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Neuroendocrine protein 7B2 (Secretogranin V) [Cleaved into: N-terminal peptide; C-terminal peptide] (Fragment)

 7B2_XENLA               Reviewed;         161 AA.
P18844;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
06-JUL-2016, entry version 61.
RecName: Full=Neuroendocrine protein 7B2;
AltName: Full=Secretogranin V;
Contains:
RecName: Full=N-terminal peptide;
Contains:
RecName: Full=C-terminal peptide;
Flags: Fragment;
Name=sgne1;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2714283; DOI=10.1111/j.1432-1033.1989.tb14695.x;
Martens G.J.M., Bussemakers M.J.G., Ayoubi T.A.Y., Jenks B.G.;
"The novel pituitary polypeptide 7B2 is a highly-conserved protein
coexpressed with proopiomelanocortin.";
Eur. J. Biochem. 181:75-79(1989).
[2]
PROTEOLYTIC PROCESSING.
PubMed=2394742;
Ayoubi T.A.Y., van Duijnhoven H.L.P., van de Ven W.J.M., Jenks B.G.,
Roubos E.W., Martens G.J.M.;
"The neuroendocrine polypeptide 7B2 is a precursor protein.";
J. Biol. Chem. 265:15644-15647(1990).
[3]
DISULFIDE BOND.
PubMed=9648890;
Van Horssen A.M., Van Kuppeveld F.J.M., Martens G.J.M.;
"Manipulation of disulfide bonds differentially affects the
intracellular transport, sorting, and processing of neuroendocrine
secretory proteins.";
J. Neurochem. 71:402-409(1998).
[4]
REVIEW.
PubMed=11439082; DOI=10.1042/0264-6021:3570329;
Mbikay M., Seidah N.G., Chretien M.;
"Neuroendocrine secretory protein 7B2: structure, expression and
functions.";
Biochem. J. 357:329-342(2001).
-!- FUNCTION: Acts as a molecular chaperone for pcsk2, preventing its
premature activation in the regulated secretory pathway. Binds to
inactive pcsk2 in the endoplasmic reticulum and facilitates its
transport from there to later compartments of the secretory
pathway where it is proteolytically matured and activated. Also
required for cleavage of pcsk2 but does not appear to be involved
in its folding (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with pcsk2 early in the secretory pathway.
Dissociation occurs at later stages (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine
secretory granules.
-!- PTM: Proteolytically cleaved in the Golgi by a furin-like
convertase to generate bioactive peptides. {ECO:0000250}.
-!- PTM: Sulfated on tyrosine residues. {ECO:0000250}.
-!- SIMILARITY: Belongs to the 7B2 family. {ECO:0000305}.
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EMBL; X15608; CAA33631.1; -; mRNA.
PIR; S03938; S03938.
UniGene; Xl.47184; -.
MEROPS; I21.001; -.
HOVERGEN; HBG000031; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
GO; GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
GO; GO:0016486; P:peptide hormone processing; ISS:UniProtKB.
GO; GO:0046883; P:regulation of hormone secretion; ISS:UniProtKB.
InterPro; IPR007945; Secretogranin_V.
PANTHER; PTHR12738; PTHR12738; 1.
Pfam; PF05281; Secretogranin_V; 1.
1: Evidence at protein level;
Chaperone; Cleavage on pair of basic residues; Disulfide bond;
Neuropeptide; Phosphoprotein; Secreted; Sulfation; Transport.
CHAIN <1 161 Neuroendocrine protein 7B2.
/FTId=PRO_0000045862.
CHAIN <1 128 N-terminal peptide. {ECO:0000250}.
/FTId=PRO_0000000053.
PEPTIDE 152 161 C-terminal peptide. {ECO:0000250}.
/FTId=PRO_0000000054.
MOD_RES 157 157 Phosphoserine. {ECO:0000250}.
DISULFID 73 82 {ECO:0000269|PubMed:9648890}.
NON_TER 1 1
SEQUENCE 161 AA; 17992 MW; A6E32531A29D82FC CRC64;
MEELGIARPR VEYPAHQAMN LVGPQSIEGG AHEGLQHLGP YGNIPNIVAE LTGDNIPKDF
REDQGYPNPP NPCPVGKTGD GCLEDTPDTA QFSREYQLHQ NLYDPEHNYP GASTWNKKLL
YEKIKGASQR QKRTVNPYLQ GQKLDKVVAK KSVPHFSDEE E


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