Alpha-2-macroglobulin precursor - Rattus norvegicus (Rat)

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P06238 (A2MG_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 111. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alpha-2-macroglobulin
Short name=Alpha-2-M

Gene names

Name:	A2m
Synonyms:	A2m1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1472 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Subunit structure	Homotetramer; disulfide-linked.
Subcellular location	Secreted.
Tissue specificity	Highest constitutive expression in ovary. Low level in testis, uterus and non-acute phase liver. Protein found in plasma. Ref.5
Induction	By inflammatory stimulus in liver. The level of this protein increases during acute phase, then decreases again. Ref.1
Sequence similarities	Belongs to the protease inhibitor I39 (alpha-2-macroglobulin) family. [View classification]

Ontologies

Keywords
Biological process	Acute phase
Cellular component	Secreted
Domain	Bait region Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Disulfide bond Glycoprotein Thioester bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acute-phase response Inferred from expression pattern PubMed 2468362. Source: RGD response to carbon dioxide Inferred from expression pattern PubMed 12042906. Source: RGD response to glucocorticoid stimulus Inferred from expression pattern PubMed 2436819. Source: RGD response to nutrient Inferred from expression pattern PubMed 9446838. Source: RGD
Cellular_component	extracellular space Inferred from electronic annotation. Source: InterPro
Molecular_function	endopeptidase inhibitor activity Non-traceable author statement. Source: UniProtKB receptor binding Traceable author statement PubMed 11839752. Source: RGD 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

27

Chain

1445

Alpha-2-macroglobulin

PRO_0000000058

Regions

Region

131

Bait region

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Disulfide bond

By similarity

Disulfide bond

By similarity

Disulfide bond

By similarity

Disulfide bond

Interchain (with C-434) By similarity

Disulfide bond

Interchain (with C-281) By similarity

Disulfide bond

By similarity

Disulfide bond

By similarity

Disulfide bond

By similarity

Disulfide bond

By similarity

Disulfide bond

By similarity

Disulfide bond

By similarity

Disulfide bond

By similarity

Disulfide bond

By similarity

Cross-link

Isoglutamyl cysteine thioester (Cys-Gln) By similarity

Experimental info

Sequence conflict

1

L → V in CAA32164. Ref.3

Sequence conflict

1

R → H in AAA40636. Ref.1

Sequence conflict

1

R → H in CAA32164. Ref.3

Sequence conflict

1

V → L in AAA40636. Ref.1

Sequence conflict

1

V → L in CAA32164. Ref.3

Sequence conflict

1

R → Q in AAA40636. Ref.1

Sequence conflict

1

R → Q in CAA32164. Ref.3

Sequence conflict

1

M → L in AAA40638. Ref.4

Sequence conflict

1

T → A in AAA40636. Ref.1

Sequence conflict

1

A → G in AAA40636. Ref.1

Sequence conflict

1

P → T in AAA40636. Ref.1

Sequence conflict

1

H → R in AAA40636. Ref.1

Sequence conflict

1

T → A in AAA40636. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P06238 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: BFD63B8A4F6A2632
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1,472

163,785

        10         20         30         40         50         60 
MGKHRLRSLA LLPLLLRLLL LLLPTDASAP QKPIYMVMVP SLLHAGTPEK ACFLFSHLNE 

        70         80         90        100        110        120 
TVAVRVSLES VRGNQSLFTD LVVDKDLFHC TSFTVPQSSS DEVMFFTVQV KGATHEFRRR 

       130        140        150        160        170        180 
STVLVKKKES LVFAQTDKPI YKPGQTVRFR VVSLDESFHP LNELIPLLYI QDPKNNRIAQ 

       190        200        210        220        230        240 
WQNFNLEGGL KQLSFPLSSE PTQGSYKVVI RTESGRTVEH PFSVEEFVLP KFEVRVTVPE 

       250        260        270        280        290        300 
TITILEEEMN VSVCGIYTYG KPVPGRVTVN ICRKYSNPSN CFGEESVAFC EKLSQQLDGR 

       310        320        330        340        350        360 
GCFSQLVKTK SFQLKRQEYE MQLDVHAKIQ EEGTGVEETG KGLTKITRTI TKLSFVNVDS 

       370        380        390        400        410        420 
HFRQGIPFVG QVLLVDGRGT PIPYETIFIG ADEANLYINT TTDKHGLARF SINTDDIMGT 

       430        440        450        460        470        480 
SLTVRAKYKD SNACYGFRWL TEENVEAWHT AYAVFSPSRS FLHLESLPDK LRCDQTLEVQ 

       490        500        510        520        530        540 
AHYILNGEAM QELKELVFYY LMMAKGGIVR AGTHVLPLKQ GQMRGHFSIL ISMETDLAPV 

       550        560        570        580        590        600 
ARLVLYAILP NGEVVGDTAK YEIENCLANK VDLVFRPNSG LPATRALLSV MASPQSLCGL 

       610        620        630        640        650        660 
RAVDQSVLLM KPETELSASL IYDLLPVKDL TGFPQGADQR EEDTNGCVKQ NDTYINGILY 

       670        680        690        700        710        720 
SPVQNTNEED MYGFLKDMGL KVFTNSNIRK PKVCERLRDN KGIPAAYHLV SQSHMDAFLE 

       730        740        750        760        770        780 
SSESPTETRR SYFPETWIWD LVVVDSAGVA EVEVTVPDTI TEWKAGAFCL SNDTGLGLSP 

       790        800        810        820        830        840 
VVQFQAFQPF FVELTMPYSV IRGEAFTLKA TVLNYLPTCI RVAVQLEASP DFLAAPEEKE 

       850        860        870        880        890        900 
QRSHCICMNQ RHTASWAVIP KSLGNVNFTV SAEALNSKEL CGNEVPVVPE QGKKDTIIKS 

       910        920        930        940        950        960 
LLVEPEGLEN EVTFNSLLCP MGAEVSELIA LKLPSDVVEE SARASVTVLG DILGSAMQNT 

       970        980        990       1000       1010       1020 
QDLLKMPYGC GEQNMVLFAP NIYVLDYLNE TQQLTQEIKT KAIAYLNTGY QRQLNYKHRD 

      1030       1040       1050       1060       1070       1080 
GSYSTFGDKP GRNHANTWLT AFVLKSFAQA RKYIFIDEVH ITQALLWLSQ QQKDNGCFRS 

      1090       1100       1110       1120       1130       1140 
SGSLLNNAMK GGVEDEVTLS AYITIALLEM SLPVTHPVVR NALFCLDTAW KSARGGAGGS 

      1150       1160       1170       1180       1190       1200 
HVYTKALLAY AFALAGNQDT KKEILKSLDE EAVKEEDSVH WTRPQKPSVS VALWYQPQAP 

      1210       1220       1230       1240       1250       1260 
SAEVEMTAYV LLAYLTTEPA PTQEDLTAAM LIVKWLTKQQ NSHGGFSSTQ DTVVALHALS 

      1270       1280       1290       1300       1310       1320 
KYGSATFTRA KKAAQVTIHS SGTFSTKFQV NNNNQLLLQR VTLPTVPGDY TVKVTGEGCV 

      1330       1340       1350       1360       1370       1380 
YLQTSLKYSV LPREEEFPFT VVVQTLPGTC EDPKAHTSFQ ISLNISYTGS RSESNMAIAD 

      1390       1400       1410       1420       1430       1440 
VKMVSGFIPL KPTVKMLERS VHVSRTEVSN NHVLIYLDKV SNQTVNLSFT VQQDIPIRDL 

      1450       1460       1470 
KPAVVKVYDY YEKDEFAVAK YSAPCSTDYG NA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00392886.
PIR	A26122.
RefSeq	NP_036620.2. NM_012488.2. XP_003749876.1. XM_003749828.1.
UniGene	Rn.225884.
3D structure databases
ProteinModelPortal	P06238.
SMR	P06238. Positions 129-230, 1336-1472.
ModBase	Search...
Protein family/group databases
MEROPS	I39.001.
Proteomic databases
PaxDb	P06238.
PRIDE	P06238.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000019346; ENSRNOP00000019346; ENSRNOG00000028896.
GeneID	100911545. 24153.
KEGG	rno:100911545. rno:24153.
UCSC	RGD:2004. rat.
Organism-specific databases
CTD	2.
RGD	2004. A2m.
Phylogenomic databases
eggNOG	COG2373.
GeneTree	ENSGT00560000076685.
HOGENOM	HOG000220939.
HOVERGEN	HBG000039.
KO	K03910.
OrthoDB	EOG4H9XJN.
Gene expression databases
Genevestigator	P06238.
GermOnline	ENSRNOG00000028896. Rattus norvegicus.
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
NextBio	602439.

Entry information

Entry name

A2MG_RAT

Accession

Primary (citable) accession number: P06238
Secondary accession number(s): Q4FZY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	December 12, 2006
Last modified:	April 3, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents