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

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	212 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Transport
Cellular component	Secreted
Domain	Signal
Molecular function	Chaperone Neuropeptide
PTM	Cleavage on pair of basic residues Disulfide bond Sulfation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	intracellular protein transport Inferred from direct assay Ref.4. Source: UniProtKB neuropeptide signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW peptide hormone processing Inferred from direct assay Ref.5. Source: UniProtKB regulation of hormone secretion Inferred from direct assay Ref.5. Source: UniProtKB
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell secretory granule Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	enzyme inhibitor activity Inferred from direct assay Ref.6. Source: UniProtKB unfolded protein binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 26	26
	Chain	27 – 212	186	Neuroendocrine protein 7B2		PRO_0000000044
	Chain	27 – 176	150	N-terminal peptide By similarity		PRO_0000000045
	Peptide	200 – 212	13	C-terminal peptide By similarity		PRO_0000000046
Amino acid modifications
	Disulfide bond	120 ↔ 130		By similarity
Experimental info
	Mutagenesis	177	1	R → A: No effect on proteolytic processing. Abolishes proteolytic processing; when associated with G-178. Ref.7
	Mutagenesis	178	1	R → G: Abolishes proteolytic processing; when associated with A-177. Ref.7
	Sequence conflict	6	1	V → G in BAB23956. Ref.2
	Sequence conflict	119	1	P → H in BAB30765. Ref.2
	Sequence conflict	145	1	Q → R in BAB31669. Ref.2
	Sequence conflict	153	1	P → T in BAC27581. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P12961 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 6D8CD046532F9609	FASTA	212	23,866
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00123059.
PIR	S12477.
RefSeq	NP_033188.3. NM_009162.3.
UniGene	Mm.4836.
3D structure databases
ProteinModelPortal	P12961.
ModBase	Search...
Protein family/group databases
MEROPS	I21.001.
PTM databases
PhosphoSite	P12961.
Proteomic databases
PaxDb	P12961.
PRIDE	P12961.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000024005; ENSMUSP00000024005; ENSMUSG00000023236.
GeneID	20394.
KEGG	mmu:20394.
Organism-specific databases
CTD	6447.
MGI	MGI:98289. Scg5.
Phylogenomic databases
eggNOG	NOG271457.
HOGENOM	HOG000259690.
HOVERGEN	HBG000031.
InParanoid	P12961.
OMA	GPYGNIP.
OrthoDB	EOG44MXSZ.
Gene expression databases
ArrayExpress	P12961.
Bgee	P12961.
CleanEx	MM_SCG5.
Genevestigator	P12961.
GermOnline	ENSMUSG00000023236. Mus musculus.
Family and domain databases
InterPro	IPR007945. Secretogranin_V. [Graphical view]
PANTHER	PTHR12738. PTHR12738. 1 hit.
Pfam	PF05281. Secretogranin_V. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	298342.
SOURCE	Search...

Entry information

Entry name

7B2_MOUSE

Accession

Primary (citable) accession number: P12961
Secondary accession number(s): Q8CCZ3 , Q9CYP0, Q9D2P6, Q9DB14

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	April 3, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program