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P06238

- A2MG_RAT

UniProt

P06238 - A2MG_RAT

Protein

Alpha-2-macroglobulin

Gene

A2m

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (12 Dec 2006)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. endopeptidase inhibitor activity Source: RGD
    2. peptidase inhibitor activity Source: RGD
    3. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

    GO - Biological processi

    1. acute-phase response Source: RGD
    2. inflammatory response Source: RGD
    3. negative regulation of endopeptidase activity Source: RGD
    4. response to carbon dioxide Source: RGD
    5. response to glucocorticoid Source: RGD
    6. response to nutrient Source: RGD
    7. response to wounding Source: RGD

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Keywords - Biological processi

    Acute phase

    Enzyme and pathway databases

    ReactomeiREACT_199178. Degradation of the extracellular matrix.

    Protein family/group databases

    MEROPSiI39.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-2-macroglobulin
    Short name:
    Alpha-2-M
    Gene namesi
    Name:A2m
    Synonyms:A2m1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 4

    Organism-specific databases

    RGDi2004. A2m.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: InterPro

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Add
    BLAST
    Chaini28 – 14721445Alpha-2-macroglobulinPRO_0000000058Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi52 ↔ 90By similarity
    Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi254 ↔ 302By similarity
    Disulfide bondi272 ↔ 290By similarity
    Disulfide bondi281 – 281Interchain (with C-434)By similarity
    Glycosylationi399 – 3991N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi434 – 434Interchain (with C-281)By similarity
    Disulfide bondi473 ↔ 566By similarity
    Disulfide bondi598 ↔ 769By similarity
    Disulfide bondi647 ↔ 694By similarity
    Glycosylationi651 – 6511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi772 – 7721N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi819 ↔ 847By similarity
    Disulfide bondi845 ↔ 881By similarity
    Glycosylationi867 – 8671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi919 ↔ 1319By similarity
    Cross-linki970 ↔ 973Isoglutamyl cysteine thioester (Cys-Gln)By similarity
    Glycosylationi989 – 9891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1077 ↔ 1125By similarity
    Disulfide bondi1350 ↔ 1465By similarity
    Glycosylationi1364 – 13641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1422 – 14221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1426 – 14261N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Thioester bond

    Proteomic databases

    PaxDbiP06238.
    PRIDEiP06238.

    Expressioni

    Tissue specificityi

    Highest constitutive expression in ovary. Low level in testis, uterus and non-acute phase liver. Protein found in plasma.1 Publication

    Inductioni

    By inflammatory stimulus in liver. The level of this protein increases during acute phase, then decreases again.1 Publication

    Gene expression databases

    GenevestigatoriP06238.

    Interactioni

    Subunit structurei

    Homotetramer; disulfide-linked.

    Structurei

    3D structure databases

    ProteinModelPortaliP06238.
    SMRiP06238. Positions 129-230, 1336-1472.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni620 – 750131Bait regionAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Bait region, Signal

    Phylogenomic databases

    eggNOGiCOG2373.
    GeneTreeiENSGT00740000115177.
    HOGENOMiHOG000220939.
    HOVERGENiHBG000039.
    KOiK03910.
    OMAiQTVQAHY.
    OrthoDBiEOG7DJSKB.
    PhylomeDBiP06238.
    TreeFamiTF313285.

    Family and domain databases

    Gene3Di1.50.10.20. 1 hit.
    2.60.40.690. 1 hit.
    InterProiIPR009048. A-macroglobulin_rcpt-bd.
    IPR011626. A2M_comp.
    IPR002890. A2M_N.
    IPR011625. A2M_N_2.
    IPR014756. Ig_E-set.
    IPR001599. Macroglobln_a2.
    IPR019742. MacrogloblnA2_CS.
    IPR019565. MacrogloblnA2_thiol-ester-bond.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view]
    PfamiPF00207. 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]
    SUPFAMiSSF48239. SSF48239. 1 hit.
    SSF49410. SSF49410. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P06238-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKHRLRSLA LLPLLLRLLL LLLPTDASAP QKPIYMVMVP SLLHAGTPEK     50
    ACFLFSHLNE TVAVRVSLES VRGNQSLFTD LVVDKDLFHC TSFTVPQSSS 100
    DEVMFFTVQV KGATHEFRRR STVLVKKKES LVFAQTDKPI YKPGQTVRFR 150
    VVSLDESFHP LNELIPLLYI QDPKNNRIAQ WQNFNLEGGL KQLSFPLSSE 200
    PTQGSYKVVI RTESGRTVEH PFSVEEFVLP KFEVRVTVPE TITILEEEMN 250
    VSVCGIYTYG KPVPGRVTVN ICRKYSNPSN CFGEESVAFC EKLSQQLDGR 300
    GCFSQLVKTK SFQLKRQEYE MQLDVHAKIQ EEGTGVEETG KGLTKITRTI 350
    TKLSFVNVDS HFRQGIPFVG QVLLVDGRGT PIPYETIFIG ADEANLYINT 400
    TTDKHGLARF SINTDDIMGT SLTVRAKYKD SNACYGFRWL TEENVEAWHT 450
    AYAVFSPSRS FLHLESLPDK LRCDQTLEVQ AHYILNGEAM QELKELVFYY 500
    LMMAKGGIVR AGTHVLPLKQ GQMRGHFSIL ISMETDLAPV ARLVLYAILP 550
    NGEVVGDTAK YEIENCLANK VDLVFRPNSG LPATRALLSV MASPQSLCGL 600
    RAVDQSVLLM KPETELSASL IYDLLPVKDL TGFPQGADQR EEDTNGCVKQ 650
    NDTYINGILY SPVQNTNEED MYGFLKDMGL KVFTNSNIRK PKVCERLRDN 700
    KGIPAAYHLV SQSHMDAFLE SSESPTETRR SYFPETWIWD LVVVDSAGVA 750
    EVEVTVPDTI TEWKAGAFCL SNDTGLGLSP VVQFQAFQPF FVELTMPYSV 800
    IRGEAFTLKA TVLNYLPTCI RVAVQLEASP DFLAAPEEKE QRSHCICMNQ 850
    RHTASWAVIP KSLGNVNFTV SAEALNSKEL CGNEVPVVPE QGKKDTIIKS 900
    LLVEPEGLEN EVTFNSLLCP MGAEVSELIA LKLPSDVVEE SARASVTVLG 950
    DILGSAMQNT QDLLKMPYGC GEQNMVLFAP NIYVLDYLNE TQQLTQEIKT 1000
    KAIAYLNTGY QRQLNYKHRD GSYSTFGDKP GRNHANTWLT AFVLKSFAQA 1050
    RKYIFIDEVH ITQALLWLSQ QQKDNGCFRS SGSLLNNAMK GGVEDEVTLS 1100
    AYITIALLEM SLPVTHPVVR NALFCLDTAW KSARGGAGGS HVYTKALLAY 1150
    AFALAGNQDT KKEILKSLDE EAVKEEDSVH WTRPQKPSVS VALWYQPQAP 1200
    SAEVEMTAYV LLAYLTTEPA PTQEDLTAAM LIVKWLTKQQ NSHGGFSSTQ 1250
    DTVVALHALS KYGSATFTRA KKAAQVTIHS SGTFSTKFQV NNNNQLLLQR 1300
    VTLPTVPGDY TVKVTGEGCV YLQTSLKYSV LPREEEFPFT VVVQTLPGTC 1350
    EDPKAHTSFQ ISLNISYTGS RSESNMAIAD VKMVSGFIPL KPTVKMLERS 1400
    VHVSRTEVSN NHVLIYLDKV SNQTVNLSFT VQQDIPIRDL KPAVVKVYDY 1450
    YEKDEFAVAK YSAPCSTDYG NA 1472
    Length:1,472
    Mass (Da):163,785
    Last modified:December 12, 2006 - v2
    Checksum:iBFD63B8A4F6A2632
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231L → V in CAA32164. (PubMed:2466233)Curated
    Sequence conflicti72 – 721R → H in AAA40636. (PubMed:2432068)Curated
    Sequence conflicti72 – 721R → H in CAA32164. (PubMed:2466233)Curated
    Sequence conflicti103 – 1031V → L in AAA40636. (PubMed:2432068)Curated
    Sequence conflicti103 – 1031V → L in CAA32164. (PubMed:2466233)Curated
    Sequence conflicti120 – 1201R → Q in AAA40636. (PubMed:2432068)Curated
    Sequence conflicti120 – 1201R → Q in CAA32164. (PubMed:2466233)Curated
    Sequence conflicti490 – 4901M → L in AAA40638. (PubMed:2414291)Curated
    Sequence conflicti1025 – 10251T → A in AAA40636. (PubMed:2432068)Curated
    Sequence conflicti1192 – 11921A → G in AAA40636. (PubMed:2432068)Curated
    Sequence conflicti1200 – 12001P → T in AAA40636. (PubMed:2432068)Curated
    Sequence conflicti1279 – 12791H → R in AAA40636. (PubMed:2432068)Curated
    Sequence conflicti1340 – 13401T → A in AAA40636. (PubMed:2432068)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02635 mRNA. Translation: AAA40636.1.
    BC098922 mRNA. Translation: AAH98922.1.
    X13983, X13984, X13985 Genomic DNA. Translation: CAA32164.1.
    M11792 mRNA. Translation: AAA40637.1.
    M11793 mRNA. Translation: AAA40638.1.
    PIRiA26122.
    RefSeqiNP_036620.2. NM_012488.2.
    XP_003749876.1. XM_003749828.2.
    UniGeneiRn.225884.

    Genome annotation databases

    EnsembliENSRNOT00000019346; ENSRNOP00000019346; ENSRNOG00000028896.
    GeneIDi100911545.
    24153.
    KEGGirno:100911545.
    rno:24153.
    UCSCiRGD:2004. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02635 mRNA. Translation: AAA40636.1 .
    BC098922 mRNA. Translation: AAH98922.1 .
    X13983 , X13984 , X13985 Genomic DNA. Translation: CAA32164.1 .
    M11792 mRNA. Translation: AAA40637.1 .
    M11793 mRNA. Translation: AAA40638.1 .
    PIRi A26122.
    RefSeqi NP_036620.2. NM_012488.2.
    XP_003749876.1. XM_003749828.2.
    UniGenei Rn.225884.

    3D structure databases

    ProteinModelPortali P06238.
    SMRi P06238. Positions 129-230, 1336-1472.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi I39.001.

    Proteomic databases

    PaxDbi P06238.
    PRIDEi P06238.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000019346 ; ENSRNOP00000019346 ; ENSRNOG00000028896 .
    GeneIDi 100911545.
    24153.
    KEGGi rno:100911545.
    rno:24153.
    UCSCi RGD:2004. rat.

    Organism-specific databases

    CTDi 2.
    RGDi 2004. A2m.

    Phylogenomic databases

    eggNOGi COG2373.
    GeneTreei ENSGT00740000115177.
    HOGENOMi HOG000220939.
    HOVERGENi HBG000039.
    KOi K03910.
    OMAi QTVQAHY.
    OrthoDBi EOG7DJSKB.
    PhylomeDBi P06238.
    TreeFami TF313285.

    Enzyme and pathway databases

    Reactomei REACT_199178. Degradation of the extracellular matrix.

    Miscellaneous databases

    NextBioi 602439.

    Gene expression databases

    Genevestigatori P06238.

    Family and domain databases

    Gene3Di 1.50.10.20. 1 hit.
    2.60.40.690. 1 hit.
    InterProi IPR009048. A-macroglobulin_rcpt-bd.
    IPR011626. A2M_comp.
    IPR002890. A2M_N.
    IPR011625. A2M_N_2.
    IPR014756. Ig_E-set.
    IPR001599. Macroglobln_a2.
    IPR019742. MacrogloblnA2_CS.
    IPR019565. MacrogloblnA2_thiol-ester-bond.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view ]
    Pfami 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 ]
    SUPFAMi SSF48239. SSF48239. 1 hit.
    SSF49410. SSF49410. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of rat liver alpha 2-macroglobulin and acute phase control of its messenger RNA."
      Gehring M.R., Shiels B.R., Northemann W., de Bruijn M.H.L., Kan C.-C., Chain A.C., Noonan D.J., Fey G.H.
      J. Biol. Chem. 262:446-454(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
      Tissue: Liver.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Placenta.
    3. "Identification of the promoter sequences involved in the interleukin-6 dependent expression of the rat alpha 2-macroglobulin gene."
      Kunz D., Zimmermann R., Heisig M., Heinrich P.C.
      Nucleic Acids Res. 17:1121-1138(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-164.
      Strain: Wistar.
      Tissue: Liver.
    4. "Molecular cloning of DNA complementary to rat alpha 2-macroglobulin mRNA."
      Hayashida K., Okubo H., Noguchi M., Yoshida H., Kangawa K., Matsuo H., Sakaki Y.
      J. Biol. Chem. 260:14224-14229(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 178-227 AND 420-526.
    5. "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: TISSUE SPECIFICITY.
      Strain: Fischer 344.
      Tissue: Liver.

    Entry informationi

    Entry nameiA2MG_RAT
    AccessioniPrimary (citable) accession number: P06238
    Secondary accession number(s): Q4FZY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: December 12, 2006
    Last modified: October 1, 2014
    This is version 121 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3