Q03238 (GRAM_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 93.
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: Granzyme M EC=3.4.21.- Alternative name(s): Met-ase Natural killer cell granular protease RNK-Met-1 | ||
| Gene names |
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| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 258 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 | Cleaves peptide substrates after methionine, leucine, and norleucine. Physiological substrates include EZR, alpha-tubulins and the apoptosis inhibitor BIRC5/Survivin. Promotes caspase activation and subsequent apoptosis of target cells By similarity. |
| Subcellular location | Secreted. Cytoplasmic granule. Note: Granules of large granular lymphocytes. |
| Sequence similarities | Belongs to the peptidase S1 family. Granzyme subfamily. Contains 1 peptidase S1 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Apoptosis Cytolysis Immunity Innate immunity |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Disulfide bond Glycoprotein Zymogen |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cytolysisInferred from electronic annotation. Source: UniProtKB-KW innate immune responseInferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro serine-type peptidase activityInferred from direct assay Ref.1. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | ‹1 – ? | Potential | |||||||||
| Propeptide | ? – 20 | Activation peptide | PRO_0000027423 | ||||||||
| Chain | 21 – 258 | 238 | Granzyme M | PRO_0000027424 | |||||||
Regions | |||||||||||
| Domain | 21 – 250 | 230 | Peptidase S1 | ||||||||
Sites | |||||||||||
| Active site | 61 | 1 | Charge relay system By similarity | ||||||||
| Active site | 107 | 1 | Charge relay system By similarity | ||||||||
| Active site | 204 | 1 | Charge relay system By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 174 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 225 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 46 ↔ 62 | By similarity | |||||||||
| Disulfide bond | 142 ↔ 210 | By similarity | |||||||||
| Disulfide bond | 173 ↔ 189 | By similarity | |||||||||
| Disulfide bond | 200 ↔ 226 | By similarity | |||||||||
Experimental info | |||||||||||
| Non-terminal residue | 1 | 1 | |||||||||
Sequences
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References
| [1] | "Purification and cloning of a novel serine protease, RNK-Met-1, from the granules of a rat natural killer cell leukemia." Smyth M.J., Wiltrout T., Trapani J.A., Ottaway K.S., Sowder R., Henderson L.E., Kam C.-M., Powers J.C., Young H.A., Sayers T.J. J. Biol. Chem. 267:24418-24425(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-44. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L05175 mRNA. Translation: AAA42056.1. |
| IPI | IPI00365967. |
| PIR | A45161. |
| UniGene | Rn.9838. |
3D structure databases | |
| ProteinModelPortal | Q03238. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q03238. 1 interaction. |
| STRING | 10116.ENSRNOP00000011086. |
Protein family/group databases | |
| MEROPS | S01.139. |
Proteomic databases | |
| PRIDE | Q03238. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| UCSC | RGD:620022. rat. |
Organism-specific databases | |
| RGD | 620022. Gzmm. |
Phylogenomic databases | |
| eggNOG | COG5640. |
| HOGENOM | HOG000251820. |
| HOVERGEN | HBG013304. |
| InParanoid | Q03238. |
| OrthoDB | EOG4TMR2V. |
Gene expression databases | |
| Genevestigator | Q03238. |
| GermOnline | ENSRNOG00000030530. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR001254. Peptidase_S1. IPR018114. Peptidase_S1_AS. IPR001314. Peptidase_S1A. IPR009003. Trypsin-like_Pept_dom. [Graphical view] |
| Pfam | PF00089. Trypsin. 1 hit. [Graphical view] |
| PRINTS | PR00722. CHYMOTRYPSIN. |
| SMART | SM00020. Tryp_SPc. 1 hit. [Graphical view] |
| SUPFAM | SSF50494. Pept_Ser_Cys. 1 hit. |
| PROSITE | PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GRAM_RAT | ||||||||
| Accession | Primary (citable) accession number: Q03238 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
