7B2_RAT
ID 7B2_RAT Reviewed; 210 AA.
AC P27682;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Neuroendocrine protein 7B2;
DE AltName: Full=Secretogranin V;
DE AltName: Full=Secretogranin-5;
DE AltName: Full=Secretory granule endocrine protein I;
DE Contains:
DE RecName: Full=N-terminal peptide;
DE Contains:
DE RecName: Full=C-terminal peptide;
DE Flags: Precursor;
GN Name=Scg5; Synonyms=Sgne1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1709861; DOI=10.1210/endo-128-6-3228;
RA Waldbieser G.C., Aimi J., Dixon J.E.;
RT "Cloning and characterization of the rat complementary deoxyribonucleic
RT acid and gene encoding the neuroendocrine peptide 7B2.";
RL Endocrinology 128:3228-3236(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary anterior lobe;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
CC -!- SUBUNIT: Interacts with PCSK2/PC2 early in the secretory pathway.
CC Dissociation occurs at later stages (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P27682; P28841: Pcsk2; NbExp=4; IntAct=EBI-988232, EBI-988244;
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; M63901; AAA40626.1; -; mRNA.
DR EMBL; BC061560; AAH61560.1; -; mRNA.
DR PIR; A49745; A49745.
DR RefSeq; NP_037307.1; NM_013175.3.
DR AlphaFoldDB; P27682; -.
DR BioGRID; 247748; 1.
DR IntAct; P27682; 1.
DR STRING; 10116.ENSRNOP00000010679; -.
DR MEROPS; I21.001; -.
DR iPTMnet; P27682; -.
DR PhosphoSitePlus; P27682; -.
DR jPOST; P27682; -.
DR PaxDb; P27682; -.
DR PRIDE; P27682; -.
DR GeneID; 25719; -.
DR KEGG; rno:25719; -.
DR UCSC; RGD:3669; rat.
DR CTD; 6447; -.
DR RGD; 3669; Scg5.
DR eggNOG; KOG4187; Eukaryota.
DR InParanoid; P27682; -.
DR OrthoDB; 1534994at2759; -.
DR PhylomeDB; P27682; -.
DR PRO; PR:P27682; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
DR GO; GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
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 DisProt; DP01557; -.
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; Signal;
KW Sulfation; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..210
FT /note="Neuroendocrine protein 7B2"
FT /id="PRO_0000000050"
FT CHAIN 25..176
FT /note="N-terminal peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000051"
FT PEPTIDE 198..210
FT /note="C-terminal peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000052"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12961"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT DISULFID 118..128
FT /evidence="ECO:0000250"
SQ SEQUENCE 210 AA; 23684 MW; 14FBA7D070E79992 CRC64;
MTSRMAILSG LLFWLLLEWN PAFAYSPRTP DRVSETDIQR LLHGVMEQLG IARPRVEYPA
HQAMNLVGPQ SIEGGAHEGL QHLGPFGNIP NIVAELTGDN IPKDFSEDQG YPDPPNPCPL
GKTADDGCLE NAPDTAEFSR EFQLDQHLFD PEHDYPGLGK WNKKLLYEKM KGGQRRKRRS
VNPYLQGKRL DNVVAKKSVP HFSEEEKEPE
