Search Results

Overview

Uniprot IDP01023
Protein NameAlpha-2-macroglobulin
Gene NameA2M
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1003 LTPEIKSKAIGYLNT
1019 YQRQLNYKHYDGSYS
1177 LNEEAVKKDNSVHWE
1274 ATFTRTGKAAQVTIQ
135 LVFVQTDKSIYKPGQ
354 ITKLSFVKVDSHFRQ
375 QVRLVDGKGVPIPNK
531 FSISIPVKSDIAPVA
557 DVIGDSAKYDVENCL
567 VENCLANKVDLSFSP
682 LKAFTNSKIRKPKMC
841 FLAVPVEKEQAPHCI
912 VEPEGLEKETTFNSL
934 VSEELSLKLPPNVVE

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

Protein Sequence

10 MGKNKLLHPS 20 LVLLLLVLLP 30 TDASVSGKPQ 40 YMVLVPSLLH 50 TETTEKGCVL 60 LSYLNETVTV 70 SASLESVRGN 80 RSLFTDLEAE 90 NDVLHCVAFA 100 VPKSSSNEEV 110 MFLTVQVKGP 120 TQEFKKRTTV 130 MVKNEDSLVF 140 VQTDKSIYKP 150 GQTVKFRVVS 160 MDENFHPLNE 170 LIPLVYIQDP 180 KGNRIAQWQS 190 FQLEGGLKQF 200 SFPLSSEPFQ 210 GSYKVVVQKK 220 SGGRTEHPFT 230 VEEFVLPKFE 240 VQVTVPKIIT 250 ILEEEMNVSV 260 CGLYTYGKPV 270 PGHVTVSICR 280 KYSDASDCHG 290 EDSQAFCEKF 300 SGQLNSHGCF 310 YQQVKTKVFQ 320 LKRKEYEMKL 330 HTEAQIQEEG 340 TVVELTGRQS 350 SEITRTITKL 360 SFVKVDSHFR 370 QGIPFFGQVR 380 LVDGKGVPIP 390 NKVIFIRGNE 400 ANYYSNATTD 410 EHGLVQFSIN 420 TTNVMGTSLT 430 VRVNYKDRSP 440 CYGYQWVSEE 450 HEEAHHTAYL 460 VFSPSKSFVH 470 LEPMSHELPC 480 GHTQTVQAHY 490 ILNGGTLLGL 500 KKLSFYYLIM 510 AKGGIVRTGT 520 HGLLVKQEDM 530 KGHFSISIPV 540 KSDIAPVARL 550 LIYAVLPTGD 560 VIGDSAKYDV 570 ENCLANKVDL 580 SFSPSQSLPA 590 SHAHLRVTAA 600 PQSVCALRAV 610 DQSVLLMKPD 620 AELSASSVYN 630 LLPEKDLTGF 640 PGPLNDQDNE 650 DCINRHNVYI 660 NGITYTPVSS 670 TNEKDMYSFL 680 EDMGLKAFTN 690 SKIRKPKMCP 700 QLQQYEMHGP 710 EGLRVGFYES 720 DVMGRGHARL 730 VHVEEPHTET 740 VRKYFPETWI 750 WDLVVVNSAG 760 VAEVGVTVPD 770 TITEWKAGAF 780 CLSEDAGLGI 790 SSTASLRAFQ 800 PFFVELTMPY 810 SVIRGEAFTL 820 KATVLNYLPK 830 CIRVSVQLEA 840 SPAFLAVPVE 850 KEQAPHCICA 860 NGRQTVSWAV 870 TPKSLGNVNF 880 TVSAEALESQ 890 ELCGTEVPSV 900 PEHGRKDTVI 910 KPLLVEPEGL 920 EKETTFNSLL 930 CPSGGEVSEE 940 LSLKLPPNVV 950 EESARASVSV 960 LGDILGSAMQ 970 NTQNLLQMPY 980 GCGEQNMVLF 990 APNIYVLDYL 1000 NETQQLTPEI 1010 KSKAIGYLNT 1020 GYQRQLNYKH 1030 YDGSYSTFGE 1040 RYGRNQGNTW 1050 LTAFVLKTFA 1060 QARAYIFIDE 1070 AHITQALIWL 1080 SQRQKDNGCF 1090 RSSGSLLNNA 1100 IKGGVEDEVT 1110 LSAYITIALL 1120 EIPLTVTHPV 1130 VRNALFCLES 1140 AWKTAQEGDH 1150 GSHVYTKALL 1160 AYAFALAGNQ 1170 DKRKEVLKSL 1180 NEEAVKKDNS 1190 VHWERPQKPK 1200 APVGHFYEPQ 1210 APSAEVEMTS 1220 YVLLAYLTAQ 1230 PAPTSEDLTS 1240 ATNIVKWITK 1250 QQNAQGGFSS 1260 TQDTVVALHA 1270 LSKYGAATFT 1280 RTGKAAQVTI 1290 QSSGTFSSKF 1300 QVDNNNRLLL 1310 QQVSLPELPG 1320 EYSMKVTGEG 1330 CVYLQTSLKY 1340 NILPEKEEFP 1350 FALGVQTLPQ 1360 TCDEPKAHTS 1370 FQISLSVSYT 1380 GSRSASNMAI 1390 VDVKMVSGFI 1400 PLKPTVKMLE 1410 RSNHVSRTEV 1420 SSNHVLIYLD 1430 KVSNQTLSLF 1440 FTVLQDVPVR 1450 DLKPAIVKVY 1460 DYYETDEFAI 1470 AEYNAPCSKD LGNA

Gene Ontology

Classification GO ID Description
Molecular Function GO:0019966 interleukin-1 binding
Cellular Component GO:0072562 blood microparticle
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0031012 extracellular matrix
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0031093 platelet alpha granule lumen
Molecular Function GO:0048306 calcium-dependent protein binding
Molecular Function GO:0004866 endopeptidase inhibitor activity
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0019838 growth factor binding
Molecular Function GO:0019959 interleukin-8 binding
Molecular Function GO:0002020 protease binding
Molecular Function GO:0004867 serine-type endopeptidase inhibitor activity
Molecular Function GO:0005102 signaling receptor binding
Molecular Function GO:0043120 tumor necrosis factor binding
Biological Process GO:0001869 negative regulation of complement activation, lectin pathway

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.