ID   7B2_PANTR               Reviewed;         211 AA.
AC   A5A6J6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Neuroendocrine protein 7B2;
DE   AltName: Full=Secretogranin-5;
DE   Contains:
DE     RecName: Full=N-terminal peptide;
DE   Contains:
DE     RecName: Full=C-terminal peptide;
DE   Flags: Precursor;
GN   Name=SCG5;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA   Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA   Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT   "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT   large potential divergence of the transcriptome.";
RL   Gene 399:1-10(2007).
CC   -!- FUNCTION: Acts as a molecular chaperone for PCSK2/PC2, 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.
CC       Plays a role in regulating pituitary hormone secretion. The C-terminal
CC       peptide inhibits PCSK2 in vitro (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with PCSK2/PC2 early in the secretory pathway.
CC       Dissociation occurs at later stages (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Neuroendocrine and
CC       endocrine secretory granules. {ECO:0000250}.
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; AB222124; BAF62369.1; -; mRNA.
DR   RefSeq; NP_001092019.1; NM_001098549.1.
DR   AlphaFoldDB; A5A6J6; -.
DR   STRING; 9598.ENSPTRP00000055998; -.
DR   MEROPS; I21.001; -.
DR   PaxDb; A5A6J6; -.
DR   PRIDE; A5A6J6; -.
DR   GeneID; 453292; -.
DR   KEGG; ptr:453292; -.
DR   CTD; 6447; -.
DR   eggNOG; KOG4187; Eukaryota.
DR   HOGENOM; CLU_113154_0_0_1; -.
DR   InParanoid; A5A6J6; -.
DR   OrthoDB; 1534994at2759; -.
DR   TreeFam; TF314328; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030141; C:secretory granule; IEA:InterPro.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR007945; Secretogranin_V.
DR   PANTHER; PTHR12738; PTHR12738; 1.
DR   Pfam; PF05281; Secretogranin_V; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Cleavage on pair of basic residues; Disulfide bond;
KW   Neuropeptide; Phosphoprotein; Reference proteome; Secreted; Signal;
KW   Sulfation; Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250"
FT   CHAIN           27..211
FT                   /note="Neuroendocrine protein 7B2"
FT                   /id="PRO_0000296644"
FT   CHAIN           27..175
FT                   /note="N-terminal peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000296645"
FT   PEPTIDE         199..211
FT                   /note="C-terminal peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000296646"
FT   REGION          106..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12961"
FT   MOD_RES         204
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12961"
FT   DISULFID        120..129
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   211 AA;  23659 MW;  649AA3FF2EC2A0A6 CRC64;
     MVSRMVSTML SGLLFWLASG WTPAFAYSPR TPDRVSEADI QRLLHGVMEQ LGIARPRVEY
     PAHQAMNLVG PQSIEGGAHE GLQHLGPFGN IPNIVAELTG DNIPKDFSED QGYPDPPNPC
     PVGKTDDGCL ENTPDTAEFS REFQLHQHLF DPEHDYPGLG KWNKKLLYEK MKGGERRKRR
     SVNPYLQGQR LDNVVAKKSV PHFSDEDKDP E