ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P23389


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name SCG1_BOVIN
Primary accession number P23389
Secondary accession number O02707
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on December 1, 2000 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 71)
Name and origin of the protein
Protein name Secretogranin-1 [Precursor]
Synonyms Secretogranin I
SgI
Chromogranin-B
CgB
Contains Secretogranin-1(476-566)
Peptide BAM-1745
Secretolytin
Gene name
Name: CHGB
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-597.
TISSUE=Adrenal chromaffin;
DOI=10.1016/0167-4781(91)90094-3; PubMed=2025642 [NCBI, ExPASy, EBI, Israel, Japan]
Bauer J.W., Fischer-Colbrie R.;
"Primary structure of bovine chromogranin B deduced from cDNA sequence.";
Biochim. Biophys. Acta 1089:124-126(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Adrenal medulla;
DOI=10.1016/S0014-5793(97)00276-7; PubMed=9136897 [NCBI, ExPASy, EBI, Israel, Japan]
Yoo S.H., Kang Y.K.;
"Identification of the secretory vesicle membrane binding region of chromogranin B.";
FEBS Lett. 406:259-262(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 21-646.
TISSUE=Adrenal medulla;
DOI=10.1007/BF00713372; PubMed=1350945 [NCBI, ExPASy, EBI, Israel, Japan]
Grandy D.K., Leduc R., Makam H., Flanagan T., Diliberto E.J., Civelli O., Viveros O.H.;
"Nucleotide and deduced amino acid sequence of bovine adrenal medulla chromogranin B (secretogranin I).";
Cell. Mol. Neurobiol. 12:185-192(1992).
[4]
PROTEIN SEQUENCE OF 239-244 AND 562-565, AND SUBCELLULAR LOCATION.
DOI=10.1016/0167-4889(93)90078-4; PubMed=8218367 [NCBI, ExPASy, EBI, Israel, Japan]
Yoo S.H.;
"pH-dependent binding of chromogranin B and secretory vesicle matrix proteins to the vesicle membrane.";
Biochim. Biophys. Acta 1179:239-246(1993).
[5]
PROTEIN SEQUENCE OF 567-580, AND MASS SPECTROMETRY.
DOI=10.1016/0167-4838(92)90430-L; PubMed=1554736 [NCBI, ExPASy, EBI, Israel, Japan]
Dillen L., Boel S., De Potter W.P., Claeys M.;
"Mass spectrometric characterization of bovine chromaffin granule peptides related to chromogranin B.";
Biochim. Biophys. Acta 1120:105-112(1992).
[6]
PROTEIN SEQUENCE OF 567-580, AND PYROGLUTAMATE FORMATION AT GLN-567.
DOI=10.1007/BF00712845; PubMed=1982622 [NCBI, ExPASy, EBI, Israel, Japan]
Flanagan T., Taylor L., Poulter L., Viveros O.H., Diliberto E.J. Jr.;
"A novel 1745-dalton pyroglutamyl peptide derived from chromogranin B is in the bovine adrenomedullary chromaffin vesicle.";
Cell. Mol. Neurobiol. 10:507-523(1990).
[7]
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, AND CHACTERIZATION OF SECRETOLYTIN.
TISSUE=Adrenal chromaffin;
PubMed=7744058 [NCBI, ExPASy, EBI, Israel, Japan]
Strub J.-M., Garcia-Sablone P., Lonning K., Taupenot L., Hubert P., van Dorsselaer A., Aunis D., Metz-Boutigue M.-H.;
"Processing of chromogranin B in bovine adrenal medulla. Identification of secretolytin, the endogenous C-terminal fragment of residues 614-626 with antibacterial activity.";
Eur. J. Biochem. 229:356-368(1995).
[8]
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, AND VARIANT VAL-597.
DOI=10.1002/pmic.200300693; PubMed=15174145 [NCBI, ExPASy, EBI, Israel, Japan]
Gasnier C., Lugardon K., Ruh O., Strub J.-M., Aunis D., Metz-Boutigue M.H.;
"Characterization and location of post-translational modifications on chromogranin B from bovine adrenal medullary chromaffin granules.";
Proteomics 4:1789-1801(2004).
[9]
CHARACTERIZATION OF SECRETOLYTIN.
DOI=10.1016/0014-5793(95)01529-9; PubMed=8603705 [NCBI, ExPASy, EBI, Israel, Japan]
Strub J.-M., Hubert P., Nullans G., Aunis D., Metz-Boutigue M.-H.;
"Antibacterial activity of secretolytin, a chromogranin B-derived peptide (614-626), is correlated with peptide structure.";
FEBS Lett. 379:273-278(1996).
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.
  • FUNCTION: 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.
  • SUBCELLULAR LOCATION: Peptide BAM-1745: Secreted.
  • SUBCELLULAR LOCATION: Secretolytin: Secreted.
  • PTM: O-glycosylated by the trisaccharide, GalNAc-Gal-NeuAc, on 2 sites in the N-terminal. May be glycated.
  • PTM: Extensively phosphorylated.
  • PTM: Differentially processed on numerous sites throughout the sequence depending on tissue type.
  • MASS SPECTROMETRY: Mass=2053; Method=MALDI; Range=161-178; Note=Monophosphorylated; Source=PubMed:15174145;.
  • MASS SPECTROMETRY: Mass=2338; Method=MALDI; Range=276-299; Note=Monophosphorylated; Source=PubMed:15174145;.
  • MASS SPECTROMETRY: Mass=6952; Method=MALDI; Range=300-360; Note=Monophosphorylated and monosulfated; Source=PubMed:15174145;.
  • MASS SPECTROMETRY: Mass=5304; Method=MALDI; Range=361-409; Note=Monophosphorylated; Source=PubMed:15174145;.
  • MASS SPECTROMETRY: Mass=2417; Method=MALDI; Range=427-445; Note=Monosulfated; Source=PubMed:15174145;.
  • MASS SPECTROMETRY: Mass=1223; Method=MALDI; Range=476-485; Note=Pyroglutamate; Source=PubMed:15174145;.
  • MASS SPECTROMETRY: Mass=3933; Method=MALDI; Range=486-516; Note=Diphosphorylated; Source=PubMed:15174145;.
  • MASS SPECTROMETRY: Mass=1919; Method=MALDI; Range=530-542; Note=Monosulfated; Source=PubMed:15174145;.
  • MASS SPECTROMETRY: Mass=1746; Method=MALDI; Range=567-580; Note=Pyroglutamate; Source=PubMed:15174145;.
  • MASS SPECTROMETRY: Mass=1746; Method=FAB; Range=567-580; Note=Pyroglutamate; Source=PubMed:1554736;.
  • MASS SPECTROMETRY: Mass=997.5; Method=MALDI; Range=590-596; Note=Monophosphorylated; Source=PubMed:15174145;.
  • MASS SPECTROMETRY: Mass=3042; Method=MALDI; Range=584-609; Note=Non-phosphorylatecd. Val-597; Source=PubMed:15174145;.
  • MASS SPECTROMETRY: Mass=3122; Method=MALDI; Range=584-609; Note=Monophosphorylatecd. Val-597; Source=PubMed:15174145;.
  • MASS SPECTROMETRY: Mass=3154; Method=MALDI; Range=584-609; Note=Monophosphorylatecd. Met-597; Source=PubMed:15174145;.
  • MASS SPECTROMETRY: Mass=3170; Method=MALDI; Range=584-609; Note=Monophosphorylatecd. Oxidized Met-597; Source=PubMed:15174145;.
  • MASS SPECTROMETRY: Mass=3202; Method=MALDI; Range=584-609; Note=Diphosphorylatecd. Val-597; Source=PubMed:15174145;.
  • MASS SPECTROMETRY: Mass=3250; Method=MALDI; Range=584-609; Note=Diphosphorylatecd. Oxidized Met-597; Source=PubMed:15174145;.
  • MASS SPECTROMETRY: Mass=1460.3; Mass_error=0.4; Method=Electrospray; Range=624-646; Note=Pyroglutamate; Source=PubMed:7744058;.
  • SIMILARITY: Belongs to the chromogranin/secretogranin protein family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X55027; CAA38846.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U88551; AAC48720.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X55489; CAA39109.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S15901; S15901.
RefSeq NP_851349.1; -.
UniGene Bt.5448
3D structure databases
DisProt DP00124; -.
ModBase P23389.
Ontologies
GO
GO:0031410; Cellular component: cytoplasmic vesicle (inferred from electronic annotation from UniProtKB-KW).
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001819; Chromogranin_AB.
IPR001990; Granin.
Graphical view of domain structure.
PANTHER PTHR10583; Chromogranin_AB; 1.
Pfam PF01271; Granin; 1.
Pfam graphical view of domain structure.
PRINTS PR00659; CHROMOGRANIN.
PROSITE PS00422; GRANINS_1; 1.
PS00423; GRANINS_2; 1.
ProtoNet P23389.
Genome annotation databases
Ensembl ENSBTAG00000011782; Bos taurus. [Contig view]
GeneID 281071; -.
KEGG bta:281071; -.
Phylogenomic databases
HOVERGEN P23389; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Cleavage on pair of basic residues; Cytoplasmic vesicle; Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein; Polymorphism; Pyrrolidone carboxylic acid; Secreted; Signal; Sulfation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    20  20      
CHAIN   21   646  626     Secretogranin-1. PRO_0000005434
CHAIN   476   566  91     Secretogranin-1(476-566). PRO_0000326263
PEPTIDE   567   580  14     Peptide BAM-1745. PRO_0000005436
PEPTIDE   630   646  17     Secretolytin. PRO_0000005437
COMPBIAS   617   624  8     Poly-Glu. 
SITE   161   162  2     Cleavage; major site. 
SITE   275   276  2     Cleavage; major site. 
SITE   278   279  2     Cleavage; major site. 
SITE   324   325  2     Cleavage; major site. 
SITE   629   630  2     Cleavage; major site. 
MOD_RES   74    74        Phosphoserine (Potential). 
MOD_RES   79    79        Phosphothreonine (Probable). 
MOD_RES   92    92        Phosphothreonine (Potential). 
MOD_RES   99    99        Phosphoserine (Potential). 
MOD_RES   100   100        Phosphoserine (Potential). 
MOD_RES   104   104        Phosphoserine (Potential). 
MOD_RES   140   140        N6-acetyllysine (By similarity). 
MOD_RES   146   146        Phosphoserine (Probable). 
MOD_RES   168   168        Phosphoserine. 
MOD_RES   276   276        Phosphoserine (Potential). 
MOD_RES   277   277        Phosphoserine (Potential). 
MOD_RES   295   295        Phosphoserine (Potential). 
MOD_RES   315   315        Sulfotyrosine (By similarity). 
MOD_RES   351   351        Phosphoserine. 
MOD_RES   354   354        Phosphoserine. 
MOD_RES   375   375        Phosphoserine (Potential). 
MOD_RES   378   378        Phosphoserine (Potential). 
MOD_RES   438   438        Sulfotyrosine (Potential). 
MOD_RES   441   441        Sulfotyrosine (Probable). 
MOD_RES   476   476        Pyrrolidone carboxylic acid; in secretogranin-1(476-566). 
MOD_RES   502   502        Phosphoserine (Potential). 
MOD_RES   503   503        Phosphoserine (Potential). 
MOD_RES   514   514        Phosphoserine (Potential). 
MOD_RES   535   535        Sulfotyrosine (Probable). 
MOD_RES   537   537        Sulfotyrosine (Potential). 
MOD_RES   567   567        Pyrrolidone carboxylic acid; in peptide BAM-1745. 
MOD_RES   584   584        Phosphoserine. 
MOD_RES   593   593        Phosphoserine. 
MOD_RES   598   598        Phosphoserine. 
CARBOHYD   113   113        O-linked (GalNAc...) (Probable). 
CARBOHYD   190   190        O-linked (GalNAc...) (Probable). 
DISULFID   36    57        By similarity. 
VARIANT   597   597  1     M -> V. 
CONFLICT   64    64        N -> S (in Ref. 1; CAA38846). 
CONFLICT   70    70        N -> D (in Ref. 2; AAC48720). 
CONFLICT   93    98        SEAPGL -> FRSPRAS (in Ref. 3; CAA39109). 
CONFLICT   181   181        T -> M (in Ref. 2; AAC48720). 
CONFLICT   261   261        H -> R (in Ref. 2; AAC48720). 
CONFLICT   386   386        P -> R (in Ref. 2; AAC48720). 
CONFLICT   481   481        H -> L (in Ref. 3; CAA39109). 
Sequence information
Length: 646 AA [This is the length of the unprocessed precursor] Molecular weight: 73340 Da [This is the MW of the unprocessed precursor] CRC64: 420DB1178FD9E415 [This is a checksum on the sequence]
        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 

P23389 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!