Q63041 (A1M_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 84.
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: Alpha-1-macroglobulin Short name=Alpha-1-M Alternative name(s): Alpha-1-macroglobulin 165 kDa subunit Cleaved into the following chain: | ||||
| Gene names |
| ||||
| 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 | 1500 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 | Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase By similarity. UniProtKB P01023 |
| Subunit structure | Homotetramer; disulfide-linked By similarity. UniProtKB P01023 |
| Subcellular location | |
| Tissue specificity | Widely expressed. Highest level in ovary, testis, uterus and prostate. Protein found in plasma. Ref.1 |
| 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 | 3D-structure 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 | Ref.1 | ||||||||||||||||||||||||||||||
| Chain | 25 – 1500 | 1476 | Alpha-1-macroglobulin Ref.1 | PRO_0000271403 | |||||||||||||||||||||||||||||
| Chain | 1245 – 1500 | 256 | Alpha-1-macroglobulin 45 kDa subunit Ref.1 | PRO_0000271404 | |||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||
| Region | 686 – 746 | 61 | Bait region By similarity UniProtKB P01023 | ||||||||||||||||||||||||||||||
| Region | 1360 – 1500 | 141 | Receptor-binding domain Ref.4 | ||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||
| Glycosylation | 55 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||
| Glycosylation | 61 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||
| Glycosylation | 157 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||
| Glycosylation | 382 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||
| Glycosylation | 412 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||
| Glycosylation | 568 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||
| Glycosylation | 883 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||
| Glycosylation | 944 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||
| Glycosylation | 1005 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||
| Glycosylation | 1390 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||
| Glycosylation | 1448 | 1 | N-linked (GlcNAc...) Potential | ||||||||||||||||||||||||||||||
| Disulfide bond | 48 ↔ 86 | By similarity UniProtKB P01023 | |||||||||||||||||||||||||||||||
| Disulfide bond | 249 ↔ 298 | By similarity UniProtKB P01023 | |||||||||||||||||||||||||||||||
| Disulfide bond | 267 ↔ 286 | By similarity UniProtKB P01023 | |||||||||||||||||||||||||||||||
| Disulfide bond | 277 | Interchain (with C-430) By similarity UniProtKB P01023 | |||||||||||||||||||||||||||||||
| Disulfide bond | 430 | Interchain (with C-277) By similarity UniProtKB P01023 | |||||||||||||||||||||||||||||||
| Disulfide bond | 469 ↔ 562 | By similarity UniProtKB P01023 | |||||||||||||||||||||||||||||||
| Disulfide bond | 594 ↔ 785 | By similarity UniProtKB P01023 | |||||||||||||||||||||||||||||||
| Disulfide bond | 642 ↔ 689 | By similarity UniProtKB P01023 | |||||||||||||||||||||||||||||||
| Disulfide bond | 835 ↔ 863 | By similarity UniProtKB P01023 | |||||||||||||||||||||||||||||||
| Disulfide bond | 861 ↔ 897 | By similarity UniProtKB P01023 | |||||||||||||||||||||||||||||||
| Disulfide bond | 935 ↔ 1344 | By similarity UniProtKB P01023 | |||||||||||||||||||||||||||||||
| Disulfide bond | 1094 ↔ 1142 | By similarity UniProtKB P01023 | |||||||||||||||||||||||||||||||
| Cross-link | 986 ↔ 989 | Isoglutamyl cysteine thioester (Cys-Gln) By similarity UniProtKB P01023 | |||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||
| Sequence conflict | 50 | 1 | H → A AA sequence Ref.1 | ||||||||||||||||||||||||||||||
| Sequence conflict | 918 | 1 | I → P AA sequence Ref.1 | ||||||||||||||||||||||||||||||
| Sequence conflict | 924 – 925 | 2 | IE → AT AA sequence Ref.1 | ||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||
| Beta strand | 1364 – 1375 | 12 | |||||||||||||||||||||||||||||||
| Turn | 1376 – 1378 | 3 | |||||||||||||||||||||||||||||||
| Beta strand | 1384 – 1393 | 10 | |||||||||||||||||||||||||||||||
| Beta strand | 1395 – 1399 | 5 | |||||||||||||||||||||||||||||||
| Beta strand | 1401 – 1408 | 8 | |||||||||||||||||||||||||||||||
| Beta strand | 1413 – 1415 | 3 | |||||||||||||||||||||||||||||||
| Helix | 1417 – 1421 | 5 | |||||||||||||||||||||||||||||||
| Helix | 1422 – 1425 | 4 | |||||||||||||||||||||||||||||||
| Beta strand | 1429 – 1435 | 7 | |||||||||||||||||||||||||||||||
| Beta strand | 1438 – 1444 | 7 | |||||||||||||||||||||||||||||||
| Beta strand | 1451 – 1461 | 11 | |||||||||||||||||||||||||||||||
| Beta strand | 1469 – 1477 | 9 | |||||||||||||||||||||||||||||||
| Beta strand | 1481 – 1487 | 7 | |||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Sequence of rat alpha 1-macroglobulin, a broad-range proteinase inhibitor from the alpha-macroglobulin-complement family." Eggertsen G., Hudson G., Shiels B., Reed D., Fey G.H. Mol. Biol. Med. 8:287-302(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-54; 724-743; 901-930 AND 1245-1269, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Strain: Fischer 344. Tissue: Liver. |
| [2] | "cDNA cloning and sequencing of rat alpha 1-macroglobulin." Warmegard B., Martin N., Johansson S. Biochemistry 31:2346-2352(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver. |
| [3] | Lubec G., Chen W.-Q. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1287-1294 AND 1321-1327, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus. |
| [4] | "Structure of a rat alpha 1-macroglobulin receptor-binding domain dimer." Xiao T., DeCamp D.L., Spran S.R. Protein Sci. 9:1889-1897(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1362-1495. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | M77183 mRNA. Translation: AAA40723.1. M84000 mRNA. Translation: AAA41591.1. | ||||||||||||
| IPI | IPI00326140. | ||||||||||||
| PIR | A42210. | ||||||||||||
| RefSeq | NP_665722.2. NM_145779.2. | ||||||||||||
| UniGene | Rn.11295. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q63041. | ||||||||||||
| SMR | Q63041. Positions 124-225, 1362-1495. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q63041. 1 interaction. | ||||||||||||
| STRING | 10116.ENSRNOP00000009467. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | Q63041. | ||||||||||||
| PRIDE | Q63041. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSRNOT00000009467; ENSRNOP00000009467; ENSRNOG00000006709. | ||||||||||||
| GeneID | 252922. | ||||||||||||
| KEGG | rno:252922. | ||||||||||||
| UCSC | RGD:628643. rat. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 5858. | ||||||||||||
| RGD | 628643. Pzp. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG2373. | ||||||||||||
| GeneTree | ENSGT00560000076685. | ||||||||||||
| HOGENOM | HOG000220939. | ||||||||||||
| HOVERGEN | HBG000039. | ||||||||||||
| InParanoid | Q63041. | ||||||||||||
| OMA | THITNAF. | ||||||||||||
| OrthoDB | EOG4DBTCV. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | Q63041. | ||||||||||||
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. [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 | |||||||||||||
| EvolutionaryTrace | Q63041. | ||||||||||||
| NextBio | 624079. | ||||||||||||
Entry information
| Entry name | A1M_RAT | ||||||||
| Accession | Primary (citable) accession number: Q63041 Secondary accession number(s): Q63332 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
