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MYOM1_APLCA
ID   MYOM1_APLCA             Reviewed;         370 AA.
AC   P15513; Q07974; Q27916;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Myomodulin neuropeptides 1;
DE   Contains:
DE     RecName: Full=Myomodulin-A;
DE              Short=MM-A;
DE     AltName: Full=Neuron B16 peptide;
DE     AltName: Full=PMSMLRL-amide;
DE   Contains:
DE     RecName: Full=Myomodulin-B;
DE              Short=MM-B;
DE              Short=MMb;
DE     AltName: Full=GSYRMMRL-amide;
DE   Contains:
DE     RecName: Full=Myomodulin-D;
DE              Short=MM-D;
DE              Short=MMd;
DE     AltName: Full=GLSMLRL-amide;
DE   Contains:
DE     RecName: Full=Myomodulin-F;
DE              Short=MM-F;
DE              Short=MMf;
DE     AltName: Full=SLNMLRL-amide;
DE   Contains:
DE     RecName: Full=Myomodulin-G;
DE              Short=MM-G;
DE              Short=MMg;
DE     AltName: Full=TLSMLRL-amide;
DE   Contains:
DE     RecName: Full=Myomodulin-H;
DE              Short=MM-H;
DE              Short=MMh;
DE     AltName: Full=GLHMLRL-amide;
DE   Contains:
DE     RecName: Full=Myomodulin-I;
DE              Short=MM-I;
DE              Short=MMi;
DE     AltName: Full=SLSMLRL-amide;
DE   Flags: Precursor;
GN   Name=MYOMOD1;
OS   Aplysia californica (California sea hare).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC   Aplysiidae; Aplysia.
OX   NCBI_TaxID=6500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-362, AND TISSUE SPECIFICITY.
RC   TISSUE=Abdominal ganglion, Cerebral ganglion, and CNS;
RX   PubMed=8422272; DOI=10.1089/dna.1993.12.53;
RA   Lopez V., Wickham L., Desgroseillers L.;
RT   "Molecular cloning of myomodulin cDNA, a neuropeptide precursor gene
RT   expressed in neuron L10 of Aplysia californica.";
RL   DNA Cell Biol. 12:53-61(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Buccal ganglion;
RX   PubMed=8340812; DOI=10.1523/jneurosci.13-08-03358.1993;
RA   Miller M.W., Beushausen S., Vitek A., Stamm S., Kupfermann I., Brosius J.,
RA   Weiss K.R.;
RT   "The myomodulin-related neuropeptides: characterization of a gene encoding
RT   a family of peptide cotransmitters in Aplysia.";
RL   J. Neurosci. 13:3358-3367(1993).
RN   [3]
RP   PROTEIN SEQUENCE OF 53-60, AMIDATION AT LEU-60, FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Buccal muscle;
RX   PubMed=1788132; DOI=10.1016/0196-9781(91)90120-e;
RA   Cropper E.C., Vilim F.S., Alevizos A., Tenenbaum R., Kolks M.A.G.,
RA   Rosen S., Kupfermann I., Weiss K.R.;
RT   "Structure, bioactivity, and cellular localization of myomodulin B: a novel
RT   Aplysia peptide.";
RL   Peptides 12:683-690(1991).
RN   [4]
RP   PROTEIN SEQUENCE OF 63-69; 193-199; 203-209; 240-246 AND 358-364, AMIDATION
RP   AT LEU-69; LEU-199; LEU-209; LEU-246 AND LEU-364, AND FUNCTION.
RC   TISSUE=Buccal muscle;
RX   PubMed=7472354; DOI=10.1152/jn.1995.74.1.54;
RA   Brezina V., Bank B., Cropper E.C., Rosen S., Vilim F.S., Kupfermann I.,
RA   Weiss K.R.;
RT   "Nine members of the myomodulin family of peptide cotransmitters at the
RT   B16-ARC neuromuscular junction of Aplysia.";
RL   J. Neurophysiol. 74:54-72(1995).
RN   [5]
RP   PROTEIN SEQUENCE OF MYOMODULIN A, AMIDATION AT LEU-256; LEU-266; LEU-276;
RP   LEU-286; LEU-296; LEU-306; LEU-316; LEU-326; LEU-336 AND LEU-346, AND
RP   FUNCTION.
RC   TISSUE=Buccal muscle;
RX   PubMed=3474664; DOI=10.1073/pnas.84.15.5483;
RA   Cropper E.C., Tenenbaum R., Kolks M.A.G., Kupfermann I., Weiss K.R.;
RT   "Myomodulin: a bioactive neuropeptide present in an identified cholinergic
RT   buccal motor neuron of Aplysia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:5483-5486(1987).
CC   -!- FUNCTION: Exogenous application of myomodulins potentiates ARC muscle
CC       contraction. {ECO:0000269|PubMed:1788132, ECO:0000269|PubMed:3474664,
CC       ECO:0000269|PubMed:7472354}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in all ganglia of the CNS, but only in a
CC       subset of neurons including L10 in the abdominal ganglion and B16 in
CC       the buccal ganglion. {ECO:0000269|PubMed:1788132,
CC       ECO:0000269|PubMed:8340812, ECO:0000269|PubMed:8422272}.
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DR   EMBL; L01421; AAA27758.1; -; mRNA.
DR   EMBL; S55210; AAB25131.1; -; mRNA.
DR   EMBL; S55211; AAB25132.1; -; mRNA.
DR   EMBL; S64300; AAB27697.1; -; mRNA.
DR   PIR; A28340; A28340.
DR   RefSeq; NP_001191423.1; NM_001204494.1.
DR   AlphaFoldDB; P15513; -.
DR   GeneID; 100533334; -.
DR   CTD; 100533334; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Neuropeptide; Repeat; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..50
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000001837"
FT   PEPTIDE         53..60
FT                   /note="Myomodulin-B"
FT                   /evidence="ECO:0000269|PubMed:1788132"
FT                   /id="PRO_0000001838"
FT   PEPTIDE         63..69
FT                   /note="Myomodulin-H"
FT                   /evidence="ECO:0000269|PubMed:7472354"
FT                   /id="PRO_0000001839"
FT   PROPEP          73..190
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000001840"
FT   PEPTIDE         193..199
FT                   /note="Myomodulin-I"
FT                   /evidence="ECO:0000269|PubMed:7472354"
FT                   /id="PRO_0000001841"
FT   PEPTIDE         203..209
FT                   /note="Myomodulin-D"
FT                   /evidence="ECO:0000269|PubMed:7472354"
FT                   /id="PRO_0000001842"
FT   PROPEP          213..237
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000001843"
FT   PEPTIDE         240..246
FT                   /note="Myomodulin-G"
FT                   /evidence="ECO:0000269|PubMed:7472354"
FT                   /id="PRO_0000001844"
FT   PEPTIDE         250..256
FT                   /note="Myomodulin-A"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT                   /id="PRO_0000001845"
FT   PEPTIDE         260..266
FT                   /note="Myomodulin-A"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT                   /id="PRO_0000001846"
FT   PEPTIDE         270..276
FT                   /note="Myomodulin-A"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT                   /id="PRO_0000001847"
FT   PEPTIDE         280..286
FT                   /note="Myomodulin-A"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT                   /id="PRO_0000001848"
FT   PEPTIDE         290..296
FT                   /note="Myomodulin-A"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT                   /id="PRO_0000001849"
FT   PEPTIDE         300..306
FT                   /note="Myomodulin-A"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT                   /id="PRO_0000001850"
FT   PEPTIDE         310..316
FT                   /note="Myomodulin-A"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT                   /id="PRO_0000001851"
FT   PEPTIDE         320..326
FT                   /note="Myomodulin-A"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT                   /id="PRO_0000001852"
FT   PEPTIDE         330..336
FT                   /note="Myomodulin-A"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT                   /id="PRO_0000001853"
FT   PEPTIDE         340..346
FT                   /note="Myomodulin-A"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT                   /id="PRO_0000001854"
FT   PROPEP          350..355
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000001855"
FT   PEPTIDE         358..364
FT                   /note="Myomodulin-F"
FT                   /evidence="ECO:0000269|PubMed:7472354"
FT                   /id="PRO_0000001856"
FT   PROPEP          368..370
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000001857"
FT   REGION          28..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..362
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         60
FT                   /note="Leucine amide"
FT   MOD_RES         69
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:7472354"
FT   MOD_RES         199
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:7472354"
FT   MOD_RES         209
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:7472354"
FT   MOD_RES         246
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:7472354"
FT   MOD_RES         256
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT   MOD_RES         266
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT   MOD_RES         276
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT   MOD_RES         286
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT   MOD_RES         296
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT   MOD_RES         306
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT   MOD_RES         316
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT   MOD_RES         326
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT   MOD_RES         336
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT   MOD_RES         346
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:3474664"
FT   MOD_RES         364
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:7472354"
FT   VARIANT         362
FT                   /note="S -> L"
FT                   /evidence="ECO:0000269|PubMed:8422272"
FT   CONFLICT        231
FT                   /note="D -> A (in Ref. 2; AAB27697)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   370 AA;  42254 MW;  3A792085939C88CB CRC64;
     MQVYMLLPLA VFASLTYQGA CEETAAAQTS SDASTSSASS EHAENELSRA KRGSYRMMRL
     GRGLHMLRLG KRGGPVEPES EENLETLLNL LQGYYSDVPE YPSEFDDTDL AYPYEEYDAP
     AHPRYRRSTP PTDGVVAPDV LQKGSSEFED FGDSQLDESD EGYYGYDPEN YLYGDFEDYL
     EPEEGGLGEE KRSLSMLRLG KRGLSMLRLG KREGEEGDEM DKKQDESLND DFENDDIKRT
     LSMLRLGKRP MSMLRLGKRP MSMLRLGKRP MSMLRLGKRP MSMLRLGKRP MSMLRLGKRP
     MSMLRLGKRP MSMLRLGKRP MSMLRLGKRP MSMLRLGKRP MSMLRLGKRD DDEKEKKSLN
     MSRLGKRSTQ
 
 
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