A2MG_PONAB
ID A2MG_PONAB Reviewed; 1474 AA.
AC Q5R4N8;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Alpha-2-macroglobulin;
DE Short=Alpha-2-M;
DE Flags: Precursor;
GN Name=A2M;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Is able to inhibit all four classes of proteinases by a
CC unique 'trapping' mechanism. This protein has a peptide stretch, called
CC the 'bait region' which contains specific cleavage sites for different
CC proteinases. When a proteinase cleaves the bait region, a
CC conformational change is induced in the protein which traps the
CC proteinase. The entrapped enzyme remains active against low molecular
CC weight substrates (activity against high molecular weight substrates is
CC greatly reduced). Following cleavage in the bait region a thioester
CC bond is hydrolyzed and mediates the covalent binding of the protein to
CC the proteinase (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000305}.
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DR EMBL; CR861207; CAH93278.1; -; mRNA.
DR RefSeq; NP_001126929.1; NM_001133457.1.
DR AlphaFoldDB; Q5R4N8; -.
DR BMRB; Q5R4N8; -.
DR SMR; Q5R4N8; -.
DR STRING; 9601.ENSPPYP00000004847; -.
DR MEROPS; I39.001; -.
DR PRIDE; Q5R4N8; -.
DR GeneID; 100173946; -.
DR KEGG; pon:100173946; -.
DR CTD; 2; -.
DR eggNOG; KOG1366; Eukaryota.
DR InParanoid; Q5R4N8; -.
DR OrthoDB; 354230at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd02897; A2M_2; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR041813; A2M_TED.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR010916; TonB_box_CS.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF17789; MG4; 1.
DR Pfam; PF07678; TED_complement; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF49410; SSF49410; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PE 2: Evidence at transcript level;
KW Bait region; Disulfide bond; Glycoprotein; Isopeptide bond;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal; Thioester bond.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1474
FT /note="Alpha-2-macroglobulin"
FT /id="PRO_0000042695"
FT REGION 690..728
FT /note="Bait region"
FT /evidence="ECO:0000250"
FT REGION 704..709
FT /note="Inhibitory"
FT /evidence="ECO:0000250"
FT REGION 719..723
FT /note="Inhibitory"
FT /evidence="ECO:0000250"
FT REGION 730..735
FT /note="Inhibitory"
FT /evidence="ECO:0000250"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 869
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 991
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 1424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 48..86
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 251..299
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 269..287
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 278
FT /note="Interchain (with C-431)"
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 431
FT /note="Interchain (with C-278)"
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 470..563
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 595..771
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 642..689
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 821..849
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 847..883
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 921..1321
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 1079..1127
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT DISULFID 1352..1467
FT /evidence="ECO:0000250|UniProtKB:P01023"
FT CROSSLNK 693
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-? in other proteins)"
FT /evidence="ECO:0000255"
FT CROSSLNK 694
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-? in other proteins)"
FT /evidence="ECO:0000255"
FT CROSSLNK 972..975
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1474 AA; 163262 MW; 14F19160ACBCAB6B CRC64;
MGKNKLLHPS LVLLLLVLLP TDASVSGKPQ YMVLVPSLLH TEAAEKGCVL LSYLNETVTV
SASLESVRGN RSLFTDLEAE NDVLHCVAFA IPKSSSNEEV MFLTVQVKGP TQEFKKRTTV
MVKNEDSLVF VQTDKSIYKP AQTVKFRVVS MDENFHPLNE LIPLVYIQDP KGNRIAQWQS
FQLEGGLKQF SFPLSSEPFQ GSYKVVVQKK SGRRTEHPFT VEEFVLPKFE VQVTVPKIIT
ILEEEMNVSV CGLYTYGKPV PGHVTVSICR KYSDASNCHG EDSQAFCEKF SGQLNSHGCF
YQQVKTKVFQ LKRKEYEMKL HTKAQIQEEG TVVELTGRQS SEITRTITKL SFVKADSHFR
QGIPFFGQVR LVDGKGVPIP NKVIFIRGNE ANYYSNATTD EHGLVQFSIN TTNVMGTSLT
VRVKYKDRSP CYGYQWVSEE HEEAHHTAYL VFSPSKSFVH LEPVSHELPC GQTQTVQAHY
ILNGGALQGL KKLSFYYLIM AKGGIVRTGT HGLLVKQEDM KGHFSISIPV KSDIAPVARL
LIYAVLPTGD VIGDSAKYDV ENCLANKVDL SFSPSQSLPA LHAHLRVTAA PQSLCALRAV
DQSVLLMKPD AELSASSVYN LLPEKDLTGF PGPLNDQGDE DCINRHNVYI NGITYTPVSS
TNEKDMYSFL EDMGLKAFTN SKIRKPKLCP QLQQYEMHGP EGLRVGFYES DVMGRGHARL
VHAEEPPTET VRKYFPETWI WDLVVVNSSG VAEVGVTVPD TITEWKAGAF CLSEDAGLGI
SSTASLRAFQ PFFVELTMPY SVIRGEVFTL KATVLNYLPK CIRVSVQLEA SPAFLAVPVE
KEQAPHCICA NGRQTVSWAI TPKSLGNVNF TVSAEALESQ ELCGTEVASV PEYGKKDTVI
KPLLVEPEGL EKETTFNSLL CPSGGEVSEE LSLKLPPNVV EESARASVSV LGDILGSAMQ
NTQNLLQMPY GCGEQNMVLF APNIYVLDYL NETQQLTPEI KSKAIGYLNT GYQRQLNYKH
YDGSYSTFGE RYGRNQGNTW LTAFVLKTFA QARAYIFIDE AHITQALIWL SQRQKDNGCF
RSSGSLLNNA IKGGVEDEVT LSAYITIALL EIPLTVTHPV VRNALFCLES AWKTAQEGDH
GSHVYTKALL AYAFALAGNQ DKRKEVLQSL HEEAVKKDNS VHWERPQKPK APVGHFYEPQ
APSAEVEMTS YALLAYLTAQ PAPTSEDLTS ATNIVKWITK QQNAQGGFSS TQDTVVALHA
LSKYGAATFT RTGKAAQVTI QSSGTFSNKF QVDNNNRLLL QQVSLPELPG EYSMKVTGEG
CVYLQTSLKY NILPEKEEFP FALGVQTLPQ TCDEPKAHTS FQISLSVSYT GSRSASNMAI
VDVKMVSGFI PLKPTVKMLE RSNHVSRTEV SNNHVLIYLD KVSNQTLSLF FTVLQDVPVR
DLKPAIVKVY DYYETDEFAI AEYNAPCSKD LGNA
