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ANFC_SCYCA
ID   ANFC_SCYCA              Reviewed;         115 AA.
AC   P23259;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=C-type natriuretic peptide prohormone;
DE   AltName: Full=CNP-115;
DE   Contains:
DE     RecName: Full=CNP-39;
DE   Contains:
DE     RecName: Full=CNP-38;
DE   Contains:
DE     RecName: Full=CNP-22;
DE   Flags: Precursor;
OS   Scyliorhinus canicula (Small-spotted catshark) (Squalus canicula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC   Scyliorhinus.
OX   NCBI_TaxID=7830;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Heart atrium, and Heart ventricle;
RX   PubMed=1828036; DOI=10.1016/0014-5793(91)80505-w;
RA   Suzuki R., Takahashi A., Hazon N., Takei Y.;
RT   "Isolation of high-molecular-weight C-type natriuretic peptide from the
RT   heart of a cartilaginous fish (European dogfish, Scyliorhinus canicula).";
RL   FEBS Lett. 282:321-325(1991).
CC   -!- FUNCTION: Hormone which may be vasoactive and natriuretic. Has a cGMP-
CC       stimulating activity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: CNP-115 is differentially processed to produce CNP-
CC       38 and CNP-39 in the heart and CNP-22 in the brain.
CC   -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR   PIR; S15822; S15822.
DR   AlphaFoldDB; P23259; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0006182; P:cGMP biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; ISS:UniProtKB.
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   PRINTS; PR00710; NATPEPTIDES.
DR   SMART; SM00183; NAT_PEP; 1.
DR   PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Hormone; Secreted; Vasoactive.
FT   CHAIN           1..115
FT                   /note="C-type natriuretic peptide prohormone"
FT                   /id="PRO_0000001603"
FT   PEPTIDE         77..115
FT                   /note="CNP-39"
FT                   /id="PRO_0000001604"
FT   PEPTIDE         78..115
FT                   /note="CNP-38"
FT                   /id="PRO_0000001605"
FT   PEPTIDE         94..115
FT                   /note="CNP-22"
FT                   /id="PRO_0000001606"
FT   REGION          24..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        99..115
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   115 AA;  12885 MW;  49AE7200EE4C7F8A CRC64;
     RPRSDDSLQT LSRLLEDEYG HYLPSDELNN EAEEMSPAAS LPELNADQSD LELPWERESR
     EIGGRPFRQE AVLARLLKDL SNNPLRFRGR SKKGPSRGCF GVKLDRIGAM SGLGC
 
 
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