Skip Header

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

Alpha-2-macroglobulin-P

Gene

A2m

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Biological processi

Pregnancy

Enzyme and pathway databases

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

Protein family/group databases

MEROPSiI39.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-2-macroglobulin-P
Alternative name(s):
Alpha-2-macroglobulin
Gene namesi
Name:A2mImported
Synonyms:A2mpImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:2449119. A2m.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence analysisAdd
BLAST
Chaini33 – 14741442Alpha-2-macroglobulin-PSequence analysisPRO_0000271402Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi55 ↔ 93By similarity
Glycosylationi62 – 621N-linked (GlcNAc...)Sequence analysis
Glycosylationi77 – 771N-linked (GlcNAc...)Sequence analysis
Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence analysis
Disulfide bondi257 ↔ 305By similarity
Disulfide bondi275 ↔ 293By similarity
Disulfide bondi284 – 284Interchain (with C-437)By similarity
Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence analysis
Disulfide bondi437 – 437Interchain (with C-284)By similarity
Disulfide bondi476 ↔ 569By similarity
Disulfide bondi601 ↔ 771By similarity
Disulfide bondi650 ↔ 697By similarity
Glycosylationi654 – 6541N-linked (GlcNAc...)Sequence analysis
Glycosylationi774 – 7741N-linked (GlcNAc...)Sequence analysis
Disulfide bondi821 ↔ 849By similarity
Disulfide bondi847 ↔ 883By similarity
Glycosylationi869 – 8691N-linked (GlcNAc...)Sequence analysis
Disulfide bondi921 ↔ 1321By similarity
Cross-linki972 ↔ 975Isoglutamyl cysteine thioester (Cys-Gln)By similarity
Glycosylationi991 – 9911N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1079 ↔ 1127By similarity
Disulfide bondi1352 ↔ 1467By similarity
Glycosylationi1366 – 13661N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Thioester bond

Proteomic databases

MaxQBiQ6GQT1.
PaxDbiQ6GQT1.
PeptideAtlasiQ6GQT1.
PRIDEiQ6GQT1.

PTM databases

iPTMnetiQ6GQT1.
PhosphoSiteiQ6GQT1.

Expressioni

Tissue specificityi

Expressed in uterus, mesometrial lympoid aggregate and mammary tissue during pregnancy. Expressed in ovary, testis and kidney. Low level expression in heart. Not expressed in liver.1 Publication

Developmental stagei

Expressed in uterus of pregnant females during decidualization from 6 dpc with highest level around 10 dpc declining throughout the rest of the pregnancy.1 Publication

Gene expression databases

BgeeiENSMUSG00000030111.
CleanExiMM_A2M.
ExpressionAtlasiQ6GQT1. baseline and differential.
GenevisibleiQ6GQT1. MM.

Interactioni

Subunit structurei

Homotetramer; disulfide-linked.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000032203.

Structurei

3D structure databases

ProteinModelPortaliQ6GQT1.
SMRiQ6GQT1. Positions 132-233, 1338-1468.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni623 – 752130Bait regionBy similarityAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Bait region, Signal

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
GeneTreeiENSGT00760000118982.
HOGENOMiHOG000220939.
HOVERGENiHBG000039.
InParanoidiQ6GQT1.
KOiK03910.
OMAiFGPRYGQ.
OrthoDBiEOG091G00F5.
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]
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.

Q6GQT1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKRWLPSLA LLPLPPPLLL LLLLLLPTNA SAPQKPIYMV MVPSLLHAGT
60 70 80 90 100
PEKGCLLFNH LNETVTVKVS MESVRGNQSL FTDLVVDKDL FHCASFIVPQ
110 120 130 140 150
SSSNEVMFLT VQVKGPTHEF RRRSTVLIKT KESLVFAQTD KPIYKPGQMV
160 170 180 190 200
RFRVVSLDEN FHPLNELIPL LYIQDSKKNR IAQWQNFRLE GGLKQLSFPL
210 220 230 240 250
SSEPTQGSYK VVIRTESGRT VEHPFSVKEF VLPKFEVKVA VPETITILEE
260 270 280 290 300
EMNVSVCGIY TYGKPVPGHV TVNICRKYSN PSSCFGEESL AFCEKFSQQL
310 320 330 340 350
DGRGCFSQLV KTKSFQLKRQ EYEMQLDVNA KIQEEGTGVE ETGKGLTKIT
360 370 380 390 400
RTITKLSFVN VDTHFRQGIP FVGQVLLVDG RGTPIPYEMI FIGADEANQN
410 420 430 440 450
INTTTDKNGL ARFSINTDDI MGTSLTVRAK YKDSNVCYGF RWLTEENVEA
460 470 480 490 500
WHTANAVFSP SRSFVHLESL PYKLRCEQTL AVQAHYILND EAVLERKELV
510 520 530 540 550
FYYLMMAKGG IVRAGTHVLP VTQGHKKGHF SILISMETDL APVARLVLYT
560 570 580 590 600
ILPNGEVVGD TVKYEIEKCL ANKVDLVFHP NIGLPATRAF LSVMASPQSL
610 620 630 640 650
CGLRAVDQSV LLTKPEAELS ASLVYDLLPV KDLTGFPKGV NQQEEDTNGC
660 670 680 690 700
LKQNDTYING ILYSPVQNTN EEDMYGFLKD MGLKVFTNLN IRKPKVCERL
710 720 730 740 750
GVNKIPAAYH LVSQGHMDAF LESSESPTET TRSYFPETWI WDLVIVDSTG
760 770 780 790 800
VAEMEVTVPD TITEWKAGAF CLSNDTGLGL SPVIDFQAFQ PFFVDLTMPY
810 820 830 840 850
SVIRGEAFTL KATVLNYLQT CIRVGVQLEA SPDFLATPEE KEQKSHCICM
860 870 880 890 900
NERHTMSWAV IPKSLGNVNF TVSAEALDSK ELCRNEVPVV PERGKKDTII
910 920 930 940 950
KSLLVEPEGL ENEVTFNSLL CPTGAEVSEQ ISLKLPSDVV EESARASVTV
960 970 980 990 1000
LGDILGSAMQ NTQDLLKMPY GCGEQNMVLF APNIYVLDYL NETEQLTQEI
1010 1020 1030 1040 1050
KTKAITYLNT GYQRQLNYKH RDGSYSTFGD KPGRSHANTW LTAFVLKSFA
1060 1070 1080 1090 1100
QARRYIFIDE SHITQALTWL SQQQKDNGCF RSSGSLLNNA MKGGVEDEVT
1110 1120 1130 1140 1150
LSAYITIALL EMSLPVTHPV VRNALFCLDT AWKSARRGAS GNHVYTKALL
1160 1170 1180 1190 1200
AYAFALAGNQ DTKKEILKSL DEEAVKEDNS VHWTRAQKPR VPADLWYQPQ
1210 1220 1230 1240 1250
APSAEVEMTA YVLLAYLTTE LVPTREDLTA AMLIVKWLTK QQNSHGGFSS
1260 1270 1280 1290 1300
TQDTVVALHA LSKYGAATFT RAKKAAHVTI QSSGAFYTKF QVNNDNQLLL
1310 1320 1330 1340 1350
QRVTLPTVPG DYTAKVAGEG CVYLQTSLKY SVLPREKEFP FALVVQTLPG
1360 1370 1380 1390 1400
TCEDLKAHTT FQISLNISYI GSRSDSNMAI ADVKMVSGFI PLKPTVKMLE
1410 1420 1430 1440 1450
RSVHVSRTEV SNNHVLIYLD KVSNQMLTLF FMVQQDIPVR DLKPAIVKVY
1460 1470
DYYEKDEFAV AKYSAPCSAG YGNA
Length:1,474
Mass (Da):164,353
Last modified:July 27, 2011 - v2
Checksum:i996A152EC0899F99
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti366 – 3661R → G in AAO25741 (PubMed:15355875).Curated
Sequence conflicti452 – 4521H → R in AAO25741 (PubMed:15355875).Curated
Sequence conflicti659 – 6668NGILYSPV → RNPVLPR in AAO25741 (PubMed:15355875).Curated
Sequence conflicti799 – 7991P → A in AAH72642 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY185125 mRNA. Translation: AAO25741.1.
AC153581 Genomic DNA. No translation available.
BC072642 mRNA. Translation: AAH72642.1.
CCDSiCCDS39617.1.
RefSeqiNP_783327.2. NM_175628.3.
UniGeneiMm.30151.

Genome annotation databases

EnsembliENSMUST00000032203; ENSMUSP00000032203; ENSMUSG00000030111.
GeneIDi232345.
KEGGimmu:232345.
UCSCiuc009doq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY185125 mRNA. Translation: AAO25741.1.
AC153581 Genomic DNA. No translation available.
BC072642 mRNA. Translation: AAH72642.1.
CCDSiCCDS39617.1.
RefSeqiNP_783327.2. NM_175628.3.
UniGeneiMm.30151.

3D structure databases

ProteinModelPortaliQ6GQT1.
SMRiQ6GQT1. Positions 132-233, 1338-1468.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000032203.

Protein family/group databases

MEROPSiI39.004.

PTM databases

iPTMnetiQ6GQT1.
PhosphoSiteiQ6GQT1.

Proteomic databases

MaxQBiQ6GQT1.
PaxDbiQ6GQT1.
PeptideAtlasiQ6GQT1.
PRIDEiQ6GQT1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032203; ENSMUSP00000032203; ENSMUSG00000030111.
GeneIDi232345.
KEGGimmu:232345.
UCSCiuc009doq.1. mouse.

Organism-specific databases

CTDi2.
MGIiMGI:2449119. A2m.

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
GeneTreeiENSGT00760000118982.
HOGENOMiHOG000220939.
HOVERGENiHBG000039.
InParanoidiQ6GQT1.
KOiK03910.
OMAiFGPRYGQ.
OrthoDBiEOG091G00F5.
TreeFamiTF313285.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiA2m. mouse.
PROiQ6GQT1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030111.
CleanExiMM_A2M.
ExpressionAtlasiQ6GQT1. baseline and differential.
GenevisibleiQ6GQT1. MM.

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]
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_MOUSE
AccessioniPrimary (citable) accession number: Q6GQT1
Secondary accession number(s): E9QMQ7, Q811S0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: July 27, 2011
Last modified: September 7, 2016
This is version 93 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.