P01351 (GAST_PIG) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 81.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Gastrin Cleaved into the following 2 chains:
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| Gene names |
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| Organism | Sus scrofa (Pig) [Complete proteome] | ||||
| Taxonomic identifier | 9823 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 104 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 | Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine. |
| Subcellular location | |
| Post-translational modification | Sulfation enhances proteolytic processing, and blocks peptide degradation. Levels of sulfation differ between proteolytically-cleaved gastrins. Thus, gastrin-6 is almost 73% sulfated, whereas the larger gastrins are less than 50% sulfated. Sulfation levels are also tissue-specific. Ref.5 |
| Sequence similarities | Belongs to the gastrin/cholecystokinin family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hormone |
| PTM | Amidation Cleavage on pair of basic residues Phosphoprotein Pyrrolidone carboxylic acid Sulfation |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | hormone activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 21 | 21 | Potential | ||||||
| Propeptide | 22 – 58 | 37 | PRO_0000010644 | ||||||
| Peptide | 59 – 92 | 34 | Big gastrin | PRO_0000010645 | |||||
| Peptide | 76 – 92 | 17 | Gastrin Ref.3 | PRO_0000010646 | |||||
| Propeptide | 96 – 104 | 9 | PRO_0000010647 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 59 | 1 | Pyrrolidone carboxylic acid; in form big gastrin Ref.1 | ||||||
| Modified residue | 76 | 1 | Pyrrolidone carboxylic acid; in form gastrin Ref.1 | ||||||
| Modified residue | 87 | 1 | Sulfotyrosine; partial Ref.5 | ||||||
| Modified residue | 92 | 1 | Phenylalanine amide By similarity | ||||||
| Modified residue | 96 | 1 | Phosphoserine By similarity | ||||||
Sequences
References
| [1] | "Molecular cloning and nucleotide sequence of full-length of cDNA coding for porcine gastrin." Yoo O.J., Powell C.T., Agarwal K.L. Proc. Natl. Acad. Sci. U.S.A. 79:1049-1053(1982) [PubMed: 6951161] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Studies on gastrin mRNA structure using an oligonucleotide probe." Agarwal K.L., Noyes B.E. Ann. N. Y. Acad. Sci. 343:433-442(1980) [PubMed: 6930858] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 56-82. |
| [3] | "The antral hormone gastrin. Structure of gastrin." Gregory H., Hardy P.M., Jones D.S., Kenner G.W., Sheppard R.C. Nature 204:931-933(1964) [PubMed: 14248711] [Abstract] Cited for: PROTEIN SEQUENCE OF 76-92. |
| [4] | "Synthesis of gastrin." Anderson J.C., Barton M.A., Gregory R.A., Hardy P.M., Kenner G.W., McLeod J.K., Preston J., Sheppard R.C., Morley J.S. Nature 204:933-934(1964) [PubMed: 14248712] [Abstract] Cited for: SYNTHESIS. |
| [5] | "Post-poly(Glu) cleavage and degradation modified by O-sulfated tyrosine: a novel post-translational processing mechanism." Rehfeld J.F., Hansen C.P., Johnsen A.H. EMBO J. 14:389-396(1995) [PubMed: 7530658] [Abstract] Cited for: PROTEOLYTIC PROCESSING, MASS SPECTROMETRY, SULFATION AT TYR-87. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | V01303 mRNA. Translation: CAA24610.1. M25036 mRNA. Translation: AAA31111.1. |
| PIR | GMPGB. A93903. |
| RefSeq | NP_001004036.1. NM_001004036.1. |
| UniGene | Ssc.644. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P01351. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 445524. |
| KEGG | ssc:445524. |
Organism-specific databases | |
| CTD | 2520. |
Phylogenomic databases | |
| GeneTree | ENSGT00390000014792. |
| HOVERGEN | HBG097593. |
| OrthoDB | EOG4CG09S. |
Family and domain databases | |
| InterPro | IPR001651. Gastrin. IPR013152. Gastrin/cholecystokinin_CS. [Graphical view] |
| KO | K13768. |
| Pfam | PF00918. Gastrin. 1 hit. [Graphical view] |
| SMART | SM00029. GASTRIN. 1 hit. [Graphical view] |
| PROSITE | PS00259. GASTRIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GAST_PIG | ||||||||
| Accession | Primary (citable) accession number: P01351 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with