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VNP32_MICCO
ID   VNP32_MICCO             Reviewed;         139 AA.
AC   P79799;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Natriuretic peptide Mc-NP;
DE   AltName: Full=Micrurus natriuretic peptide;
DE            Short=MNP;
DE   AltName: Full=Putative natriuretic peptide 3A32;
DE   Flags: Precursor;
OS   Micrurus corallinus (Brazilian coral snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Micrurus.
OX   NCBI_TaxID=54390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Ho P.L., Soares M.B., Yamane T., Raw I.A.;
RT   "Reverse biology applied to Micrurus corallinus, a South American coral
RT   snake.";
RL   J. Toxicol. Toxin Rev. 14:327-337(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom gland;
RX   PubMed=9432002; DOI=10.1111/j.1432-1033.1997.00144.x;
RA   Ho P.L., Soares M.B., Maack T., Gimenez I., Puorto G., Furtado M.F.D.,
RA   Raw I.A.;
RT   "Cloning of an unusual natriuretic peptide from the South American coral
RT   snake Micrurus corallinus.";
RL   Eur. J. Biochem. 250:144-149(1997).
CC   -!- FUNCTION: Snake venom natriuretic peptide that exhibits hypotensive and
CC       vasodepressor activity. Acts by activating natriuretic receptors (NPR1
CC       and/or NPR2 and/or NPR3) (By similarity). A synthetic peptide (AA 77-
CC       108, where the Cys-95 is replaced by a Ser) increases sodium excretion
CC       and urinary volume in rat kidneys. {ECO:0000250,
CC       ECO:0000269|PubMed:9432002}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:9432002}.
CC   -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR   EMBL; U77596; AAC60341.1; -; mRNA.
DR   AlphaFoldDB; P79799; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
DR   GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
DR   InterPro; IPR002406; C_natriurtcpep.
DR   InterPro; IPR000663; Natr_peptide.
DR   InterPro; IPR030480; Natr_peptide_CS.
DR   Pfam; PF00212; ANP; 1.
DR   PRINTS; PR00713; CNATPEPTIDE.
DR   SMART; SM00183; NAT_PEP; 1.
DR   PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hypotensive agent; Secreted; Signal; Toxin; Vasoactive;
KW   Vasodilator.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..75
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000335923"
FT   PEPTIDE         76..116
FT                   /note="Natriuretic peptide Mc-NP"
FT                   /id="PRO_0000335924"
FT   PROPEP          117..139
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000335925"
FT   REGION          45..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        86..102
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   139 AA;  14881 MW;  4262B7771870E1FB CRC64;
     MVGLSRLRGG GLLLVLALLP LALDGKPLEE APTAPSRIIP FSRPVRKQSQ AVLDPMVHPE
     RPAGSGDDGD SRRLEGLAKE ALGDGCFGQR IDRICNVSGM GCNHVRTDPA PTALARIIPF
     SRPVRKESRA ALDRMQQPG
 
 
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