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Neuroendocrine protein 7B2 (Secretogranin V) (Secretogranin-5) (Secretory granule endocrine protein I) [Cleaved into: N-terminal peptide; C-terminal peptide]

 7B2_MOUSE               Reviewed;         212 AA.
P12961; Q8CCZ3; Q9CYP0; Q9D2P6; Q9DB14;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
07-JUN-2017, entry version 136.
RecName: Full=Neuroendocrine protein 7B2;
AltName: Full=Secretogranin V;
AltName: Full=Secretogranin-5;
AltName: Full=Secretory granule endocrine protein I;
Contains:
RecName: Full=N-terminal peptide;
Contains:
RecName: Full=C-terminal peptide;
Flags: Precursor;
Name=Scg5; Synonyms=Sgne-1, Sgne1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=BALB/cJ; TISSUE=Pancreas;
PubMed=2542174;
Mbikay M., Grant S.G.N., Sirois F., Tadros H., Skowronski J.,
Lazure C., Seidah N.G., Hanahan D., Chretien M.;
"cDNA sequence of neuroendocrine protein 7B2 expressed in beta cell
tumors of transgenic mice.";
Int. J. Pept. Protein Res. 33:39-45(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Cerebellum, Embryo, Hippocampus, and Medulla oblongata;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Retina;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9348280; DOI=10.1083/jcb.139.3.625;
Muller L., Zhu X., Lindberg I.;
"Mechanism of the facilitation of PC2 maturation by 7B2: involvement
in ProPC2 transport and activation but not folding.";
J. Cell Biol. 139:625-638(1997).
[5]
FUNCTION.
PubMed=10089884; DOI=10.1016/S0092-8674(00)80579-6;
Westphal C.H., Muller L., Zhou A., Zhu X., Bonner-Weir S.,
Schambelan M., Steiner D.F., Lindberg I., Leder P.;
"The neuroendocrine protein 7B2 is required for peptide hormone
processing in vivo and provides a novel mechanism for pituitary
Cushing's disease.";
Cell 96:689-700(1999).
[6]
INHIBITION OF PCSK2 BY C-TERMINAL PEPTIDE.
PubMed=8016065; DOI=10.1073/pnas.91.13.5784;
Martens G.J.M., Braks J.A., Eib D.W., Zhou Y., Lindberg I.;
"The neuroendocrine polypeptide 7B2 is an endogenous inhibitor of
prohormone convertase PC2.";
Proc. Natl. Acad. Sci. U.S.A. 91:5784-5787(1994).
[7]
SULFATION, CLEAVAGE BY FURIN-LIKE CONVERTASE, AND MUTAGENESIS OF
ARG-177 AND ARG-178.
PubMed=8034690;
Paquet L., Bergeron F., Boudreault A., Seidah N.G., Chretien M.,
Mbikay M., Lazure C.;
"The neuroendocrine precursor 7B2 is a sulfated protein
proteolytically processed by a ubiquitous furin-like convertase.";
J. Biol. Chem. 269:19279-19285(1994).
[8]
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-205, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Acts as a molecular chaperone for PCSK2/PC2, 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. Plays a role in regulating pituitary hormone
secretion. The C-terminal peptide inhibits PCSK2 in vitro.
{ECO:0000269|PubMed:10089884, ECO:0000269|PubMed:9348280}.
-!- SUBUNIT: Interacts with PCSK2/PC2 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:0000269|PubMed:8034690}.
-!- PTM: Sulfated on tyrosine residues. {ECO:0000269|PubMed:8034690}.
-!- DISRUPTION PHENOTYPE: Mice have no demonstrable Pcsk2/Pc2
activity, are deficient in processing islet hormones, and display
hypoglycemia, hyperproinsulinemia and hypoglucagonemia, similar to
Pcsk2 null mice. In contrast to Pcsk2 null mice, they develop
Cushing's disease due to excessive secretion of corticotropin from
the pituitary and die before 9 weeks, indicating a role for Sgne1
in control of peptide secretion from the pituitary.
{ECO:0000269|PubMed:9348280}.
-!- SIMILARITY: Belongs to the 7B2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X15830; CAA33835.1; -; mRNA.
EMBL; AK005331; BAB23956.1; -; mRNA.
EMBL; AK011938; BAB27927.1; -; mRNA.
EMBL; AK017481; BAB30765.1; -; mRNA.
EMBL; AK019337; BAB31669.1; -; mRNA.
EMBL; AK031856; BAC27581.1; -; mRNA.
EMBL; BC029021; AAH29021.1; -; mRNA.
CCDS; CCDS16561.1; -.
PIR; S12477; S12477.
RefSeq; NP_033188.3; NM_009162.3.
UniGene; Mm.4836; -.
ProteinModelPortal; P12961; -.
IntAct; P12961; 1.
MINT; MINT-1508684; -.
STRING; 10090.ENSMUSP00000024005; -.
MEROPS; I21.001; -.
iPTMnet; P12961; -.
PhosphoSitePlus; P12961; -.
PaxDb; P12961; -.
PeptideAtlas; P12961; -.
PRIDE; P12961; -.
Ensembl; ENSMUST00000024005; ENSMUSP00000024005; ENSMUSG00000023236.
GeneID; 20394; -.
KEGG; mmu:20394; -.
UCSC; uc008lpq.1; mouse.
CTD; 6447; -.
MGI; MGI:98289; Scg5.
eggNOG; KOG4187; Eukaryota.
eggNOG; ENOG410ZRXV; LUCA.
GeneTree; ENSGT00390000009816; -.
HOGENOM; HOG000259690; -.
HOVERGEN; HBG000031; -.
InParanoid; P12961; -.
OMA; PAHQATN; -.
OrthoDB; EOG091G0LE0; -.
PhylomeDB; P12961; -.
TreeFam; TF314328; -.
PRO; PR:P12961; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000023236; -.
CleanEx; MM_SCG5; -.
ExpressionAtlas; P12961; baseline and differential.
Genevisible; P12961; MM.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IDA:UniProtKB.
GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
GO; GO:0016486; P:peptide hormone processing; IDA:UniProtKB.
GO; GO:0046883; P:regulation of hormone secretion; IDA: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; Complete proteome;
Direct protein sequencing; Disulfide bond; Neuropeptide;
Phosphoprotein; Reference proteome; Secreted; Signal; Sulfation;
Transport.
SIGNAL 1 26
CHAIN 27 212 Neuroendocrine protein 7B2.
/FTId=PRO_0000000044.
CHAIN 27 176 N-terminal peptide. {ECO:0000250}.
/FTId=PRO_0000000045.
PEPTIDE 200 212 C-terminal peptide. {ECO:0000250}.
/FTId=PRO_0000000046.
MOD_RES 141 141 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 205 205 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
DISULFID 120 130 {ECO:0000250}.
MUTAGEN 177 177 R->A: No effect on proteolytic
processing. Abolishes proteolytic
processing; when associated with G-178.
{ECO:0000269|PubMed:8034690}.
MUTAGEN 178 178 R->G: Abolishes proteolytic processing;
when associated with A-177.
{ECO:0000269|PubMed:8034690}.
CONFLICT 6 6 V -> G (in Ref. 2; BAB23956).
{ECO:0000305}.
CONFLICT 119 119 P -> H (in Ref. 2; BAB30765).
{ECO:0000305}.
CONFLICT 145 145 Q -> R (in Ref. 2; BAB31669).
{ECO:0000305}.
CONFLICT 153 153 P -> T (in Ref. 2; BAC27581).
{ECO:0000305}.
SEQUENCE 212 AA; 23866 MW; 6D8CD046532F9609 CRC64;
MASRLVSAML SGLLFWLMFE WNPAFAYSPR TPDRVSETDI QRLLHGVMEQ LGIARPRVEY
PAHQAMNLVG PQSIEGGAHE GLQHLGPFGN IPNIVAELTG DNIPKDFSED QGYPDPPNPC
PLGKTADDGC LENAPDTAEF SREFQLDQHL FDPEHDYPGL GKWNKKLLYE KMKGGQRRKR
RSVNPYLQGK RLDNVVAKKS VPHFSEEEKE AE


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