Q6IE52 (MUG2_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 60.
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: Murinoglobulin-2 | ||
| 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 | 1448 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 | A proteinase activates the inhibitor by specific proteolysis in the bait region, which, by an unknown mechanism leads to reaction at the cysteinyl-glutamyl internal thiol ester site and to a conformational change, whereby the proteinase is trapped and/or covalently bound to the inhibitor. While in the tetrameric proteinase inhibitors steric inhibition is sufficiently strong, monomeric forms need a covalent linkage between the activated glutamyl residue of the original thiol ester and a terminal amino group of a lysine or another nucleophilic group on the proteinase, for inhibition to be effective. |
| Subunit structure | Monomer By similarity. UniProtKB P14046 |
| Subcellular location | Secreted By similarity. |
| Sequence similarities | Belongs to the protease inhibitor I39 (alpha-2-macroglobulin) family. [View classification] |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Bait region Signal |
| Molecular function | Protease inhibitor Serine protease inhibitor |
| PTM | Disulfide bond Glycoprotein Thioester bond |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | negative regulation of endopeptidase activity Inferred from electronic annotation. Source: GOC |
| Cellular_component | extracellular space Inferred from electronic annotation. Source: InterPro |
| Molecular_function | serine-type endopeptidase inhibitor 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 – 24 | 24 | Potential | ||||||||
| Chain | 25 – 1448 | 1424 | Murinoglobulin-2 | PRO_0000271252 | |||||||
Regions | |||||||||||
| Region | 678 – 709 | 32 | Bait region By similarity UniProtKB P28665 | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 55 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 295 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 315 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 387 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 502 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 751 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 846 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 968 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1114 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1285 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1398 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 48 ↔ 86 | By similarity UniProtKB P01023 | |||||||||
| Disulfide bond | 245 ↔ 277 | By similarity UniProtKB P01023 | |||||||||
| Disulfide bond | 263 ↔ 289 | By similarity UniProtKB P01023 | |||||||||
| Disulfide bond | 462 ↔ 556 | By similarity UniProtKB P01023 | |||||||||
| Disulfide bond | 588 ↔ 748 | By similarity UniProtKB P01023 | |||||||||
| Disulfide bond | 636 ↔ 681 | By similarity UniProtKB P01023 | |||||||||
| Disulfide bond | 824 ↔ 860 | By similarity UniProtKB P01023 | |||||||||
| Disulfide bond | 898 ↔ 1295 | By similarity UniProtKB P01023 | |||||||||
| Disulfide bond | 1056 ↔ 1101 | By similarity UniProtKB P01023 | |||||||||
| Disulfide bond | 1326 ↔ 1441 | By similarity UniProtKB P01023 | |||||||||
| Cross-link | 949 ↔ 952 | Isoglutamyl cysteine thioester (Cys-Gln) By similarity UniProtKB P01023 | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. Collins F.S.Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway. |
| [2] | Lubec G., Kang S.U. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 873-878, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain. |
| [3] | "A genomic analysis of rat proteases and protease inhibitors." Puente X.S., Lopez-Otin C. Genome Res. 14:609-622(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AC113675 Genomic DNA. No translation available. BN000341 mRNA. Translation: CAE51393.1. |
| IPI | IPI00476749. |
| RefSeq | NP_001002826.1. NM_001002826.1. |
| UniGene | Rn.198690. |
3D structure databases | |
| ProteinModelPortal | Q6IE52. |
| SMR | Q6IE52. Positions 125-221, 1315-1447. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10116.ENSRNOP00000040516. |
Proteomic databases | |
| PRIDE | Q6IE52. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 408236. |
| KEGG | rno:408236. |
| UCSC | RGD:1302962. rat. |
Organism-specific databases | |
| CTD | 17837. |
| RGD | 1302962. Mug2. |
Phylogenomic databases | |
| HOGENOM | HOG000220939. |
| HOVERGEN | HBG000039. |
Gene expression databases | |
| ArrayExpress | Q6IE52. |
| Genevestigator | Q6IE52. |
Family and domain databases | |
| Gene3D | 2.60.40.690. 1 hit. |
| InterPro | IPR009048. A-macroglobulin_rcpt-bd. IPR011626. A2M_comp. IPR002890. A2M_N. IPR011625. A2M_N_2. IPR001599. Macroglobln_a2. IPR019742. MacrogloblnA2_CS. IPR019565. MacrogloblnA2_thiol-ester-bond. IPR008930. Terpenoid_cyclase/PrenylTrfase. IPR010916. TonB_box_CS. [Graphical view] |
| Pfam | PF00207. A2M. 1 hit. PF07678. A2M_comp. 1 hit. PF01835. A2M_N. 1 hit. PF07703. A2M_N_2. 1 hit. PF07677. A2M_recep. 1 hit. PF10569. Thiol-ester_cl. 1 hit. [Graphical view] |
| SUPFAM | SSF49410. AM_receptor_bind. 1 hit. SSF48239. Terp_cyc_toroid. 1 hit. |
| PROSITE | PS00477. ALPHA_2_MACROGLOBULIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 696498. |
Entry information
| Entry name | MUG2_RAT | ||||||||
| Accession | Primary (citable) accession number: Q6IE52 | ||||||||
| 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
