Secretogranin-1 precursor - Bos taurus (Bovine)

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Reviewed, UniProtKB/Swiss-Prot P23389 (SCG1_BOVIN)

Last modified June 16, 2009. Version 75. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Secretogranin-1
Alternative name(s):
    Secretogranin I
      Short name=SgI
    Chromogranin-B
      Short name=CgB
Cleaved into the following 3 chains:
    1- Recommended name:
            Secretogranin-1(476-566)
    2- Recommended name:
            Peptide BAM-1745
    3- Recommended name:
            Secretolytin

Gene names

Name:

CHGB

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length	646 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Secretogranin-1 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides. The 16 pairs of basic AA distributed throughout its sequence may be used as proteolytic cleavage sites. Secretolytin has antibacterial activity.
Subcellular location	Secretogranin-1: Cytoplasmic vesicle › secretory vesicle membrane; Peripheral membrane protein; Lumenal side. Note: Neuroendocrine and endocrine secretory granules. Found to be membrane bound inside the secretory vesicles. The N-terminal region exhibits pH-dependent membrane-binding activity, binds to the membrane at intravesicular pH (5.5) and freed when the pH is near to physiological pH. Ref.4 Peptide BAM-1745: Secreted. Ref.4 Secretolytin: Secreted. Ref.4
Post-translational modification	O-glycosylated by the trisaccharide, GalNAc-Gal-NeuAc, on 2 sites in the N-terminal. May be glycated. Ref.8 Extensively phosphorylated. Ref.8 Differentially processed on numerous sites throughout the sequence depending on tissue type.
Sequence similarities	Belongs to the chromogranin/secretogranin protein family.
Mass spectrometry	Molecular mass is 2053 Da from positions 161 - 178. Determined by MALDI. Monophosphorylated. Ref.8 Molecular mass is 2338 Da from positions 276 - 299. Determined by MALDI. Monophosphorylated. Ref.8 Molecular mass is 6952 Da from positions 300 - 360. Determined by MALDI. Monophosphorylated and monosulfated. Ref.8 Molecular mass is 5304 Da from positions 361 - 409. Determined by MALDI. Monophosphorylated. Ref.8 Molecular mass is 2417 Da from positions 427 - 445. Determined by MALDI. Monosulfated. Ref.8 Molecular mass is 1223 Da from positions 476 - 485. Determined by MALDI. Pyroglutamate. Ref.8 Molecular mass is 3933 Da from positions 486 - 516. Determined by MALDI. Diphosphorylated. Ref.8 Molecular mass is 1919 Da from positions 530 - 542. Determined by MALDI. Monosulfated. Ref.8 Molecular mass is 1746 Da from positions 567 - 580. Determined by MALDI. Pyroglutamate. Ref.8 Molecular mass is 1746 Da from positions 567 - 580. Determined by FAB. Pyroglutamate. Ref.5 Molecular mass is 997.5 Da from positions 590 - 596. Determined by MALDI. Monophosphorylated. Ref.8 Molecular mass is 3042 Da from positions 584 - 609. Determined by MALDI. Non-phosphorylatecd. Val-597. Ref.8 Molecular mass is 3122 Da from positions 584 - 609. Determined by MALDI. Monophosphorylatecd. Val-597. Ref.8 Molecular mass is 3154 Da from positions 584 - 609. Determined by MALDI. Monophosphorylatecd. Met-597. Ref.8 Molecular mass is 3170 Da from positions 584 - 609. Determined by MALDI. Monophosphorylatecd. Oxidized Met-597. Ref.8 Molecular mass is 3202 Da from positions 584 - 609. Determined by MALDI. Diphosphorylatecd. Val-597. Ref.8 Molecular mass is 3250 Da from positions 584 - 609. Determined by MALDI. Diphosphorylatecd. Oxidized Met-597. Ref.8 Molecular mass is 1460.3±0.4 Da from positions 624 - 646. Determined by ESI. Pyroglutamate. Ref.7

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Ontologies

Keywords
Cellular component	Cytoplasmic vesicle Membrane Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
PTM	Acetylation Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein Pyrrolidone carboxylic acid Sulfation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW secretory granule membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Ref.8 Ref.7

Chain

21 – 646

626

Secretogranin-1

PRO_0000005434

Chain

476 – 566

Secretogranin-1(476-566)

PRO_0000326263

Peptide

567 – 580

Peptide BAM-1745

PRO_0000005436

Peptide

630 – 646

Secretolytin

PRO_0000005437

Regions

Compositional bias

617 – 624

Poly-Glu

Sites

Site

161 – 162

Cleavage; major site

Site

275 – 276

Cleavage; major site

Site

278 – 279

Cleavage; major site

Site

324 – 325

Cleavage; major site

Site

629 – 630

Cleavage; major site

Amino acid modifications

Modified residue

Phosphoserine Potential

Modified residue

Phosphothreonine Probable

Modified residue

Phosphothreonine Potential

Modified residue

Phosphoserine Potential

Modified residue

100

Phosphoserine Potential

Modified residue

104

Phosphoserine Potential

Modified residue

140

N6-acetyllysine By similarity

Modified residue

146

Phosphoserine Probable

Modified residue

168

Phosphoserine Ref.8

Modified residue

276

Phosphoserine Potential

Modified residue

277

Phosphoserine Potential

Modified residue

295

Phosphoserine Potential

Modified residue

315

Sulfotyrosine By similarity

Modified residue

351

Phosphoserine Ref.8

Modified residue

354

Phosphoserine Ref.8

Modified residue

375

Phosphoserine Potential

Modified residue

378

Phosphoserine Potential

Modified residue

438

Sulfotyrosine Potential

Modified residue

441

Sulfotyrosine Probable

Modified residue

476

Pyrrolidone carboxylic acid; in secretogranin-1(476-566)

Modified residue

502

Phosphoserine Potential

Modified residue

503

Phosphoserine Potential

Modified residue

514

Phosphoserine Potential

Modified residue

535

Sulfotyrosine Probable

Modified residue

537

Sulfotyrosine Potential

Modified residue

567

Pyrrolidone carboxylic acid; in peptide BAM-1745

Modified residue

584

Phosphoserine Ref.8

Modified residue

593

Phosphoserine Ref.8

Modified residue

598

Phosphoserine Ref.8

Glycosylation

113

O-linked (GalNAc...) Probable

Glycosylation

190

O-linked (GalNAc...) Probable

Disulfide bond

36 ↔ 57

By similarity

Natural variations

Natural variant

597

M → V Ref.8 Ref.1

Experimental info

Sequence conflict

N → S in CAA38846. Ref.1

Sequence conflict

N → D in AAC48720. Ref.2

Sequence conflict

93 – 98

SEAPGL → FRSPRAS in CAA39109. Ref.3

Sequence conflict

181

T → M in AAC48720. Ref.2

Sequence conflict

261

H → R in AAC48720. Ref.2

Sequence conflict

386

P → R in AAC48720. Ref.2

Sequence conflict

481

H → L in CAA39109. Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

P23389-1 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 420DB1178FD9E415
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FASTA

646

73,340

        10         20         30         40         50         60 
MQPAALLGLL GATVVAAVSS MPVDIRNHNE EVVTHCIIEV LSNALLKSSA PPITPECRQV 

        70         80         90        100        110        120 
LKKNGKELKN EEKSENENTR FEVRLLRDPA DTSEAPGLSS REDSGEGDAQ VPTVADTESG 

       130        140        150        160        170        180 
GHSRERAGEP PGSQVAKEAK TRYSKSEGQN REEEMVKYQK RERGEVGSEE RLSEGPGKAQ 

       190        200        210        220        230        240 
TAFLNQRNQT PAKKEELVSR YDTQSARGLE KSHSRERSSQ ESGEETKSQE NWPQELQRHP 

       250        260        270        280        290        300 
EGQEAPGESE EDASPEVDKR HSRPRHHHGR SRPDRSSQEG NPPLEEESHV GTGNSDEEKA 

       310        320        330        340        350        360 
RHPAHFRALE EGAEYGEEVR RHSAAQAPGD LQGARFGGRG RGEHQALRRP SEESLEQENK 

       370        380        390        400        410        420 
RHGLSPDLNM AQGYSEESEE ERGPAPGPSY RARGGEAAAY STLGQTDEKR FLGETHHRVQ 

       430        440        450        460        470        480 
ESQRDKARRR LPGELRNYLD YGEEKGEEAA RGKWQPQGDP RDADENREEA RLRGKQYAPH 

       490        500        510        520        530        540 
HITEKRLGEL LNPFYDPSQW KSSRFERKDP MDDSFLEGEE ENGLTLNEKN FFPEYNYDWW 

       550        560        570        580        590        600 
EKKPFEEDVN WGYEKRNPVP KLDLKRQYDR VAELDQLLHY RKKSAEFPDF YDSEEQMSPQ 

       610        620        630        640 
HTAENEEEKA GQGVLTEEEE KELENLAAMD LELQKIAEKF SGTRRG

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References

[1]	"Primary structure of bovine chromogranin B deduced from cDNA sequence." Bauer J.W., Fischer-Colbrie R. Biochim. Biophys. Acta 1089:124-126(1991) [PubMed: 2025642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-597. Tissue: Adrenal chromaffin.
[2]	"Identification of the secretory vesicle membrane binding region of chromogranin B." Yoo S.H., Kang Y.K. FEBS Lett. 406:259-262(1997) [PubMed: 9136897] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Adrenal medulla.
[3]	"Nucleotide and deduced amino acid sequence of bovine adrenal medulla chromogranin B (secretogranin I)." Grandy D.K., Leduc R., Makam H., Flanagan T., Diliberto E.J., Civelli O., Viveros O.H. Cell. Mol. Neurobiol. 12:185-192(1992) [PubMed: 1350945] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-646. Tissue: Adrenal medulla.
[4]	"pH-dependent binding of chromogranin B and secretory vesicle matrix proteins to the vesicle membrane." Yoo S.H. Biochim. Biophys. Acta 1179:239-246(1993) [PubMed: 8218367] [Abstract] Cited for: PROTEIN SEQUENCE OF 239-244 AND 562-565, SUBCELLULAR LOCATION.
[5]	"Mass spectrometric characterization of bovine chromaffin granule peptides related to chromogranin B." Dillen L., Boel S., De Potter W.P., Claeys M. Biochim. Biophys. Acta 1120:105-112(1992) [PubMed: 1554736] [Abstract] Cited for: PROTEIN SEQUENCE OF 567-580, MASS SPECTROMETRY.
[6]	"A novel 1745-dalton pyroglutamyl peptide derived from chromogranin B is in the bovine adrenomedullary chromaffin vesicle." Flanagan T., Taylor L., Poulter L., Viveros O.H., Diliberto E.J. Jr. Cell. Mol. Neurobiol. 10:507-523(1990) [PubMed: 1982622] [Abstract] Cited for: PROTEIN SEQUENCE OF 567-580, PYROGLUTAMATE FORMATION AT GLN-567.
[7]	"Processing of chromogranin B in bovine adrenal medulla. Identification of secretolytin, the endogenous C-terminal fragment of residues 614-626 with antibacterial activity." Strub J.-M., Garcia-Sablone P., Lonning K., Taupenot L., Hubert P., van Dorsselaer A., Aunis D., Metz-Boutigue M.-H. Eur. J. Biochem. 229:356-368(1995) [PubMed: 7744058] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-35; 86-99; 127-145; 146-161; 162-176; 186-194; 235-243; 276-289; 308-314; 340-347; 325-335; 430-444; 584-604 AND 634-646, PROTEOLYTIC PROCESSING, MASS SPECTROMETRY, CHACTERIZATION OF SECRETOLYTIN. Tissue: Adrenal chromaffin.
[8]	"Characterization and location of post-translational modifications on chromogranin B from bovine adrenal medullary chromaffin granules." Gasnier C., Lugardon K., Ruh O., Strub J.-M., Aunis D., Metz-Boutigue M.H. Proteomics 4:1789-1801(2004) [PubMed: 15174145] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-211; 276-289; 300-409; 427-445; 476-516; 530-542; 567-580 AND 584-646, PHOSPHORYLATION AT SER-168; SER-351; SER-354; SER-584; SER-593 AND SER-598; PYROGLUTAMATE FORMATION AT GLN-476 AND GLN-567, GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY, VARIANT VAL-597.
[9]	"Antibacterial activity of secretolytin, a chromogranin B-derived peptide (614-626), is correlated with peptide structure." Strub J.-M., Hubert P., Nullans G., Aunis D., Metz-Boutigue M.-H. FEBS Lett. 379:273-278(1996) [PubMed: 8603705] [Abstract] Cited for: CHARACTERIZATION OF SECRETOLYTIN.

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Cross-references

Sequence databases
	X55027 mRNA. Translation: CAA38846.1. U88551 mRNA. Translation: AAC48720.1. X55489 mRNA. Translation: CAA39109.1.
IPI	IPI00688350.
PIR	S15901.
RefSeq	NP_851349.1.
UniGene	Bt.5448
3D structure databases
DisProt	DP00124.
ModBase	Search...
Genome annotation databases
Ensembl	ENSBTAG00000011782. Bos taurus. [Contig view]
GeneID	281071.
KEGG	bta:281071.
Phylogenomic databases
HOVERGEN	P23389.
Family and domain databases
InterPro	IPR001819. Chromogranin_AB. IPR018054. Chromogranin_CS. IPR001990. Granin. [Graphical view]
PANTHER	PTHR10583. Chromogranin_AB. 1 hit.
Pfam	PF01271. Granin. 1 hit. [Graphical view]
PRINTS	PR00659. CHROMOGRANIN.
PROSITE	PS00422. GRANINS_1. 1 hit. PS00423. GRANINS_2. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

SCG1_BOVIN

Accession

Primary (citable) accession number: P23389
Secondary accession number(s): O02707

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	December 1, 2000
Last modified:	June 16, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents