7B2_PIG
ID 7B2_PIG Reviewed; 207 AA.
AC P01165;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 25-MAY-2022, entry version 88.
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 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 [MRNA].
RX PubMed=3234177; DOI=10.1089/dna.1988.7.713;
RA Brayton K.A., Aimi J., Qiu H., Yazdanparast R., Ghatei M.A., Polak J.M.,
RA Bloom S.R., Dixon J.E.;
RT "Cloning, characterization, and sequence of a porcine cDNA encoding a
RT secreted neuronal and endocrine protein.";
RL DNA 7:713-719(1988).
RN [2]
RP PROTEIN SEQUENCE OF 23-171.
RC TISSUE=Pituitary;
RX PubMed=1797712; DOI=10.1111/j.1399-3011.1991.tb01519.x;
RA Lazure C., Benjannet S., Seidah N.G., Chretien M.;
RT "Processed forms of neuroendocrine proteins 7B2 and secretogranin II are
RT found in porcine pituitary extracts.";
RL Int. J. Pept. Protein Res. 38:392-400(1991).
RN [3]
RP PROTEIN SEQUENCE OF 23-103.
RX PubMed=6625600; DOI=10.1016/0003-9861(83)90063-2;
RA Seidah N.G., Hsi K.L., de Serres G., Rochemont J., Hamelin J., Antakly T.,
RA Cantin M., Chretien M.;
RT "Isolation and NH2-terminal sequence of a highly conserved human and
RT porcine pituitary protein belonging to a new superfamily.
RT Immunocytochemical localization in pars distalis and pars nervosa of the
RT pituitary and in the supraoptic nucleus of the hypothalamus.";
RL Arch. Biochem. Biophys. 225:525-534(1983).
RN [4]
RP PROTEIN SEQUENCE OF 23-72.
RX PubMed=6816630; DOI=10.1016/0014-5793(82)81055-7;
RA Hsi K.L., Seidah N.G., de Serres G., Chretien M.;
RT "Isolation and NH2-terminal sequence of a novel porcine anterior pituitary
RT polypeptide. Homology to proinsulin, secretin and Rous sarcoma virus
RT transforming protein TVFV60.";
RL FEBS Lett. 147:261-266(1982).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=6514132; DOI=10.1159/000124020;
RA Iguchi H., Chan J.S., Seidah N.G., Chretien M.;
RT "Tissue distribution and molecular forms of a novel pituitary protein in
RT the rat.";
RL Neuroendocrinology 39:453-458(1984).
RN [6]
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/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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6514132}.
CC Note=Neuroendocrine and endocrine 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; M23654; AAA50416.1; -; mRNA.
DR PIR; A31600; PUPG.
DR AlphaFoldDB; P01165; -.
DR SMR; P01165; -.
DR STRING; 9823.ENSSSCP00000005176; -.
DR MEROPS; I21.001; -.
DR PaxDb; P01165; -.
DR PeptideAtlas; P01165; -.
DR PRIDE; P01165; -.
DR eggNOG; KOG4187; Eukaryota.
DR InParanoid; P01165; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; IDA: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; Direct protein sequencing;
KW Disulfide bond; Neuropeptide; Phosphoprotein; Reference proteome; Secreted;
KW Signal; Sulfation; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:1797712,
FT ECO:0000269|PubMed:6625600, ECO:0000269|PubMed:6816630"
FT CHAIN 23..207
FT /note="Neuroendocrine protein 7B2"
FT /id="PRO_0000000047"
FT CHAIN 23..171
FT /note="N-terminal peptide"
FT /id="PRO_0000000048"
FT PEPTIDE 195..207
FT /note="C-terminal peptide"
FT /id="PRO_0000000049"
FT REGION 168..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12961"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12961"
FT DISULFID 116..125
FT /evidence="ECO:0000250"
SQ SEQUENCE 207 AA; 23224 MW; 20077D0E1EB6D0AC CRC64;
MVSTMLSGLV LWLTFGWTPA LAYSPRTPDR VSETDIQRLL HGVMEQLGIA RPRVEYPAHQ
AMNLVGPQSI EGGAHEGLQH LGPFGNIPNI VAELTGDNTP KDFSEDQGYP DPPNPCPIGK
TDDGCLENTP DTAEFSREFQ LHQHLFDPEH DYPGLGKWNK KLLYEKMKGG QRRKRRSVNP
YLQGQRLDNV VAKKSVPHFS DEDKDPE
