ID A0A3Q1LLI6_BOVIN Unreviewed; 1410 AA.
AC A0A3Q1LLI6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Alpha-2-macroglobulin {ECO:0008006|Google:ProtNLM};
GN Name=LOC506828 {ECO:0000313|Ensembl:ENSBTAP00000057434.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000057434.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000057434.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000057434.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000057434.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000057434.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000256|ARBA:ARBA00010952}.
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DR Ensembl; ENSBTAT00000072340.1; ENSBTAP00000057434.1; ENSBTAG00000038461.3.
DR VEuPathDB; HostDB:ENSBTAG00000038461; -.
DR GeneTree; ENSGT00940000163775; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000038461; Expressed in liver and 91 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1LLI6; baseline.
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; 1.50.10.20; -; 1.
DR Gene3D; 2.20.130.20; -; 1.
DR Gene3D; 2.60.120.1540; -; 1.
DR Gene3D; 2.60.40.1930; -; 2.
DR Gene3D; 6.20.50.160; -; 1.
DR Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR047565; Alpha-macroglob_thiol-ester_cl.
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; IPR041555; MG3.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR PANTHER; PTHR11412:SF116; PREGNANCY ZONE PROTEIN; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF17791; MG3; 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 SMART; SM01419; Thiol-ester_cl; 1.
DR SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PE 3: Inferred from homology;
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1410
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018733176"
FT DOMAIN 420..568
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 694..779
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1327..1401
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1410 AA; 156329 MW; 2CE015A18D3CD490 CRC64;
TMRGHQLPNP VLILLFLLLP RDASATSKPQ YLVLVPSQLY AGVPEKVCVL LNHLNETVAL
TVTLESETEG RNLLTDLEAK NSFYCSSFTV SIPPRGKGNH YRESTLVDAL GSDPQQLKNV
SLVLCDDLDG WDRGGREVQE RGDICINYTP IKNKIQKRKM RSTDFKLQGG LSQLSFPLSV
EPALGPYKVV LLKEPGKRIE HSFEVDEYGK NSTHVKHMYD IKEYKIGSFL YVVTSKNLAY
INQKPVRGLV TINVCRKYLQ YSSSCNGKYP KSICEEFSQQ ADDEGCFTQL VNAKSLQLKQ
KGYERTLQVE AKVREEGTGL ELTGHGSSEI TNTLSKLKFT KVHSHYRRGL PFFGQVKFTT
NEHGLVNFSI DTSNFTSSFI SVGVIYKQNS HCFDSRWLEE SHIPATHTAS HIFSPSKSYI
QLEPVADTVI CGKTQEIRVH YILNGQILTD ERELTFYYLI KARGSIAQSE THVLSIKQGE
LKGVFSFSFR VESDIAPIAQ LLVYTILPNG EVIADTEELD IENCFANKVN LSFSSAQGLP
ASNTSLKITA APYSLCGLRA VDKSVLLMKP EAEFSPQSVY NLLSVKKIFS MGYRGPMNED
REKCINAEDI THNGIIYIPK QFISDDDAYS IFEPSCCLST APGLASSRSL PGPIHGMATP
LAGIDARGVY PSSSREDSSA MKVKETIRKY FPETWIWDMW GKHELAIKVP DTITEWKASA
LCLSGTAGLG LSPTISLTAF QPFFLELTLP YSVVRGEAFT LKATVFNYLS HCIRVSIQLE
ASSAFLAIPV EKNEESQCVC GNKQRTVSWA VTPKSLGEVN FTATAEALRS QELCGNKVPH
FPEIGQKDTV IKPLLVENIS LIFPSLMCIC LVSLETGGSE KLSLKLPSNV VEGSARATYS
VLGDILGSAM QNLQNLLRMP YGCGEQNMVL FTPNIYVLNY LNETGQLTEK IKSKAISYLI
SGYQRQLNYK HSDGSYSTFG DRDGRSQGNT WLTAFVLKSF SQAQSHIFVE DSHITDSLTW
LSRKQKENGC FQRSGSLLNN AIKGGVDDEV TLSAYITIAL LEMPLLVTHS IVRNALFCLE
RAWQSASEAQ GSFVYTKALL AYAFALAGDQ AKRNELLESL HKEAVKEEDS IHWQRPRKPQ
EVNELYSPHR APSVDVEMTS YCLLAHLTAQ PAPSSEDLSV ATQIVKWLTK QQNPNGGFSS
TQDTVVALQA LSKYGAATFI KGEKAATVTV KSAGTFSEEF QVDEAKRLLL QEVALPEIPG
KYSTAVTGSG CVYIQTSLRY NILPKKEGKA PFTLKVETLP KNCDGVSTHR KVQIHVNISY
TGERPSSNMV IVDVKMVSGF IPVKSSVRKV SPKSLTDSKL THHILSFFFS VEQDIAVKNL
KPATIKAYDY YETEEFTIEE YSVPCSAGKV
//
