Reviewed, UniProtKB/Swiss-Prot P18844 (7B2_XENLA)

Names and origin

Protein names

Recommended name:
    Neuroendocrine protein 7B2
Alternative name(s):
    Secretogranin V
Cleaved into the following 2 chains:
    1- Recommended name:
            N-terminal peptide
    2- Recommended name:
            C-terminal peptide

Gene names

Name:

sgne1

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	161 AA.
Sequence status	Fragment.
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, 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 By similarity.
Subunit structure	Interacts with pcsk2 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 By similarity. Sulfated on tyrosine residues By similarity.
Sequence similarities	Belongs to the 7B2 family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Secreted
Molecular function	Chaperone Neuropeptide
PTM	Cleavage on pair of basic residues Disulfide bond Phosphoprotein Sulfation
Gene Ontology (GO)
Biological process	intracellular protein transport Inferred from sequence or structural similarity. Source: UniProtKB neuropeptide signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW peptide hormone processing Inferred from sequence or structural similarity. Source: UniProtKB regulation of hormone secretion Inferred from sequence or structural similarity. 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 sequence or structural similarity. 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
	Chain	‹1 – 161	›161	Neuroendocrine protein 7B2		PRO_0000045862
	Chain	‹1 – 128	›128	N-terminal peptide By similarity		PRO_0000000053
	Peptide	152 – 161	10	C-terminal peptide By similarity		PRO_0000000054
Amino acid modifications
	Modified residue	157	1	Phosphoserine By similarity
	Disulfide bond	73 ↔ 82		Ref.3
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P18844-1 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: A6E32531A29D82FC	FASTA	161	17,992
	10 20 30 40 50 60 MEELGIARPR VEYPAHQAMN LVGPQSIEGG AHEGLQHLGP YGNIPNIVAE LTGDNIPKDF 70 80 90 100 110 120 REDQGYPNPP NPCPVGKTGD GCLEDTPDTA QFSREYQLHQ NLYDPEHNYP GASTWNKKLL 130 140 150 160 YEKIKGASQR QKRTVNPYLQ GQKLDKVVAK KSVPHFSDEE E

References

[1]	"The novel pituitary polypeptide 7B2 is a highly-conserved protein coexpressed with proopiomelanocortin." Martens G.J.M., Bussemakers M.J.G., Ayoubi T.A.Y., Jenks B.G. Eur. J. Biochem. 181:75-79(1989) [PubMed: 2714283] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The neuroendocrine polypeptide 7B2 is a precursor protein." Ayoubi T.A.Y., van Duijnhoven H.L.P., van de Ven W.J.M., Jenks B.G., Roubos E.W., Martens G.J.M. J. Biol. Chem. 265:15644-15647(1990) [PubMed: 2394742] [Abstract] Cited for: PROTEOLYTIC PROCESSING.
[3]	"Manipulation of disulfide bonds differentially affects the intracellular transport, sorting, and processing of neuroendocrine secretory proteins." Van Horssen A.M., Van Kuppeveld F.J.M., Martens G.J.M. J. Neurochem. 71:402-409(1998) [PubMed: 9648890] [Abstract] Cited for: DISULFIDE BOND.
[4]	"Neuroendocrine secretory protein 7B2: structure, expression and functions." Mbikay M., Seidah N.G., Chretien M. Biochem. J. 357:329-342(2001) [PubMed: 11439082] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X15608 mRNA. Translation: CAA33631.1.
PIR	S03938.
UniGene	Xl.47184
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	I21.001.
Phylogenomic databases
HOVERGEN	P18844.
Family and domain databases
InterPro	IPR007945. Secretogranin_V. [Graphical view]
PANTHER	PTHR12738. Secretogranin_V. 1 hit.
Pfam	PF05281. Secretogranin_V. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

7B2_XENLA

Accession

Primary (citable) accession number: P18844

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	June 16, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Xenopus annotation project