FSGGLGKRGM DSLAFSGGLG KRGMDSLAFS GGLGKRGMDS FTFAPGLGKR GMDSLAFAGG 

       250        260        270        280        290        300 
LGKRMDGFAF APGLGKRMDS FAFAPGLGKR GMDSLAFAGG LGKRMDSFAF APGLGKRMDS 

       310        320        330        340        350        360 
FAFAPGLGKR GLDRYGFVGG LGKRGMDHFA FTGGLGKRDS GEASGDLEEG KRGLDAYSFT 

       370        380        390        400        410        420 
GALGKRGLDR YGFVGGLGKR GMDDFAFSPG LGKKRMDSFM FGSRLGKRGM DRFSFSGHLG 

       430        440        450        460        470        480 
KRKMDQFSFG PGLGKRGFDH YGFTGGIGKR GFDHYGFTGG IGKRQLDPML FSGRLGKRSS 

       490        500 
SEQEEEDVRQ VEKRSTTEEQ SSKSL 

« Hide

References

[1]"The buccalin-related neuropeptides: isolation and characterization of an Aplysia cDNA clone encoding a family of peptide cotransmitters."
Miller M.W., Beushausen S., Cropper E.C., Eisinger K., Stamm S., Vilim F.S., Vitek A., Zajc A., Kupfermann I., Brosius J., Weiss K.R.
J. Neurosci. 13:3346-3357(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 437-447 AND 451-461.
[2]"Structure and action of buccalin: a modulatory neuropeptide localized to an identified small cardioactive peptide-containing cholinergic motor neuron of Aplysia californica."
Cropper E.C., Miller M.W., Tenenbaum R., Kolks M.A.G., Kupfermann I., Weiss K.R.
Proc. Natl. Acad. Sci. U.S.A. 85:6177-6181(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 133-143; 147-157; 161-171; 175-185; 189-199 AND 203-213, AMIDATION AT LEU-143; LEU-157; LEU-171; LEU-185; LEU-199 AND LEU-213.
[3]"Structure, localization, and action of buccalin B: a bioactive peptide from Aplysia."
Vilim F.S., Cropper E.C., Rosen S.C., Tenenbaum R., Kupfermann I., Weiss K.R.
Peptides 15:959-969(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 367-377, FUNCTION.
[4]"Mass spectrometric survey of interganglionically transported peptides in Aplysia."
Li L., Moroz T.P., Garden R.W., Floyd P.D., Weiss K.R., Sweedler J.V.
Peptides 19:1425-1433(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S64298 mRNA. Translation: AAB27696.2.
PIRA35594.
RefSeqNP_001191649.1. NM_001204720.1.
UniGeneAcl.5094.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100533443.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameBUCC_APLCA
AccessionPrimary (citable) accession number: P20481
Secondary accession number(s): Q9TWM2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 1, 1996
Last modified: April 3, 2013
This is version 50 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)