Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q61838

- A2M_MOUSE

UniProt

Q61838 - A2M_MOUSE

Protein

Alpha-2-macroglobulin

Gene

A2m

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 3 (28 Jun 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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: MGI
    2. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

    GO - Biological processi

    1. embryo implantation Source: MGI
    2. negative regulation of endopeptidase activity Source: GOC

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-2-macroglobulin
    Short name:
    Alpha-2-M
    Alternative name(s):
    Pregnancy zone protein
    Cleaved into the following 2 chains:
    Gene namesi
    Name:A2m
    Synonyms:Pzp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:87854. Pzp.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: MGI
    2. extracellular space Source: InterPro

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 14951471Alpha-2-macroglobulinPRO_0000338413Add
    BLAST
    Chaini25 – 12391215Alpha-2-macroglobulin 165 kDa subunitPRO_0000000056Add
    BLAST
    Chaini1240 – 1495256Alpha-2-macroglobulin 35 kDa subunitPRO_0000000057Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi48 ↔ 86By similarity
    Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi157 – 1571N-linked (GlcNAc...)2 Publications
    Disulfide bondi249 ↔ 298By similarity
    Disulfide bondi267 ↔ 286By similarity
    Disulfide bondi277 – 277Interchain (with C-430)By similarity
    Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi405 – 4051N-linked (GlcNAc...)1 Publication
    Glycosylationi412 – 4121N-linked (GlcNAc...)1 Publication
    Disulfide bondi430 – 430Interchain (with C-277)By similarity
    Disulfide bondi469 ↔ 562By similarity
    Glycosylationi568 – 5681N-linked (GlcNAc...)1 Publication
    Disulfide bondi594 ↔ 783By similarity
    Disulfide bondi642 ↔ 689By similarity
    Disulfide bondi833 ↔ 861By similarity
    Disulfide bondi859 ↔ 895By similarity
    Glycosylationi881 – 8811N-linked (GlcNAc...)1 Publication
    Disulfide bondi933 ↔ 1339By similarity
    Glycosylationi942 – 9421N-linked (GlcNAc...)Sequence Analysis
    Cross-linki984 ↔ 987Isoglutamyl cysteine thioester (Cys-Gln)By similarity
    Glycosylationi1003 – 10031N-linked (GlcNAc...)2 Publications
    Disulfide bondi1092 ↔ 1140By similarity
    Glycosylationi1385 – 13851N-linked (GlcNAc...)2 Publications
    Glycosylationi1443 – 14431N-linked (GlcNAc...)2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Thioester bond

    Proteomic databases

    MaxQBiQ61838.
    PaxDbiQ61838.
    PRIDEiQ61838.

    PTM databases

    PhosphoSiteiQ61838.

    Expressioni

    Tissue specificityi

    Highest expression in liver, medium expression in ovary, heart and stomach. Low expression in lung, kidney and uterus. Protein found in plasma.1 Publication

    Developmental stagei

    Contrary to the rat protein, which is an acute phase protein, this protein is always present at high levels in circulation.

    Gene expression databases

    BgeeiQ61838.
    CleanExiMM_A2M.
    MM_PZP.
    GenevestigatoriQ61838.

    Interactioni

    Protein-protein interaction databases

    BioGridi197897. 2 interactions.
    IntActiQ61838. 6 interactions.
    MINTiMINT-1846187.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61838.
    SMRiQ61838. Positions 124-225, 1357-1486.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni686 – 74459Bait regionAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Bait region, Signal

    Phylogenomic databases

    eggNOGiCOG2373.
    GeneTreeiENSGT00740000115177.
    HOGENOMiHOG000220939.
    HOVERGENiHBG000039.

    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.

    Q61838-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRRNQLPTPA FLLLFLLLPR DATTATAKPQ YVVLVPSEVY SGVPEKACVS     50
    LNHVNETVML SLTLEYAMQQ TKLLTDQAVD KDSFYCSPFT ISGSPLPYTF 100
    ITVEIKGPTQ RFIKKKSIQI IKAESPVFVQ TDKPIYKPGQ IVKFRVVSVD 150
    ISFRPLNETF PVVYIETPKR NRIFQWQNIH LAGGLHQLSF PLSVEPALGI 200
    YKVVVQKDSG KKIEHSFEVK EYVLPKFEVI IKMQKTMAFL EEELPITACG 250
    VYTYGKPVPG LVTLRVCRKY SRYRSTCHNQ NSMSICEEFS QQADDKGCFR 300
    QVVKTKVFQL RQKGHDMKIE VEAKIKEEGT GIELTGIGSC EIANALSKLK 350
    FTKVNTNYRP GLPFSGQVLL VDEKGKPIPN KNITSVVSPL GYLSIFTTDE 400
    HGLANISIDT SNFTAPFLRV VVTYKQNHVC YDNWWLDEFH TQADHSATLV 450
    FSPSQSYIQL ELVFGTLACG QTQEIRIHYL LNEDIMKNEK DLTFYYLIKA 500
    RGSIFNLGSH VLSLEQGNMK GVFSLPIQVE PGMAPEAQLL IYAILPNEEL 550
    VADAQNFEIE KCFANKVNLS FPSAQSLPAS DTHLKVKAAP LSLCALTAVD 600
    QSVLLLKPEA KLSPQSIYNL LPGKTVQGAF FGVPVYKDHE NCISGEDITH 650
    NGIVYTPKHS LGDNDAHSIF QSVGINIFTN SKIHKPRFCQ EFQHYPAMGG 700
    VAPQALAVAA SGPGSSFRAM GVPMMGLDYS DEINQVVEVR ETVRKYFPET 750
    WIWDLVPLDV SGDGELAVKV PDTITEWKAS AFCLSGTTGL GLSSTISLQA 800
    FQPFFLELTL PYSVVRGEAF TLKATVLNYM SHCIQIRVDL EISPDFLAVP 850
    VGGHENSHCI CGNERKTVSW AVTPKSLGEV NFTATAEALQ SPELCGNKLT 900
    EVPALVHKDT VVKSVIVEPE GIEKEQTYNT LLCPQDTELQ DNWSLELPPN 950
    VVEGSARATH SVLGDILGSA MQNLQNLLQM PYGCGEQNMV LFVPNIYVLN 1000
    YLNETQQLTE AIKSKAINYL ISGYQRQLNY QHSDGSYSTF GNHGGGNTPG 1050
    NTWLTAFVLK AFAQAQSHIF IEKTHITNAF NWLSMKQKEN GCFQQSGYLL 1100
    NNAMKGGVDD EVTLSAYITI ALLEMPLPVT HSAVRNALFC LETAWASISQ 1150
    SQESHVYTKA LLAYAFALAG NKAKRSELLE SLNKDAVKEE DSLHWQRPGD 1200
    VQKVKALSFY QPRAPSAEVE MTAYVLLAYL TSESSRPTRD LSSSDLSTAS 1250
    KIVKWISKQQ NSHGGFSSTQ DTVVALQALS KYGAATFTRS QKEVLVTIES 1300
    SGTFSKTFHV NSGNRLLLQE VRLPDLPGNY VTKGSGSGCV YLQTSLKYNI 1350
    LPVADGKAPF ALQVNTLPLN FDKAGDHRTF QIRINVSYTG ERPSSNMVIV 1400
    DVKMVSGFIP MKPSVKKLQD QPNIQRTEVN TNHVLIYIEK LTNQTLGFSF 1450
    AVEQDIPVKN LKPAPIKVYD YYETDEFTVE EYSAPFSDGS EQGNA 1495
    Length:1,495
    Mass (Da):165,853
    Last modified:June 28, 2011 - v3
    Checksum:i5D060D6C639DF3BC
    GO

    Sequence cautioni

    The sequence AAA39508.1 differs from that shown. Reason: Frameshift at positions 41 and 47.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti43 – 431V → I in AAA39508. (PubMed:1280217)Curated
    Sequence conflicti43 – 431V → I in AAH57983. (PubMed:15489334)Curated
    Sequence conflicti43 – 431V → I in AAA87890. (PubMed:7528166)Curated
    Sequence conflicti91 – 911I → V in AAA87890. (PubMed:7528166)Curated
    Sequence conflicti142 – 1443VKF → GII in AAA87890. (PubMed:7528166)Curated
    Sequence conflicti160 – 1612FP → VS in AAA87890. (PubMed:7528166)Curated
    Sequence conflicti287 – 2871E → A in AAA39508. (PubMed:1280217)Curated
    Sequence conflicti300 – 3001R → S in AAA39508. (PubMed:1280217)Curated
    Sequence conflicti311 – 3111R → S in AAA39508. (PubMed:1280217)Curated
    Sequence conflicti491 – 4911D → T in AAA39508. (PubMed:1280217)Curated
    Sequence conflicti505 – 5051F → G in AAA39508. (PubMed:1280217)Curated
    Sequence conflicti541 – 5411I → V in AAH57983. (PubMed:15489334)Curated
    Sequence conflicti792 – 7921L → S in AAA39508. (PubMed:1280217)Curated
    Sequence conflicti884 – 8841A → R in AAA39508. (PubMed:1280217)Curated
    Sequence conflicti890 – 8923QSP → ESQ in AAA39508. (PubMed:1280217)Curated
    Sequence conflicti943 – 9431W → S in AAA39508. (PubMed:1280217)Curated
    Sequence conflicti1133 – 11331A → V in AAH57983. (PubMed:15489334)Curated
    Sequence conflicti1263 – 12686HGGFSS → DGGLLL in AAA39508. (PubMed:1280217)Curated
    Sequence conflicti1284 – 12841A → S in AAA39508. (PubMed:1280217)Curated
    Sequence conflicti1298 – 12992IE → SR in AAA39508. (PubMed:1280217)Curated
    Sequence conflicti1375 – 13751G → E in AAA39508. (PubMed:1280217)Curated
    Sequence conflicti1417 – 14171K → R in AAA39508. (PubMed:1280217)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93264 mRNA. Translation: AAA39508.1. Frameshift.
    AC123060 Genomic DNA. No translation available.
    BC057983 mRNA. Translation: AAH57983.1.
    U06977 Genomic DNA. Translation: AAA87890.1.
    CCDSiCCDS39650.1.
    PIRiS27001.
    RefSeqiNP_031402.3. NM_007376.4.
    UniGeneiMm.260144.

    Genome annotation databases

    EnsembliENSMUST00000112132; ENSMUSP00000107760; ENSMUSG00000030359.
    GeneIDi11287.
    KEGGimmu:11287.
    UCSCiuc009eef.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93264 mRNA. Translation: AAA39508.1 . Frameshift.
    AC123060 Genomic DNA. No translation available.
    BC057983 mRNA. Translation: AAH57983.1 .
    U06977 Genomic DNA. Translation: AAA87890.1 .
    CCDSi CCDS39650.1.
    PIRi S27001.
    RefSeqi NP_031402.3. NM_007376.4.
    UniGenei Mm.260144.

    3D structure databases

    ProteinModelPortali Q61838.
    SMRi Q61838. Positions 124-225, 1357-1486.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 197897. 2 interactions.
    IntActi Q61838. 6 interactions.
    MINTi MINT-1846187.

    PTM databases

    PhosphoSitei Q61838.

    Proteomic databases

    MaxQBi Q61838.
    PaxDbi Q61838.
    PRIDEi Q61838.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000112132 ; ENSMUSP00000107760 ; ENSMUSG00000030359 .
    GeneIDi 11287.
    KEGGi mmu:11287.
    UCSCi uc009eef.1. mouse.

    Organism-specific databases

    CTDi 5858.
    MGIi MGI:87854. Pzp.

    Phylogenomic databases

    eggNOGi COG2373.
    GeneTreei ENSGT00740000115177.
    HOGENOMi HOG000220939.
    HOVERGENi HBG000039.

    Miscellaneous databases

    NextBioi 278574.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q61838.
    CleanExi MM_A2M.
    MM_PZP.
    Genevestigatori Q61838.

    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. "The primary sequence and the subunit structure of mouse alpha-2-macroglobulin, deduced from protein sequencing of the isolated subunits and from molecular cloning of the cDNA."
      van Leuven F., Torrekens S., Overbergh L., Lorent K., de Strooper B., van den Berghe H.
      Eur. J. Biochem. 210:319-327(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-44 AND 1240-1259.
      Tissue: Liver.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "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].
      Strain: FVB/N.
      Tissue: Liver.
    4. "Molecular cloning of the mouse gene coding for alpha 2-macroglobulin and targeting of the gene in embryonic stem cells."
      Umans L., Serneels L., Hilliker C., Stas L., Overbergh L., de Strooper B., van Leuven F., van den Berghe H.
      Genomics 22:519-529(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-161.
      Strain: 129/J.
    5. "Characterization of a murine alpha 2 macroglobulin gene expressed in reproductive and cardiovascular tissue."
      He H., McCartney D.J., Wei Q., Esadeg S., Zhang J., Foster R.A., Hayes M.A., Tayade C., Van Leuven F., Croy B.A.
      Biol. Reprod. 72:266-275(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
      Strain: C57BL/6.
      Tissue: Placenta.
    6. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
      Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
      J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-157; ASN-405; ASN-412; ASN-1003; ASN-1385 AND ASN-1443.
      Strain: C57BL/6.
      Tissue: Plasma.
    7. "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
      Bernhard O.K., Kapp E.A., Simpson R.J.
      J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-157; ASN-568; ASN-881; ASN-1003; ASN-1385 AND ASN-1443.
      Strain: C57BL/6.
      Tissue: Plasma.

    Entry informationi

    Entry nameiA2M_MOUSE
    AccessioniPrimary (citable) accession number: Q61838
    Secondary accession number(s): E9QPW0, Q60628, Q6PEM2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 122 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3