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P20481

- BUCC_APLCA

UniProt

P20481 - BUCC_APLCA

Protein

Buccalin

Gene
N/A
Organism
Aplysia californica (California sea hare)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Modulatory neuropeptide, acting presynaptically on nerve terminals to inhibit acetylcholine release.1 Publication

    GO - Biological processi

    1. neuropeptide signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Neuropeptide

    Names & Taxonomyi

    Protein namesi
    OrganismiAplysia californica (California sea hare)
    Taxonomic identifieri6500 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraEuopisthobranchiaAplysiomorphaAplysioideaAplysiidaeAplysia

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Propeptidei26 – 6237Sequence AnalysisPRO_0000001881Add
    BLAST
    Peptidei63 – 7412Buccalin-DPRO_0000001882Add
    BLAST
    Peptidei78 – 8811Buccalin-EPRO_0000001883Add
    BLAST
    Peptidei93 – 10210Buccalin-FPRO_0000001884
    Peptidei106 – 11611Buccalin-GPRO_0000001885Add
    BLAST
    Peptidei120 – 12910Buccalin-HSequence AnalysisPRO_0000001886
    Peptidei133 – 14311Buccalin-APRO_0000001887Add
    BLAST
    Peptidei147 – 15711Buccalin-APRO_0000001888Add
    BLAST
    Peptidei161 – 17111Buccalin-APRO_0000001889Add
    BLAST
    Peptidei175 – 18511Buccalin-APRO_0000001890Add
    BLAST
    Peptidei189 – 19911Buccalin-APRO_0000001891Add
    BLAST
    Peptidei203 – 21311Buccalin-APRO_0000001892Add
    BLAST
    Peptidei217 – 22711Buccalin-ISequence AnalysisPRO_0000001893Add
    BLAST
    Peptidei231 – 24111Buccalin-JSequence AnalysisPRO_0000001894Add
    BLAST
    Peptidei245 – 25410Buccalin-KSequence AnalysisPRO_0000001895
    Peptidei258 – 26710Buccalin-LSequence AnalysisPRO_0000001896
    Peptidei271 – 28111Buccalin-JSequence AnalysisPRO_0000001897Add
    BLAST
    Peptidei285 – 29410Buccalin-LSequence AnalysisPRO_0000001898
    Peptidei298 – 30710Buccalin-LSequence AnalysisPRO_0000001899
    Peptidei311 – 32111Buccalin-BPRO_0000001900Add
    BLAST
    Peptidei325 – 33511Buccalin-MPRO_0000001901Add
    BLAST
    Peptidei339 – 34911Buccalin gene-predicted acidic peptide ASequence AnalysisPRO_0000001902Add
    BLAST
    Peptidei353 – 36311Buccalin-NPRO_0000001903Add
    BLAST
    Peptidei367 – 37711Buccalin-BPRO_0000001904Add
    BLAST
    Peptidei381 – 39111Buccalin-OSequence AnalysisPRO_0000001905Add
    BLAST
    Peptidei396 – 40510Buccalin-PSequence AnalysisPRO_0000001906
    Peptidei409 – 41911Buccalin-QPRO_0000001907Add
    BLAST
    Peptidei424 – 43310Buccalin-RPRO_0000001908
    Peptidei437 – 44711Buccalin-CPRO_0000001909Add
    BLAST
    Peptidei451 – 46111Buccalin-CPRO_0000001910Add
    BLAST
    Peptidei465 – 47511Buccalin-SPRO_0000001911Add
    BLAST
    Peptidei479 – 49214Buccalin gene-predicted acidic peptide BSequence AnalysisPRO_0000001912Add
    BLAST
    Propeptidei495 – 50511Sequence AnalysisPRO_0000001913Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei74 – 741Valine amideSequence Analysis
    Modified residuei88 – 881Leucine amideSequence Analysis
    Modified residuei102 – 1021Leucine amide
    Modified residuei106 – 1061Pyrrolidone carboxylic acidSequence Analysis
    Modified residuei116 – 1161Isoleucine amide
    Modified residuei129 – 1291Leucine amideSequence Analysis
    Modified residuei143 – 1431Leucine amide1 Publication
    Modified residuei157 – 1571Leucine amide1 Publication
    Modified residuei171 – 1711Leucine amide1 Publication
    Modified residuei185 – 1851Leucine amide1 Publication
    Modified residuei199 – 1991Leucine amide1 Publication
    Modified residuei213 – 2131Leucine amide1 Publication
    Modified residuei227 – 2271Leucine amideSequence Analysis
    Modified residuei241 – 2411Leucine amideSequence Analysis
    Modified residuei254 – 2541Leucine amideSequence Analysis
    Modified residuei267 – 2671Leucine amide
    Modified residuei281 – 2811Leucine amideSequence Analysis
    Modified residuei294 – 2941Leucine amideSequence Analysis
    Modified residuei307 – 3071Leucine amideSequence Analysis
    Modified residuei321 – 3211Leucine amide
    Modified residuei335 – 3351Leucine amide
    Modified residuei349 – 3491Glutamic acid 1-amideSequence Analysis
    Modified residuei363 – 3631Leucine amide
    Modified residuei377 – 3771Leucine amide
    Modified residuei391 – 3911Leucine amideSequence Analysis
    Modified residuei405 – 4051Leucine amideSequence Analysis
    Modified residuei419 – 4191Leucine amide
    Modified residuei433 – 4331Leucine amide
    Modified residuei447 – 4471Isoleucine amide
    Modified residuei461 – 4611Isoleucine amide
    Modified residuei465 – 4651Pyrrolidone carboxylic acidSequence Analysis
    Modified residuei475 – 4751Leucine amide

    Keywords - PTMi

    Amidation, Cleavage on pair of basic residues, Pyrrolidone carboxylic acid

    Expressioni

    Tissue specificityi

    Cholinergic motor neuron B15 innervating buccal muscles in Aplysia.

    Family & Domainsi

    Keywords - Domaini

    Signal

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P20481-1 [UniParc]FASTAAdd to Basket

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    MAHHRGHRHI LLYVSLALSL GLALAEDATD PSDDTGSFDD VEAVSEEADL    50
    DPYSMSQELN KRPNVDPYSY LPSVGKRAFD HYGFTGGLGK RKIDHFGFVG 100
    GLGKRQIDPL GFSGGIGKRY DSFAYSAGLG KRGMDSLAFS GGLGKRGMDS 150
    LAFSGGLGKR GMDSLAFSGG LGKRGMDSLA FSGGLGKRGM DSLAFSGGLG 200
    KRGMDSLAFS GGLGKRGMDS FTFAPGLGKR GMDSLAFAGG LGKRMDGFAF 250
    APGLGKRMDS FAFAPGLGKR GMDSLAFAGG LGKRMDSFAF APGLGKRMDS 300
    FAFAPGLGKR GLDRYGFVGG LGKRGMDHFA FTGGLGKRDS GEASGDLEEG 350
    KRGLDAYSFT GALGKRGLDR YGFVGGLGKR GMDDFAFSPG LGKKRMDSFM 400
    FGSRLGKRGM DRFSFSGHLG KRKMDQFSFG PGLGKRGFDH YGFTGGIGKR 450
    GFDHYGFTGG IGKRQLDPML FSGRLGKRSS SEQEEEDVRQ VEKRSTTEEQ 500
    SSKSL 505
    Length:505
    Mass (Da):53,517
    Last modified:October 1, 1996 - v2
    Checksum:iFC17DB022C818D51
    GO

    Mass spectrometryi

    Molecular mass is 1059.1±0.4 Da from positions 93 - 102. Determined by MALDI. 1 Publication
    Molecular mass is 1101.6±0.0 Da from positions 106 - 116. Determined by MALDI. 1 Publication
    Molecular mass is 1052.8±0.3 Da from positions 133 - 143. Determined by MALDI. Buccalin-A.1 Publication
    Molecular mass is 1053.6±0.1 Da from positions 258 - 267. Determined by MALDI. 1 Publication
    Molecular mass is 1151.9±0.3 Da from positions 311 - 321. Determined by MALDI. Buccalin-B.1 Publication
    Molecular mass is 1150.6±0.1 Da from positions 325 - 335. Determined by MALDI. 1 Publication
    Molecular mass is 1112.9±0.4 Da from positions 353 - 363. Determined by MALDI. 1 Publication
    Molecular mass is 1251.6±0.0 Da from positions 409 - 419. Determined by MALDI. 1 Publication
    Molecular mass is 1096.7±0.2 Da from positions 424 - 433. Determined by MALDI. 1 Publication
    Molecular mass is 1168.7±0.2 Da from positions 437 - 447. Determined by MALDI. Buccalin-C.1 Publication
    Molecular mass is 1274.9±0.2 Da from positions 465 - 475. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S64298 mRNA. Translation: AAB27696.2.
    PIRiA35594.
    RefSeqiNP_001191649.1. NM_001204720.1.
    UniGeneiAcl.5094.

    Genome annotation databases

    GeneIDi100533443.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S64298 mRNA. Translation: AAB27696.2 .
    PIRi A35594.
    RefSeqi NP_001191649.1. NM_001204720.1.
    UniGenei Acl.5094.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100533443.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiBUCC_APLCA
    AccessioniPrimary (citable) accession number: P20481
    Secondary accession number(s): Q9TWM2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 51 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    External Data

    Dasty 3