Buccalin precursor - Aplysia californica (California sea hare)

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P20481 (BUCC_APLCA) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 48. History...

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

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names	Recommended name: Buccalin Cleaved into the following 21 chains: Buccalin-D Buccalin-E Buccalin-F Buccalin-G Buccalin-H Buccalin-A Buccalin-I Buccalin-J Buccalin-K Buccalin-L Buccalin-B Short name=BUCb Buccalin-M Buccalin gene-predicted acidic peptide A Short name=BGPAP A Buccalin-N Buccalin-O Buccalin-P Buccalin-Q Buccalin-R Buccalin-C Buccalin-S Buccalin gene-predicted acidic peptide B Short name=BGPAP B
Organism	Aplysia californica (California sea hare)
Taxonomic identifier	6500 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Mollusca › Gastropoda › Heterobranchia › Euthyneura › Euopisthobranchia › Aplysiomorpha › Aplysioidea › Aplysiidae › Aplysia

Protein attributes

Sequence length	505 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Domain	Signal
Molecular function	Neuropeptide
PTM	Amidation Cleavage on pair of basic residues Pyrrolidone carboxylic acid
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	neuropeptide signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

Potential

Propeptide

26 – 62

Potential

PRO_0000001881

Peptide

63 – 74

Buccalin-D

PRO_0000001882

Peptide

78 – 88

Buccalin-E

PRO_0000001883

Peptide

93 – 102

Buccalin-F

PRO_0000001884

Peptide

106 – 116

Buccalin-G

PRO_0000001885

Peptide

120 – 129

Buccalin-H Potential

PRO_0000001886

Peptide

133 – 143

Buccalin-A Ref.2

PRO_0000001887

Peptide

147 – 157

Buccalin-A

PRO_0000001888

Peptide

161 – 171

Buccalin-A

PRO_0000001889

Peptide

175 – 185

Buccalin-A

PRO_0000001890

Peptide

189 – 199

Buccalin-A

PRO_0000001891

Peptide

203 – 213

Buccalin-A

PRO_0000001892

Peptide

217 – 227

Buccalin-I Potential

PRO_0000001893

Peptide

231 – 241

Buccalin-J Potential

PRO_0000001894

Peptide

245 – 254

Buccalin-K Potential

PRO_0000001895

Peptide

258 – 267

Buccalin-L Potential

PRO_0000001896

Peptide

271 – 281

Buccalin-J Potential

PRO_0000001897

Peptide

285 – 294

Buccalin-L Potential

PRO_0000001898

Peptide

298 – 307

Buccalin-L Potential

PRO_0000001899

Peptide

311 – 321

Buccalin-B

PRO_0000001900

Peptide

325 – 335

Buccalin-M

PRO_0000001901

Peptide

339 – 349

Buccalin gene-predicted acidic peptide A Potential

PRO_0000001902

Peptide

353 – 363

Buccalin-N

PRO_0000001903

Peptide

367 – 377

Buccalin-B Ref.3

PRO_0000001904

Peptide

381 – 391

Buccalin-O Potential

PRO_0000001905

Peptide

396 – 405

Buccalin-P Potential

PRO_0000001906

Peptide

409 – 419

Buccalin-Q

PRO_0000001907

Peptide

424 – 433

Buccalin-R

PRO_0000001908

Peptide

437 – 447

Buccalin-C Ref.1

PRO_0000001909

Peptide

451 – 461

Buccalin-C

PRO_0000001910

Peptide

465 – 475

Buccalin-S

PRO_0000001911

Peptide

479 – 492

Buccalin gene-predicted acidic peptide B Potential

PRO_0000001912

Propeptide

495 – 505

Potential

PRO_0000001913

Amino acid modifications

Modified residue

Valine amide Potential

Modified residue

Leucine amide Potential

Modified residue

102

Leucine amide

Modified residue

106

Pyrrolidone carboxylic acid Potential

Modified residue

116

Isoleucine amide

Modified residue

129

Leucine amide Potential

Modified residue

143

Leucine amide Ref.2

Modified residue

157

Leucine amide Ref.2

Modified residue

171

Leucine amide Ref.2

Modified residue

185

Leucine amide Ref.2

Modified residue

199

Leucine amide Ref.2

Modified residue

213

Leucine amide Ref.2

Modified residue

227

Leucine amide Potential

Modified residue

241

Leucine amide Potential

Modified residue

254

Leucine amide Potential

Modified residue

267

Leucine amide

Modified residue

281

Leucine amide Potential

Modified residue

294

Leucine amide Potential

Modified residue

307

Leucine amide Potential

Modified residue

321

Leucine amide

Modified residue

335

Leucine amide

Modified residue

349

Glutamic acid 1-amide Potential

Modified residue

363

Leucine amide

Modified residue

377

Leucine amide

Modified residue

391

Leucine amide Potential

Modified residue

405

Leucine amide Potential

Modified residue

419

Leucine amide

Modified residue

433

Leucine amide

Modified residue

447

Isoleucine amide

Modified residue

461

Isoleucine amide

Modified residue

465

Pyrrolidone carboxylic acid Potential

Modified residue

475

Leucine amide

Sequences

Sequence

Length

Mass (Da)

Tools

P20481 [UniParc].

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

FASTA

505

53,517

        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

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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: 8101868] [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: 3413086] [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: 7991459] [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: 9809658] [Abstract] Cited for: MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S64298 mRNA. Translation: AAB27696.2.
PIR	A35594.
RefSeq	NP_001191649.1. NM_001204720.1.
UniGene	Acl.5094.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100533443.
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

BUCC_APLCA

Accession

Primary (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:	September 21, 2011
This is version 48 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Cleaved into the following 21 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Family and domain databases

Entry information