ID A0A093HRV0_STRCA Unreviewed; 1427 AA.
AC A0A093HRV0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Alpha-2-macroglobulin {ECO:0000313|EMBL:KFV85383.1};
DE Flags: Fragment;
GN ORFNames=N308_05412 {ECO:0000313|EMBL:KFV85383.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV85383.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV85383.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV85383.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL206731; KFV85383.1; -; Genomic_DNA.
DR STRING; 441894.ENSSCUP00000016889; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
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; 2.60.40.1940; -; 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:UP000053584};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 430..578
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 702..792
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1334..1421
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV85383.1"
FT NON_TER 1427
FT /evidence="ECO:0000313|EMBL:KFV85383.1"
SQ SEQUENCE 1427 AA; 159010 MW; 5E75FCF8599AECB4 CRC64;
YMVLLPFLIH TDAPEKICVQ LTHLNESVTL SATLEYQGEN RSLIDDIVSE KDVFTCIPFS
LPKSNSTSAA LLTVLVKGAT LEFRSRKSVL VKNSESLVFV QTDKPIYKPG QTVLFRIISL
DEEFHPLNEK VELYPHLQDP QKNRVYQWQG VELETGLIQL AFPLTSDPIH GSYKIVAQKS
LMSRVEHSFS VEEYVLPKYE VLVKLPKLIT IEDKEFPVSV CGLYTYGKPV PGLVNVQVCR
KFSHSSSNCY GKEAEAVCEE FTKQADARGC VSDVVRTKIF QLQRRGYEMN IEVQGKIIED
GTGIEITGTG SCEITSIMSK ASFELLDSYY RPGIPLFGKV KLVDGTDAPV VNETIMISVD
GDRYKGNYTT DEQGQSWFSI DTTTFTEVSL EIQADHKPEL NCYDSDWVTP SYEHAMKRLS
RFYSPSKSFL KIDPKPETLS CGSTTEIRVH YIFTPEAIGE QKKVVIYYLV MAKGGIMLAD
THDLTVNPGD AYGTFLLTFP VEAAIAPLAR MLAYTTSPSG EVITSSADFQ VESCLPNKVS
LSFAPQEGLP SSNTRLQLHT SPRSLCALRA VEKSVLLMKP EDELSANSVY DLLQRKEIQG
YSFKDYYLEE DGANPCVSLD NILLNGFLYT PISPDGEGDA YDILKELGLK VFTSSKIHKP
QICQRYTGHM MERSYSGSNY TMMEQTDAGN PVETVRKYFP ETWIWEVVSV NSEGNAELDV
TIPDTITEWK ANAFCTSADA GFGLSPTVSL RAFQPFFVEL TLPYSVVRGE AFMLKATVFN
YLTACIRVSM SLAKSTHFWA TPVEKEEESY CICVNERKTV AWAVTPKSLG QVEFSVSTEA
LQDQQPCGNA IVETPEKGRK DTVIRQLLVE PEGIEVETTY NSVLCASEKS MSEPVALVLP
ENVVDGSARA YFSVLGDILG TAMQNLHQLL QMPFGCGEQN MVLFAPNIYI LDYLNKTKQL
SEEVKSKAIG YLVSGYQRQL NYKHWDGSYS TFGPRYGQAG NTWLTAFVLK SFARARPHIF
IDEKHIQDAL VWLTRKQKEN GCFHSSGTLL NNAMKGGVND EVTLTAYITI ALLEIPLPIT
HSVVRNALFC LETAADEKGS HVYTKALLAY AFALAGKEEK RRALLGSLEK EAVKKDGSVH
WQRPGKEPAV DLPYYHYRAP SAEVEMTAYV LLAHLTAQPA PSQDELSFAS LIAKWISSQQ
NPNGGFSSTQ DTVVALQALS LYGAVTYAKS GASSKVTLRS GGDFQQDFQV DPTNRLLLQR
MPLPTVPGEY STEVSGEGCV YLQTSLRYNV QPSQENAPFM LQVHTVPEMC DDSKAHRIFD
IAINVSYTGE RNVSNMVIVD VKMLSGFIPV KSSVRKLEGN QLIERTELST NHVLVYLEKL
SNTTLNFSFT VERDIPVQGL KPAQVKVYDY YETDEFAVEE YNAPCTT
//
