P68000 (COLI_BALBO) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 26.
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: Pro-opiomelanocortin Short name=POMC Alternative name(s): Corticotropin-lipotropin Cleaved into the following 3 chains:
| ||
| Gene names |
| ||
| Organism | Balaenoptera borealis (Sei whale) (Pollack whale) | ||
| Taxonomic identifier | 9768 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Cetacea › Mysticeti › Balaenopteridae › Balaenoptera |
Protein attributes
| Sequence length | 39 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 | ACTH stimulates the adrenal glands to release cortisol. MSH (melanocyte-stimulating hormone) increases the pigmentation of skin by increasing melanin production in melanocytes. Beta-endorphin and Met-enkephalin are endogenous opiates. |
| Subcellular location | |
| Tissue specificity | ACTH and MSH are produced by the pituitary gland. |
| Sequence similarities | Belongs to the POMC family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Molecular function | Hormone |
| PTM | Amidation Cleavage on pair of basic residues Phosphoprotein |
| Technical term | 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Peptide | 1 – 39 | 39 | Corticotropin | PRO_0000024937 | |||||
| Peptide | 1 – 13 | 13 | Melanotropin alpha | PRO_0000024938 | |||||
| Peptide | 19 – 39 | 21 | Corticotropin-like intermediary peptide | PRO_0000024939 | |||||
Amino acid modifications | |||||||||
| Modified residue | 13 | 1 | Valine amide | ||||||
| Modified residue | 31 | 1 | Phosphoserine By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
| Non-terminal residue | 39 | 1 | |||||||
Sequences
References
| [1] | "Amino acid sequence of corticotropins from seiwhale (Balaenoptera borealis) and pinwhale (Balaenoptera physalus)." Pankov Y.A., Nikolaeva O.P., Elizarova G.P. Biokhimiia 42:2044-2050(1977) [PubMed: 201308] [Abstract] Cited for: PROTEIN SEQUENCE. |
Cross-references
Sequence databases | |
|---|---|
| PIR | PN0127. |
3D structure databases | |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P68000. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR001941. Mcortin_ACTH. IPR013531. Mcrtin_ACTH_cent. [Graphical view] |
| PANTHER | PTHR11416. Mcortin_ACTH. 1 hit. |
| Pfam | PF00976. ACTH_domain. 1 hit. [Graphical view] |
| PRINTS | PR00383. MELANOCORTIN. |
| ProtoNet | Search... |
Entry information
| Entry name | COLI_BALBO | ||||||||
| Accession | Primary (citable) accession number: P68000 Secondary accession number(s): P01195 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with