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Database: UniProt
Entry: A0A094MX60_ANTCR
LinkDB: A0A094MX60_ANTCR
Original site: A0A094MX60_ANTCR 
ID   A0A094MX60_ANTCR        Unreviewed;       944 AA.
AC   A0A094MX60;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   08-NOV-2023, entry version 24.
DE   SubName: Full=Alpha-2-macroglobulin {ECO:0000313|EMBL:KFZ59056.1};
DE   Flags: Fragment;
GN   ORFNames=N321_10929 {ECO:0000313|EMBL:KFZ59056.1};
OS   Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC   Caprimulgidae; Antrostomus.
OX   NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ59056.1, ECO:0000313|Proteomes:UP000053620};
RN   [1] {ECO:0000313|EMBL:KFZ59056.1, ECO:0000313|Proteomes:UP000053620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ59056.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KL351302; KFZ59056.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094MX60; -.
DR   Proteomes; UP000053620; 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   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; 6.20.50.160; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR011625; A2M_N_BRD.
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; 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; 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; SM01419; Thiol-ester_cl; 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:UP000053620};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}.
FT   DOMAIN          292..440
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          566..656
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFZ59056.1"
FT   NON_TER         944
FT                   /evidence="ECO:0000313|EMBL:KFZ59056.1"
SQ   SEQUENCE   944 AA;  105197 MW;  4DB4F36A8D7BAF75 CRC64;
     DPQRNRIYQW QGVELETGLT QLSFPLTSEP IQGSYKIVVQ KSFSSHVEHS FSVEEYVLPK
     YEVLVKLPKM ITIKDTELPV SVCGLYTYGK PVPGLVNVQV CRKFSHSASN CYGKEAEAVC
     EEFTRQADAR GCVSGVVRTK IFQLQRRGYE MSIDVQGKIT EDGTGIEMTG TGSCGITSIM
     SKISFDLLDS QYRPGIPLFG RVKLVDGTDA PIANETIMIS VDGDRYRGNY TTDEQGQSWF
     SIDTTTFTQA SLEIRADHKP ELNCYDSDWI TPSYEHAMRR ISRFYSPSKS FLKIEPKPET
     LSCGSSTEIQ VHYIFTPEAM GEEKKIVIYY LVMAKGDIML ADTHDLTVNP GDDYGTFQLT
     FPVESAIAPL ARMLVYTTSP SGEVIASSAD FQVESCLPNK VRLNFEPKEG LPASNTRLQL
     HASPRSLCAL RAVDKSVLLM KPEDELSPSS VYDLLPLKEI RGYSFKDYYL EEDNVNPCVS
     LDNILLNGFV YIPISPDGEG DAYDILKELG LKVFTSSKIH KPEICQDYSG HMMERSYSSS
     NLDYEMTETL VAGHPVETVR KYFPETWIWD IVPVNSEGKA DLDVTIPDTI TEWKANAFCT
     SADRGFGLSP TVSLRAFQPF FVELTLPYSV VRGESFTLKA TVFNYLTACI RVSVSLAEST
     HFLAAPVENQ EESHCVCVNE RKTVAWAVTP RSLGQVEFSV STEALQNQQP CGNAIVETPE
     KGRKDTVIRQ LLVEPEGTEV ETTYNSVLCA SEKPMSEPVS LVLPEAVVDG SARAYFSVLG
     DIMGTAMQNL HQLLQMPFGC GEQNMVLFAP NIYVLDYLNK TGQLSEEVKS KAIGYLVSGY
     QRQLNYKHWD GSYSTFGPRY GQVGNTWLTA FVLKSFAQAR PHIFIDEKHI QDALVWLTQK
     QKENGCFRSS GTLLNNAMKG GVNDEITLTA YITIALLEIP LPVT
//
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