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Protein

Alpha-2-macroglobulin

Gene

A2M

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Enzyme and pathway databases

ReactomeiR-BTA-114608. Platelet degranulation.
R-BTA-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-BTA-1474228. Degradation of the extracellular matrix.
R-BTA-194223. HDL-mediated lipid transport.
R-BTA-194840. Rho GTPase cycle.

Protein family/group databases

MEROPSiI39.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-2-macroglobulin
Short name:
Alpha-2-M
Gene namesi
Name:A2M
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Add BLAST23
ChainiPRO_000009379024 – 1510Alpha-2-macroglobulinAdd BLAST1487

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi48 ↔ 86By similarity
Glycosylationi55N-linked (GlcNAc...)Sequence analysis1
Glycosylationi70N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi251 ↔ 299By similarity
Disulfide bondi269 ↔ 287By similarity
Disulfide bondi278Interchain (with C-431)By similarity
Disulfide bondi431Interchain (with C-278)By similarity
Disulfide bondi470 ↔ 563By similarity
Disulfide bondi595 ↔ 773By similarity
Disulfide bondi644 ↔ 691By similarity
Disulfide bondi823 ↔ 850By similarity
Disulfide bondi848 ↔ 884By similarity
Glycosylationi870N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi922 ↔ 1358By similarity
Cross-linki1009 ↔ 1012Isoglutamyl cysteine thioester (Cys-Gln)By similarity
Glycosylationi1028N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1116 ↔ 1164By similarity
Disulfide bondi1389 ↔ 15031 Publication
Glycosylationi1440N-linked (GlcNAc...)1 Publication1
Glycosylationi1460N-linked (GlcNAc...)By similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Thioester bond

Proteomic databases

PaxDbiQ7SIH1.
PeptideAtlasiQ7SIH1.
PRIDEiQ7SIH1.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiENSBTAG00000018137.

Interactioni

Subunit structurei

Homotetramer; disulfide-linked.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000006167.

Structurei

Secondary structure

11510
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1377 – 1388Combined sources12
Helixi1392 – 1395Combined sources4
Beta strandi1397 – 1406Combined sources10
Beta strandi1408 – 1421Combined sources14
Beta strandi1426 – 1428Combined sources3
Helixi1430 – 1434Combined sources5
Beta strandi1438 – 1447Combined sources10
Beta strandi1450 – 1456Combined sources7
Beta strandi1463 – 1473Combined sources11
Beta strandi1481 – 1489Combined sources9
Beta strandi1494 – 1499Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AYOX-ray1.90A/B1375-1504[»]
ProteinModelPortaliQ7SIH1.
SMRiQ7SIH1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SIH1.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni692 – 730Bait regionBy similarityAdd BLAST39
Regioni706 – 711InhibitoryBy similarity6
Regioni721 – 725InhibitoryBy similarity5
Regioni732 – 737InhibitoryBy similarity6

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410KCRI. Eukaryota.
ENOG410XQIV. LUCA.
GeneTreeiENSGT00760000118982.
HOGENOMiHOG000220939.
HOVERGENiHBG000039.
InParanoidiQ7SIH1.
KOiK03910.
OMAiINTTNIM.
OrthoDBiEOG091G00F5.
TreeFamiTF313285.

Family and domain databases

Gene3Di1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
2.60.40.920. 1 hit.
InterProiIPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR003344. Big_1_dom.
IPR014756. Ig_E-set.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR010916. TonB_box_CS.
[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]
SMARTiSM01360. A2M. 1 hit.
SM01359. A2M_N_2. 1 hit.
SM01361. A2M_recep. 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.

Q7SIH1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKNKLLYPS LTLLLLLLLP TDASVSGKPQ YMVLVPSLLH TETPEKGCLL
60 70 80 90 100
LSHLNETVTV SASLESVREN RSLFTDVVAE KDLFHCVSFT LPRSPTSQEV
110 120 130 140 150
MFLTIQVKGP TQEFKKRTTV LVKNEESLVF VQTDKPIYKP EQTVKFRIVL
160 170 180 190 200
LDESFHPLNE LVPLVYVEDP KGNRIAQWQN LEVENGLQQL TFPLSSEPFQ
210 220 230 240 250
GSYKVVVQKG SGGTAEHPFT VEEFVLPKFE VQVRMPKIIT ILEEEVQVSV
260 270 280 290 300
CGLYTYGKPV PGRVTMNMCR KYRNPSNCYG EESNAVCEKF SGELNNEGCF
310 320 330 340 350
SQQVNTKIFQ LKRQEFEMKI EVEAKIQEEG TEVELTGKGA TEITTTITKL
360 370 380 390 400
SFVTVDSNLR RGIPFTGKVL LVDGKGVPMP NKVIFITANE ANHNSNTTTD
410 420 430 440 450
EHGLAQFSIT TTKIKGTSLS IRVKYKDHSP CYGYQWLSEE HQDAYHSANL
460 470 480 490 500
VFSRSNSFVY LEPLPRELPC GKTQTVQAHY VLKGQVLKDL KELVFYYLIM
510 520 530 540 550
AKGGIVRSGT HTLPVEQGDM QGHFSMSVPV ESDIAPVARL LIYAILPDGE
560 570 580 590 600
VVGDSARYEI EHCLANKVGL NFSPGQSFPA SQAHLRVTAS PQSLCALRAV
610 620 630 640 650
DQSVLLMRPE AELSAATVYN LLPVKDLSSF PSSVNQQEED NEDCISHDNV
660 670 680 690 700
YINGIMYFPV SNTNEKDMYS FLQDMGLKAF TNSKIHKPKI CPQPEEHRIQ
710 720 730 740 750
HHTLLASPVR AEMGRNRDFV HFDDTSEPPT ETVRKYFPET WIWDLVVVSS
760 770 780 790 800
SGVHEVEVTV PDTITEWKAG ALCLSRDTGL GLSPTASLRV FQPFFVELTM
810 820 830 840 850
PYSVIRGEAF TLKATVLNYL PKCIRVSVQL EASPAFLAVP EKEQETYCIC
860 870 880 890 900
GNGRQTVSWA VTPKSLGNVN FTVSAEAVES QELCGSEVPV VPEHGRKDTI
910 920 930 940 950
IKPLLVEPEG LEKEVIFNSL LCPSVDFVFL GAEDGGQVLR HFPPAAATDT
960 970 980 990 1000
AADAHDPARP GAKVSESLSL KLPPNVVEES ARASFSVLGD ILGSAMRNTQ
1010 1020 1030 1040 1050
NLLQMPYGCG EQNMARFAPN IYVLDYLNET QQLTAELKSK AILYLNTGYQ
1060 1070 1080 1090 1100
RQLLYKHFDG SYSTFGEHRG NSEGNTWLTA FVLKSFAQAR GYIFIDEAHI
1110 1120 1130 1140 1150
TEALTWLAQK QKSNGCFRST GTLLNNAIKG GVDDEVTLSA YITIALLEMP
1160 1170 1180 1190 1200
LPVTHPVVRN ALFCLDSAWK SAKEGSQGSH VYTKALLAYA FALAGNQERR
1210 1220 1230 1240 1250
TEVLTSLYEE AVKEDNTIHW TRPQKPRLLT EDIYQPRAPS AEVEMTAYVI
1260 1270 1280 1290 1300
LAHVTAQPAP NPEDLKRATS IVKWISKQQN CQGGFSSTQD TVVALHALSR
1310 1320 1330 1340 1350
YGAATFTSAR KAAQVTIQSS GTFSTKFQVE NSNRLLLQQV SLPEVPGEYS
1360 1370 1380 1390 1400
MSVTGEGCVY LQTSLKYNIL PKKDEFPFAL EVQTLPQTCD GPKAHTSFQI
1410 1420 1430 1440 1450
SLSVSYIGSR PASNMAIVDV KMVSGFIPLK PTVKMLERSN VSRTEVSNNH
1460 1470 1480 1490 1500
VLIYLDKVTN ETLTLTFTVL QDIPVRDLKP AIVKVYDYYE TDEFAVAEYS
1510
APCSKDIGNA
Length:1,510
Mass (Da):167,576
Last modified:April 20, 2010 - v2
Checksum:i93928C5436E0E20F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC153840 mRNA. Translation: AAI53841.1.
RefSeqiNP_001103265.1. NM_001109795.1.
UniGeneiBt.60794.

Genome annotation databases

EnsembliENSBTAT00000006167; ENSBTAP00000006167; ENSBTAG00000018137.
GeneIDi513856.
KEGGibta:513856.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC153840 mRNA. Translation: AAI53841.1.
RefSeqiNP_001103265.1. NM_001109795.1.
UniGeneiBt.60794.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AYOX-ray1.90A/B1375-1504[»]
ProteinModelPortaliQ7SIH1.
SMRiQ7SIH1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000006167.

Protein family/group databases

MEROPSiI39.001.

Proteomic databases

PaxDbiQ7SIH1.
PeptideAtlasiQ7SIH1.
PRIDEiQ7SIH1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000006167; ENSBTAP00000006167; ENSBTAG00000018137.
GeneIDi513856.
KEGGibta:513856.

Organism-specific databases

CTDi2.

Phylogenomic databases

eggNOGiENOG410KCRI. Eukaryota.
ENOG410XQIV. LUCA.
GeneTreeiENSGT00760000118982.
HOGENOMiHOG000220939.
HOVERGENiHBG000039.
InParanoidiQ7SIH1.
KOiK03910.
OMAiINTTNIM.
OrthoDBiEOG091G00F5.
TreeFamiTF313285.

Enzyme and pathway databases

ReactomeiR-BTA-114608. Platelet degranulation.
R-BTA-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-BTA-1474228. Degradation of the extracellular matrix.
R-BTA-194223. HDL-mediated lipid transport.
R-BTA-194840. Rho GTPase cycle.

Miscellaneous databases

EvolutionaryTraceiQ7SIH1.

Gene expression databases

BgeeiENSBTAG00000018137.

Family and domain databases

Gene3Di1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
2.60.40.920. 1 hit.
InterProiIPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR003344. Big_1_dom.
IPR014756. Ig_E-set.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR010916. TonB_box_CS.
[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]
SMARTiSM01360. A2M. 1 hit.
SM01359. A2M_N_2. 1 hit.
SM01361. A2M_recep. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiA2MG_BOVIN
AccessioniPrimary (citable) accession number: Q7SIH1
Secondary accession number(s): A8E647
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: April 20, 2010
Last modified: November 30, 2016
This is version 102 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.