ID F7C733_ORNAN Unreviewed; 1409 AA.
AC F7C733;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Alpha-2-macroglobulin {ECO:0008006|Google:ProtNLM};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000022376.2, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000022376.2}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000022376.2};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SUBUNIT: Homotetramer; disulfide-linked.
CC {ECO:0000256|ARBA:ARBA00038769}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000256|ARBA:ARBA00010952}.
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DR Ensembl; ENSOANT00000022380.3; ENSOANP00000022376.2; ENSOANG00000014192.4.
DR GeneTree; ENSGT00940000154904; -.
DR HOGENOM; CLU_001634_2_1_1; -.
DR Proteomes; UP000002279; Unplaced.
DR Bgee; ENSOANG00000014192; Expressed in liver and 5 other cell types or tissues.
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; -; 3.
DR Gene3D; 2.60.40.1940; -; 1.
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; 2.
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; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11412:SF165; ALPHA-2-MACROGLOBULIN; 1.
DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
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 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
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..1409
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028034996"
FT DOMAIN 404..563
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 674..764
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1313..1400
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
FT REGION 867..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1409 AA; 155129 MW; 231F1D3A56133992 CRC64;
MGGRRLPRFS LFLLFLGLLA TNTSAAPEQY MLLISSLLHA EVPEKACILL SHLNETVTLS
AVLEYGTENR SLVANLVDDL VANKDTFHCS PFTVRGSWTT VAFLSVRVKG PTQEFRKRKA
VLVRNMQSLV FVQTDKPIYK PGQTVRFRVV SVDEDFHPLN ETVSQMDPKR NRIAQWRDVR
LRDGFGQFSF PLSSEPSQGQ YKVVVQKESG ARKEHPFTVE EFVLPKFEVL VKMPKKITIL
DEEIAVSVCG IYTYGKPVPG TVTWSVCRRF SQGQSECYGK ESEAICEEFS QQADSQGCVS
GVIETKLFQL KQQGFLMNIE AEATIREEGT ELELSGRAVC EVTKTLSKIT FEKVDSHFRR
GLPFFGQVRL LDGKDAPIPN ALVQVSVDAT HHLSNHSTDE YGLVQFSIDT SNFTTAPISV
RVTYKDSPVC YDYKWLSGNH ESAEHKAKHV YSASQNYIRL EPISDTLVCG HQQDIHKGSF
SVELLVGPEI APVMRFLIYS ILPDGEVVAD SEKFNIEKCF SNKVELQFSS IHTLPGSGAR
LRVTASPQSL CALRALDQSV LLLKAEAELS PSSVYSLLPE QDLEGFPEGL RNLGNDLRNC
TKVQPIIVNG IPFFPMDSPD EDDAYSFLKV KSLFPTEMLL LEGKQCRSKW TALNEVSWES
SVQAETVRKY FPEAWIWELL VVDTSGQSEV AVTIPDTITE WKVGAFCLSA ATGLGLAPTT
SLRAFQPFFL ELTLPYSMVR GEGFPLKATV FSYLPGCIRV SVQLEASPDF LAVPMEKGAC
SHCICGSGRL TLSWMVTPSS LGEVMFSVSA EALQSPELCG NEAAEVPEVG RKDTVIRTLL
VEPEGIEKEE TFNSLLCVKG ETLQPLMDNP APPWRGNNGE GSPRGPTSPR GDILGSALQN
LQNLLQMPYG CGEQNMVLFA PNIYVLNYLN KTQQLTPSIR AQAMGYLSSG YQRQLNYKHQ
DGSYSTFGEH HGSSQGNTWL TAFVLKALAQ ARAHIFVDEE HISSALLWLS GKQKDNGCFL
SSGSLLNNAI KGGVDNEVTL SAYITTALLE MPLPATHPVV RNALYCLETA WRAMAGNPDS
HVYTKALLAY AFALAGHEAQ RREVLQALDR DAVRAGGSIH WQRSGQAPAS IQPQGWGRAP
SAEVEMTAYV LLARLTAQPA PSPEDLSTAA LIIQWIAKQQ NAHGGFSSTQ DTVVALHALA
QYGTATFNRE GKAAVTVRSK GTFSKEFHVE DDNRLLVQQV ALAEVPGEYS ATVTGAGCVY
LQTSLRYNIV AGQGKSPIAL QVQTIPQSCS EVEAEKTFQI SISASYTGSR PASNMVIADV
KMVSGFIPLK SSVKMLQESN HVSRTEVTNN HVLIYLEQLT NETLSLTFTV TQDVLVQNLR
PAPVRVYDYY ETDEVAIVEY SAPCSTGRV
//