O35314 · SCG1_RAT
- ProteinSecretogranin-1
- GeneChgb
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids675 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Secretogranin-1 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Cellular Component | secretory granule |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSecretogranin-1
- Alternative names
- Cleaved into 3 chains
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionO35314
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Neuroendocrine and endocrine secretory granules.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, modified residue, glycosylation, peptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MQRAMLLGLLGAAALAAVIS | ||||||
Chain | PRO_0000005446 | 21-675 | Secretogranin-1 | |||
Sequence: APVDNRDHNEEMVTRCIIEVLSNALSKSSAPTITPECRQVLRKSGKEVKGEEKGENENSKFEVRLLRDPSDASVGRWASSREETGAPVEDSPGQAKVDNEEWTGGGGHSREAVDDQESLHPSNQQVSKEAKIRHSEERGGKEEEEEEGKIYPKGEHRGDAGEEKKHTEESGEKHNAFSNKRSEASAKKKEESVARAEAHFVELEKTHSREQSSQESGEETRRQEKPQELPDQDQSEEESEEGEEGEEGATSEVTKRRPRHHHWRSQSNKPSYEGRRPLSEERKHAAGESKDANVATANLGEKRGHHLAHYRASEEEPDYGEELRSYPGFQAPQGLQYQGRGSEEVRAPSPRSEESQEKEYKRNHPDSELESTANRHSEETEEERSYEGAKGRQHRGRGREPGAYPALDSRQEKRLLDEGHDPVHESPVDTAKRYPQSKWQEQEKNYLNYDEEGDQGRWWQQEEQLEPEESREEVSFPDRQYAPYPTTEKRKRLGALFNPYFDPLQWKNSDFEKKGNPDDSFLDDDGEDGNGVTMTEKNFFPEYNYDWWEKRPFSEDVNWGYEKRSFARAPHLDLKRQYDDGVAELDQLLHYRKKAAEFPDFYDSEEQMGPHQEAEDEKDRADQRVLTEEEKKELENLAAMDLELQKIAEKFSQRG | ||||||
Disulfide bond | 36↔57 | |||||
Sequence: CIIEVLSNALSKSSAPTITPEC | ||||||
Modified residue | 93 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 93 | O-linked (Xyl...) (chondroitin sulfate) serine | ||||
Sequence: S | ||||||
Modified residue | 99 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 100 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 129 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 147 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 190 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 236 | O-linked (Xyl...) (chondroitin sulfate) serine | ||||
Sequence: S | ||||||
Modified residue | 255 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 259 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 291 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 309 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 333 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 339 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 362 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 372 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 375 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 397 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 469 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 490 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 529 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 540 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 563 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Peptide | PRO_0000432733 | 572-582 | PE-11 | |||
Sequence: PFSEDVNWGYE | ||||||
Peptide | PRO_0000005447 | 615-674 | CCB peptide short form | |||
Sequence: AAEFPDFYDSEEQMGPHQEAEDEKDRADQRVLTEEEKKELENLAAMDLELQKIAEKFSQR | ||||||
Peptide | PRO_0000411990 | 615-675 | CCB peptide long form | |||
Sequence: AAEFPDFYDSEEQMGPHQEAEDEKDRADQRVLTEEEKKELENLAAMDLELQKIAEKFSQRG | ||||||
Modified residue | 622 | Sulfotyrosine; partial | ||||
Sequence: Y | ||||||
Modified residue | 624 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 674 | Arginine amide; in CCB peptide short form | ||||
Sequence: R |
Post-translational modification
Extensively processed in glucagonoma tissue by limited proteolysis at conserved basic residues. Alternative processing are seen in different tissues. The proglucagon-converting enzymes present in transformed alpha-cells are likely candidates to be involved in tissue-specific processing.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the brain, adrenal medulla and anterior pituitary. In the brain, localized to the hippocampal formation, the endocrine hypothalamus, the olfactory system, and in anatomically distinct structures in the pons-medulla.
Developmental stage
First expressed in the brain around embryonic days 13-14, and peaks by postnatal day 20.
Gene expression databases
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 64-89 | Basic and acidic residues | ||||
Sequence: SGKEVKGEEKGENENSKFEVRLLRDP | ||||||
Region | 64-507 | Disordered | ||||
Sequence: SGKEVKGEEKGENENSKFEVRLLRDPSDASVGRWASSREETGAPVEDSPGQAKVDNEEWTGGGGHSREAVDDQESLHPSNQQVSKEAKIRHSEERGGKEEEEEEGKIYPKGEHRGDAGEEKKHTEESGEKHNAFSNKRSEASAKKKEESVARAEAHFVELEKTHSREQSSQESGEETRRQEKPQELPDQDQSEEESEEGEEGEEGATSEVTKRRPRHHHWRSQSNKPSYEGRRPLSEERKHAAGESKDANVATANLGEKRGHHLAHYRASEEEPDYGEELRSYPGFQAPQGLQYQGRGSEEVRAPSPRSEESQEKEYKRNHPDSELESTANRHSEETEEERSYEGAKGRQHRGRGREPGAYPALDSRQEKRLLDEGHDPVHESPVDTAKRYPQSKWQEQEKNYLNYDEEGDQGRWWQQEEQLEPEESREEVSFPDRQYAPYPTT | ||||||
Compositional bias | 123-137 | Basic and acidic residues | ||||
Sequence: TGGGGHSREAVDDQE | ||||||
Compositional bias | 147-252 | Basic and acidic residues | ||||
Sequence: SKEAKIRHSEERGGKEEEEEEGKIYPKGEHRGDAGEEKKHTEESGEKHNAFSNKRSEASAKKKEESVARAEAHFVELEKTHSREQSSQESGEETRRQEKPQELPDQ | ||||||
Compositional bias | 253-267 | Acidic residues | ||||
Sequence: DQSEEESEEGEEGEE | ||||||
Compositional bias | 286-309 | Basic and acidic residues | ||||
Sequence: QSNKPSYEGRRPLSEERKHAAGES | ||||||
Compositional bias | 322-342 | Basic and acidic residues | ||||
Sequence: KRGHHLAHYRASEEEPDYGEE | ||||||
Compositional bias | 366-448 | Basic and acidic residues | ||||
Sequence: RAPSPRSEESQEKEYKRNHPDSELESTANRHSEETEEERSYEGAKGRQHRGRGREPGAYPALDSRQEKRLLDEGHDPVHESPV | ||||||
Compositional bias | 456-496 | Basic and acidic residues | ||||
Sequence: QSKWQEQEKNYLNYDEEGDQGRWWQQEEQLEPEESREEVSF | ||||||
Region | 528-555 | Disordered | ||||
Sequence: NSDFEKKGNPDDSFLDDDGEDGNGVTMT | ||||||
Region | 620-646 | Disordered | ||||
Sequence: DFYDSEEQMGPHQEAEDEKDRADQRVL |
Sequence similarities
Belongs to the chromogranin/secretogranin protein family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length675
- Mass (Da)77,536
- Last updated2007-02-20 v2
- Checksum042B045B272074FC
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6AW29 | A0A8I6AW29_RAT | Chgb | 693 | ||
A0A8I6A6A1 | A0A8I6A6A1_RAT | Chgb | 675 | ||
A0A8L2QFU5 | A0A8L2QFU5_RAT | Chgb | 682 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 64-89 | Basic and acidic residues | ||||
Sequence: SGKEVKGEEKGENENSKFEVRLLRDP | ||||||
Compositional bias | 123-137 | Basic and acidic residues | ||||
Sequence: TGGGGHSREAVDDQE | ||||||
Compositional bias | 147-252 | Basic and acidic residues | ||||
Sequence: SKEAKIRHSEERGGKEEEEEEGKIYPKGEHRGDAGEEKKHTEESGEKHNAFSNKRSEASAKKKEESVARAEAHFVELEKTHSREQSSQESGEETRRQEKPQELPDQ | ||||||
Compositional bias | 253-267 | Acidic residues | ||||
Sequence: DQSEEESEEGEEGEE | ||||||
Compositional bias | 286-309 | Basic and acidic residues | ||||
Sequence: QSNKPSYEGRRPLSEERKHAAGES | ||||||
Compositional bias | 322-342 | Basic and acidic residues | ||||
Sequence: KRGHHLAHYRASEEEPDYGEE | ||||||
Sequence conflict | 358 | in Ref. 1; AAB72089 | ||||
Sequence: Q → R | ||||||
Compositional bias | 366-448 | Basic and acidic residues | ||||
Sequence: RAPSPRSEESQEKEYKRNHPDSELESTANRHSEETEEERSYEGAKGRQHRGRGREPGAYPALDSRQEKRLLDEGHDPVHESPV | ||||||
Compositional bias | 456-496 | Basic and acidic residues | ||||
Sequence: QSKWQEQEKNYLNYDEEGDQGRWWQQEEQLEPEESREEVSF | ||||||
Sequence conflict | 461-464 | in Ref. 1; AAB72089 | ||||
Sequence: EQEK → GQGE | ||||||
Sequence conflict | 588 | in Ref. 1; AAB72089 | ||||
Sequence: R → K |
Mass Spectrometry
CCB peptide long form
Molecular mass is 7,270.2446 Da. Determined by MALDI. Sulfated and phosphorylated CCB peptide long form.CCB peptide long form
Molecular mass is 7,190.3135 Da. Determined by MALDI. Sulfated or phosphorylated CCB peptide long form.CCB peptide long form
Molecular mass is 7,110.2524 Da. Determined by MALDI. CCB peptide long form without any modifications.CCB peptide short form
Molecular mass is 7,212.2847 Da. Determined by MALDI. Sulfated and phosphorylated CCB peptide short form.CCB peptide short form
Molecular mass is 7,132.28 Da. Determined by MALDI. Sulfated or phosphorylated CCB peptide short form.CCB peptide short form
Molecular mass is 7,052.341 Da. Determined by MALDI. CCB peptide short form without any modifications.Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF019974 EMBL· GenBank· DDBJ | AAB72089.1 EMBL· GenBank· DDBJ | mRNA | ||
BC128743 EMBL· GenBank· DDBJ | AAI28744.1 EMBL· GenBank· DDBJ | mRNA |