SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P06238

- A2MG_RAT

UniProt

P06238 - A2MG_RAT

(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)

Protein

Alpha-2-macroglobulin

Gene
A2m, A2m1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

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.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231L → V in CAA32164. 1 Publication
Sequence conflicti72 – 721R → H in AAA40636. 1 Publication
Sequence conflicti72 – 721R → H in CAA32164. 1 Publication
Sequence conflicti103 – 1031V → L in AAA40636. 1 Publication
Sequence conflicti103 – 1031V → L in CAA32164. 1 Publication
Sequence conflicti120 – 1201R → Q in AAA40636. 1 Publication
Sequence conflicti120 – 1201R → Q in CAA32164. 1 Publication
Sequence conflicti490 – 4901M → L in AAA40638. 1 Publication
Sequence conflicti1025 – 10251T → A in AAA40636. 1 Publication
Sequence conflicti1192 – 11921A → G in AAA40636. 1 Publication
Sequence conflicti1200 – 12001P → T in AAA40636. 1 Publication
Sequence conflicti1279 – 12791H → R in AAA40636. 1 Publication
Sequence conflicti1340 – 13401T → A in AAA40636. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 120 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

Similar proteinsi