ID   7B2_XENLA               Reviewed;         161 AA.
AC   P18844;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Neuroendocrine protein 7B2;
DE   AltName: Full=Secretogranin V;
DE   Contains:
DE     RecName: Full=N-terminal peptide;
DE   Contains:
DE     RecName: Full=C-terminal peptide;
DE   Flags: Fragment;
GN   Name=sgne1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2714283; DOI=10.1111/j.1432-1033.1989.tb14695.x;
RA   Martens G.J.M., Bussemakers M.J.G., Ayoubi T.A.Y., Jenks B.G.;
RT   "The novel pituitary polypeptide 7B2 is a highly-conserved protein
RT   coexpressed with proopiomelanocortin.";
RL   Eur. J. Biochem. 181:75-79(1989).
RN   [2]
RP   PROTEOLYTIC PROCESSING.
RX   PubMed=2394742; DOI=10.1016/s0021-9258(18)55446-6;
RA   Ayoubi T.A.Y., van Duijnhoven H.L.P., van de Ven W.J.M., Jenks B.G.,
RA   Roubos E.W., Martens G.J.M.;
RT   "The neuroendocrine polypeptide 7B2 is a precursor protein.";
RL   J. Biol. Chem. 265:15644-15647(1990).
RN   [3]
RP   DISULFIDE BOND.
RX   PubMed=9648890; DOI=10.1046/j.1471-4159.1998.71010402.x;
RA   Van Horssen A.M., Van Kuppeveld F.J.M., Martens G.J.M.;
RT   "Manipulation of disulfide bonds differentially affects the intracellular
RT   transport, sorting, and processing of neuroendocrine secretory proteins.";
RL   J. Neurochem. 71:402-409(1998).
RN   [4]
RP   REVIEW.
RX   PubMed=11439082; DOI=10.1042/0264-6021:3570329;
RA   Mbikay M., Seidah N.G., Chretien M.;
RT   "Neuroendocrine secretory protein 7B2: structure, expression and
RT   functions.";
RL   Biochem. J. 357:329-342(2001).
CC   -!- FUNCTION: Acts as a molecular chaperone for pcsk2, preventing its
CC       premature activation in the regulated secretory pathway. Binds to
CC       inactive pcsk2 in the endoplasmic reticulum and facilitates its
CC       transport from there to later compartments of the secretory pathway
CC       where it is proteolytically matured and activated. Also required for
CC       cleavage of pcsk2 but does not appear to be involved in its folding (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with pcsk2 early in the secretory pathway.
CC       Dissociation occurs at later stages (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine
CC       secretory granules.
CC   -!- PTM: Proteolytically cleaved in the Golgi by a furin-like convertase to
CC       generate bioactive peptides. {ECO:0000250}.
CC   -!- PTM: Sulfated on tyrosine residues. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 7B2 family. {ECO:0000305}.
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DR   EMBL; X15608; CAA33631.1; -; mRNA.
DR   PIR; S03938; S03938.
DR   AlphaFoldDB; P18844; -.
DR   MEROPS; I21.001; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
DR   GO; GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0016486; P:peptide hormone processing; ISS:UniProtKB.
DR   GO; GO:0046883; P:regulation of hormone secretion; ISS:UniProtKB.
DR   InterPro; IPR007945; Secretogranin_V.
DR   PANTHER; PTHR12738; PTHR12738; 1.
DR   Pfam; PF05281; Secretogranin_V; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Cleavage on pair of basic residues; Disulfide bond;
KW   Neuropeptide; Phosphoprotein; Reference proteome; Secreted; Sulfation;
KW   Transport.
FT   CHAIN           <1..161
FT                   /note="Neuroendocrine protein 7B2"
FT                   /id="PRO_0000045862"
FT   CHAIN           <1..128
FT                   /note="N-terminal peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000000053"
FT   PEPTIDE         152..161
FT                   /note="C-terminal peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000000054"
FT   REGION          56..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         157
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..82
FT                   /evidence="ECO:0000269|PubMed:9648890"
FT   NON_TER         1
SQ   SEQUENCE   161 AA;  17992 MW;  A6E32531A29D82FC CRC64;
     MEELGIARPR VEYPAHQAMN LVGPQSIEGG AHEGLQHLGP YGNIPNIVAE LTGDNIPKDF
     REDQGYPNPP NPCPVGKTGD GCLEDTPDTA QFSREYQLHQ NLYDPEHNYP GASTWNKKLL
     YEKIKGASQR QKRTVNPYLQ GQKLDKVVAK KSVPHFSDEE E