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ANFC_PIG
ID   ANFC_PIG                Reviewed;         126 AA.
AC   P18104; P21806;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=C-type natriuretic peptide;
DE   Contains:
DE     RecName: Full=CNP-22;
DE   Contains:
DE     RecName: Full=CNP-29;
DE   Contains:
DE     RecName: Full=CNP-53;
DE   Flags: Precursor;
GN   Name=NPPC; Synonyms=CNP;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2146957; DOI=10.1016/0006-291x(90)90720-8;
RA   Tawaragi Y., Fuchimura K., Nakazato H., Tanaka S., Minamino N., Kangawa K.,
RA   Matsuo H.;
RT   "Gene and precursor structure of porcine C-type natriuretic peptide.";
RL   Biochem. Biophys. Res. Commun. 172:627-632(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 74-126.
RC   TISSUE=Brain;
RX   PubMed=2383278; DOI=10.1016/0006-291x(90)92187-5;
RA   Minamino N., Kangawa K., Matsuo H.;
RT   "N-terminally extended form of C-type natriuretic peptide (CNP-53)
RT   identified in porcine brain.";
RL   Biochem. Biophys. Res. Commun. 170:973-979(1990).
RN   [3]
RP   PROTEIN SEQUENCE OF 105-126.
RC   TISSUE=Brain;
RX   PubMed=2139780; DOI=10.1016/0006-291x(90)92401-k;
RA   Sudoh T., Minamino N., Kangawa K., Matsuo H.;
RT   "C-type natriuretic peptide (CNP): a new member of natriuretic peptide
RT   family identified in porcine brain.";
RL   Biochem. Biophys. Res. Commun. 168:863-870(1990).
CC   -!- FUNCTION: [CNP-22]: Hormone which plays a role in endochondral
CC       ossification through regulation of cartilaginous growth plate
CC       chondrocytes proliferation and differentiation (By similarity). May
CC       also be vasoactive and natriuretic. Acts by specifically binding and
CC       stimulating NPR2 to produce cGMP. Binds the clearance receptor NPR3 (By
CC       similarity). {ECO:0000250|UniProtKB:P23582,
CC       ECO:0000250|UniProtKB:Q61839}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: [CNP-22]: Degraded by IDE (in vitro).
CC       {ECO:0000250|UniProtKB:P23582}.
CC   -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR   EMBL; M64758; AAA31018.1; -; Genomic_DNA.
DR   PIR; A36155; A36155.
DR   RefSeq; NP_001008482.1; NM_001008482.1.
DR   RefSeq; XP_005672336.1; XM_005672279.1.
DR   AlphaFoldDB; P18104; -.
DR   STRING; 9823.ENSSSCP00000022217; -.
DR   PaxDb; P18104; -.
DR   Ensembl; ENSSSCT00000028969; ENSSSCP00000022217; ENSSSCG00000026852.
DR   Ensembl; ENSSSCT00005058520; ENSSSCP00005036131; ENSSSCG00005036665.
DR   Ensembl; ENSSSCT00005058551; ENSSSCP00005036158; ENSSSCG00005036665.
DR   Ensembl; ENSSSCT00015018952; ENSSSCP00015007436; ENSSSCG00015014287.
DR   Ensembl; ENSSSCT00025005802; ENSSSCP00025002310; ENSSSCG00025004345.
DR   Ensembl; ENSSSCT00030057887; ENSSSCP00030026352; ENSSSCG00030041644.
DR   Ensembl; ENSSSCT00035094585; ENSSSCP00035039727; ENSSSCG00035070028.
DR   Ensembl; ENSSSCT00040058920; ENSSSCP00040024672; ENSSSCG00040043932.
DR   Ensembl; ENSSSCT00045010609; ENSSSCP00045007227; ENSSSCG00045006394.
DR   Ensembl; ENSSSCT00050040183; ENSSSCP00050016630; ENSSSCG00050029879.
DR   Ensembl; ENSSSCT00055042421; ENSSSCP00055033776; ENSSSCG00055021594.
DR   Ensembl; ENSSSCT00060063698; ENSSSCP00060027337; ENSSSCG00060046901.
DR   Ensembl; ENSSSCT00065085310; ENSSSCP00065037277; ENSSSCG00065062196.
DR   Ensembl; ENSSSCT00070017167; ENSSSCP00070014204; ENSSSCG00070008864.
DR   GeneID; 493772; -.
DR   KEGG; ssc:493772; -.
DR   CTD; 4880; -.
DR   VGNC; VGNC:96450; NPPC.
DR   eggNOG; ENOG502S2QY; Eukaryota.
DR   GeneTree; ENSGT00390000015492; -.
DR   HOGENOM; CLU_160791_0_0_1; -.
DR   InParanoid; P18104; -.
DR   OMA; HDYPNAR; -.
DR   OrthoDB; 1491136at2759; -.
DR   TreeFam; TF106305; -.
DR   Reactome; R-SSC-5578768; Physiological factors.
DR   Proteomes; UP000008227; Chromosome 15.
DR   Proteomes; UP000314985; Chromosome 15.
DR   Bgee; ENSSSCG00000026852; Expressed in endocardial endothelium and 16 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR   GO; GO:0051427; F:hormone receptor binding; IBA:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; ISS:AgBase.
DR   GO; GO:0006182; P:cGMP biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0003418; P:growth plate cartilage chondrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0003419; P:growth plate cartilage chondrocyte proliferation; ISS:UniProtKB.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:Ensembl.
DR   GO; GO:0051447; P:negative regulation of meiotic cell cycle; IEA:Ensembl.
DR   GO; GO:1900194; P:negative regulation of oocyte maturation; IEA:Ensembl.
DR   GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:0006457; P:protein folding; IEA:Ensembl.
DR   GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; ISS:UniProtKB.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
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; Osteogenesis; Reference proteome; Secreted;
KW   Signal; Vasoactive.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..73
FT                   /evidence="ECO:0000269|PubMed:2383278"
FT                   /id="PRO_0000001561"
FT   PEPTIDE         74..126
FT                   /note="CNP-53"
FT                   /id="PRO_0000001562"
FT   PEPTIDE         98..126
FT                   /note="CNP-29"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000001563"
FT   PEPTIDE         105..126
FT                   /note="CNP-22"
FT                   /id="PRO_0000001564"
FT   REGION          19..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        110..126
SQ   SEQUENCE   126 AA;  13243 MW;  E2474B2D4AABF4DD CRC64;
     MHLSQLLACA LLLTLLSLRP SEAKPGAPPK VPRTPPGEEV AEPQAAGGGQ KKGDKTPGGG
     GANLKGDRSR LLRDLRVDTK SRAAWARLLH EHPNARKYKG GNKKGLSKGC FGLKLDRIGS
     MSGLGC
 
 
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