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P12961 (7B2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neuroendocrine protein 7B2
Alternative name(s):
Secretogranin V
Secretogranin-5
Secretory granule endocrine protein I

Cleaved into the following 2 chains:

  1. N-terminal peptide
  2. C-terminal peptide
Gene names
Name:Scg5
Synonyms:Sgne-1, Sgne1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.4 Ref.5

Subunit structure

Interacts with PCSK2/PC2 early in the secretory pathway. Dissociation occurs at later stages By similarity.

Subcellular location

Secreted. Note: Neuroendocrine and endocrine secretory granules.

Post-translational modification

Proteolytically cleaved in the Golgi by a furin-like convertase to generate bioactive peptides. Ref.7

Sulfated on tyrosine residues.

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. Ref.4

Sequence similarities

Belongs to the 7B2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626
Chain27 – 212186Neuroendocrine protein 7B2
PRO_0000000044
Chain27 – 176150N-terminal peptide By similarity
PRO_0000000045
Peptide200 – 21213C-terminal peptide By similarity
PRO_0000000046

Amino acid modifications

Disulfide bond120 ↔ 130 By similarity

Experimental info

Mutagenesis1771R → A: No effect on proteolytic processing. Abolishes proteolytic processing; when associated with G-178. Ref.7
Mutagenesis1781R → G: Abolishes proteolytic processing; when associated with A-177. Ref.7
Sequence conflict61V → G in BAB23956. Ref.2
Sequence conflict1191P → H in BAB30765. Ref.2
Sequence conflict1451Q → R in BAB31669. Ref.2
Sequence conflict1531P → T in BAC27581. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P12961 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 6D8CD046532F9609

FASTA21223,866
        10         20         30         40         50         60 
MASRLVSAML SGLLFWLMFE WNPAFAYSPR TPDRVSETDI QRLLHGVMEQ LGIARPRVEY 

        70         80         90        100        110        120 
PAHQAMNLVG PQSIEGGAHE GLQHLGPFGN IPNIVAELTG DNIPKDFSED QGYPDPPNPC 

       130        140        150        160        170        180 
PLGKTADDGC LENAPDTAEF SREFQLDQHL FDPEHDYPGL GKWNKKLLYE KMKGGQRRKR 

       190        200        210 
RSVNPYLQGK RLDNVVAKKS VPHFSEEEKE AE 

« Hide

References

« Hide 'large scale' references
[1]"cDNA sequence of neuroendocrine protein 7B2 expressed in beta cell tumors of transgenic mice."
Mbikay M., Grant S.G.N., Sirois F., Tadros H., Skowronski J., Lazure C., Seidah N.G., Hanahan D., Chretien M.
Int. J. Pept. Protein Res. 33:39-45(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: BALB/c.
Tissue: Pancreas.
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum, Embryo, Hippocampus and Medulla oblongata.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Retina.
[4]"Mechanism of the facilitation of PC2 maturation by 7B2: involvement in ProPC2 transport and activation but not folding."
Muller L., Zhu X., Lindberg I.
J. Cell Biol. 139:625-638(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]"The neuroendocrine protein 7B2 is required for peptide hormone processing in vivo and provides a novel mechanism for pituitary Cushing's disease."
Westphal C.H., Muller L., Zhou A., Zhu X., Bonner-Weir S., Schambelan M., Steiner D.F., Lindberg I., Leder P.
Cell 96:689-700(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"The neuroendocrine polypeptide 7B2 is an endogenous inhibitor of prohormone convertase PC2."
Martens G.J.M., Braks J.A., Eib D.W., Zhou Y., Lindberg I.
Proc. Natl. Acad. Sci. U.S.A. 91:5784-5787(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION OF PCSK2 BY C-TERMINAL PEPTIDE.
[7]"The neuroendocrine precursor 7B2 is a sulfated protein proteolytically processed by a ubiquitous furin-like convertase."
Paquet L., Bergeron F., Boudreault A., Seidah N.G., Chretien M., Mbikay M., Lazure C.
J. Biol. Chem. 269:19279-19285(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION, CLEAVAGE BY FURIN-LIKE CONVERTASE, MUTAGENESIS OF ARG-177 AND ARG-178.
[8]"Neuroendocrine secretory protein 7B2: structure, expression and functions."
Mbikay M., Seidah N.G., Chretien M.
Biochem. J. 357:329-342(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15830 mRNA. Translation: CAA33835.1.
AK005331 mRNA. Translation: BAB23956.1.
AK011938 mRNA. Translation: BAB27927.1.
AK017481 mRNA. Translation: BAB30765.1.
AK019337 mRNA. Translation: BAB31669.1.
AK031856 mRNA. Translation: BAC27581.1.
BC029021 mRNA. Translation: AAH29021.1.
PIRS12477.
RefSeqNP_033188.3. NM_009162.3.
UniGeneMm.4836.

3D structure databases

ProteinModelPortalP12961.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP12961. 1 interaction.
MINTMINT-1508684.

Protein family/group databases

MEROPSI21.001.

PTM databases

PhosphoSiteP12961.

Proteomic databases

PaxDbP12961.
PRIDEP12961.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024005; ENSMUSP00000024005; ENSMUSG00000023236.
GeneID20394.
KEGGmmu:20394.
UCSCuc008lpq.1. mouse.

Organism-specific databases

CTD6447.
MGIMGI:98289. Scg5.

Phylogenomic databases

eggNOGNOG271457.
HOGENOMHOG000259690.
HOVERGENHBG000031.
InParanoidP12961.
OMAPAHQATN.
OrthoDBEOG7KSX9R.
PhylomeDBP12961.
TreeFamTF314328.

Gene expression databases

ArrayExpressP12961.
BgeeP12961.
CleanExMM_SCG5.
GenevestigatorP12961.

Family and domain databases

InterProIPR007945. Secretogranin_V.
[Graphical view]
PANTHERPTHR12738. PTHR12738. 1 hit.
PfamPF05281. Secretogranin_V. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio298342.
PROP12961.
SOURCESearch...

Entry information

Entry name7B2_MOUSE
AccessionPrimary (citable) accession number: P12961
Secondary accession number(s): Q8CCZ3 expand/collapse secondary AC list , Q9CYP0, Q9D2P6, Q9DB14
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot