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BRK1A_BOMMX
ID   BRK1A_BOMMX             Reviewed;         294 AA.
AC   Q7T3L1;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Kininogen-1a;
DE   Contains:
DE     RecName: Full=Maximakinin;
DE     AltName: Full=Bombinakinin M;
DE   Contains:
DE     RecName: Full=Bradykinin;
DE   Contains:
DE     RecName: Full=Bombinakinin-GAP;
DE     AltName: Full=Bombinakinin M gene-associated protein;
DE   Flags: Precursor;
OS   Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Bombinatoridae; Bombina.
OX   NCBI_TaxID=161274;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAP47179.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 265-292, SYNTHESIS OF
RP   265-292, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, DISULFIDE BOND, AND AMIDATION AT VAL-292.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:12668203};
RX   PubMed=12668203; DOI=10.1016/s0196-9781(03)00027-5;
RA   Lai R., Liu H., Lee W.H., Zhang Y.;
RT   "Bombinakinin M gene associated peptide, a novel bioactive peptide from
RT   skin secretions of the toad Bombina maxima.";
RL   Peptides 24:199-204(2003).
RN   [2]
RP   SYNTHESIS OF 265-292, AND FUNCTION.
RX   PubMed=20138946; DOI=10.1016/j.peptides.2010.01.016;
RA   Wang L., Chen Y., Yang M., Zhou M., Chen T., Sui D.Y., Shaw C.;
RT   "Peptide DV-28 amide: An inhibitor of bradykinin-induced arterial smooth
RT   muscle relaxation encoded by Bombina orientalis skin kininogen-2.";
RL   Peptides 31:979-982(2010).
CC   -!- FUNCTION: [Bombinakinin-GAP]: Plays a role in the control of feeding by
CC       the brain; intracerebroventricular administration of the peptide
CC       induced significant decrease in food intake in rats. Inhibits the
CC       bradykinin-induced in vitro relaxation of rat arterial smooth muscle.
CC       May target bradykinin receptors (BDKRB). {ECO:0000269|PubMed:12668203,
CC       ECO:0000269|PubMed:20138946}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12668203}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:12668203}.
CC   -!- MASS SPECTROMETRY: [Bombinakinin-GAP]: Mass=3228; Mass_error=0.4;
CC       Method=FAB; Evidence={ECO:0000269|PubMed:12668203};
CC   -!- SIMILARITY: Belongs to the bradykinin-related peptide family.
CC       {ECO:0000305}.
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DR   EMBL; AF515613; AAP47179.1; -; mRNA.
DR   AlphaFoldDB; Q7T3L1; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; NAS:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IDA:UniProtKB.
DR   GO; GO:0042755; P:eating behavior; IDA:UniProtKB.
DR   GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
DR   InterPro; IPR009608; Bradykinin.
DR   Pfam; PF06753; Bradykinin; 8.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond;
KW   G-protein coupled receptor impairing toxin; Repeat; Secreted; Signal;
KW   Toxin; Vasoactive; Vasodilator.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..294
FT                   /note="Kininogen-1a"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003385"
FT   PEPTIDE         41..59
FT                   /note="Maximakinin"
FT                   /evidence="ECO:0000250|UniProtKB:Q90W88"
FT                   /id="PRO_0000003386"
FT   PEPTIDE         51..66
FT                   /note="Bradykinin"
FT                   /evidence="ECO:0000250|UniProtKB:Q90W88"
FT                   /id="PRO_0000003387"
FT   PEPTIDE         69..87
FT                   /note="Maximakinin"
FT                   /evidence="ECO:0000250|UniProtKB:Q90W88"
FT                   /id="PRO_0000003388"
FT   PEPTIDE         79..94
FT                   /note="Bradykinin"
FT                   /evidence="ECO:0000250|UniProtKB:Q90W88"
FT                   /id="PRO_0000003389"
FT   PEPTIDE         97..115
FT                   /note="Maximakinin"
FT                   /evidence="ECO:0000250|UniProtKB:Q90W88"
FT                   /id="PRO_0000003390"
FT   PEPTIDE         107..122
FT                   /note="Bradykinin"
FT                   /evidence="ECO:0000250|UniProtKB:Q90W88"
FT                   /id="PRO_0000003391"
FT   PEPTIDE         125..143
FT                   /note="Maximakinin"
FT                   /evidence="ECO:0000250|UniProtKB:Q90W88"
FT                   /id="PRO_0000003392"
FT   PEPTIDE         135..150
FT                   /note="Bradykinin"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000003393"
FT   PEPTIDE         153..171
FT                   /note="Maximakinin"
FT                   /evidence="ECO:0000250|UniProtKB:Q90W88"
FT                   /id="PRO_0000003394"
FT   PEPTIDE         163..178
FT                   /note="Bradykinin"
FT                   /evidence="ECO:0000250|UniProtKB:Q90W88"
FT                   /id="PRO_0000003395"
FT   PEPTIDE         181..199
FT                   /note="Maximakinin"
FT                   /evidence="ECO:0000250|UniProtKB:Q90W88"
FT                   /id="PRO_0000003396"
FT   PEPTIDE         191..206
FT                   /note="Bradykinin"
FT                   /evidence="ECO:0000250|UniProtKB:Q90W88"
FT                   /id="PRO_0000003397"
FT   PEPTIDE         209..227
FT                   /note="Maximakinin"
FT                   /evidence="ECO:0000250|UniProtKB:Q90W88"
FT                   /id="PRO_0000003398"
FT   PEPTIDE         219..234
FT                   /note="Bradykinin"
FT                   /evidence="ECO:0000250|UniProtKB:Q90W88"
FT                   /id="PRO_0000003399"
FT   PEPTIDE         237..255
FT                   /note="Maximakinin"
FT                   /evidence="ECO:0000250|UniProtKB:Q90W88"
FT                   /id="PRO_0000003400"
FT   PEPTIDE         247..262
FT                   /note="Bradykinin"
FT                   /evidence="ECO:0000250|UniProtKB:Q90W88"
FT                   /id="PRO_0000003401"
FT   PEPTIDE         265..292
FT                   /note="Bombinakinin-GAP"
FT                   /evidence="ECO:0000269|PubMed:12668203"
FT                   /id="PRO_0000003402"
FT   REGION          28..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          238..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         292
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:12668203"
FT   DISULFID        282..288
FT                   /evidence="ECO:0000269|PubMed:12668203"
SQ   SEQUENCE   294 AA;  33857 MW;  7C87B4D88482C530 CRC64;
     MRLWFCLSFF IVLCLEHFTG TLADERNVPE SEEKTEQFLR DLPKINRKGP RPPGFSPFRG
     KFHSQSLRDL PKINRKGPRP PGFSPFRGKF HSQSLRDLPK INRKGPRPPG FSPFRGKFHS
     QSLRDLPKIN RKGPRPPGFS PFRGKFHSQS LRDLPKINRK GPRPPGFSPF RGKFHSQSLR
     DLPKINRKGP RPPGFSPFRG KFHSQSLRDL PKINRKGPRP PGFSPFRGKF HSQSLRDLPK
     INRKGPRPPG FSPFRGKFHS QSLRDMYEIK QYKTAHGRPP ICAPGEQCPI WVGK
 
 
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