ID   A0A2K6EDH7_MACNE        Unreviewed;      1025 AA.
AC   A0A2K6EDH7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Alpha-2-macroglobulin domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000046215.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000046215.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   AlphaFoldDB; A0A2K6EDH7; -.
DR   Ensembl; ENSMNET00000070729.1; ENSMNEP00000046215.1; ENSMNEG00000045563.1.
DR   GeneTree; ENSGT00940000158779; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000045563; Expressed in pituitary gland and 1 other cell type or tissue.
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; -; 2.
DR   Gene3D; 2.20.130.20; -; 1.
DR   Gene3D; 2.60.40.1930; -; 2.
DR   Gene3D; 2.60.40.1940; -; 1.
DR   Gene3D; 6.20.50.160; -; 1.
DR   Gene3D; 2.60.40.690; 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; 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; IPR041555; MG3.
DR   InterPro; IPR040839; MG4.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR   PANTHER; PTHR11412:SF174; OVOSTATIN HOMOLOG 1-RELATED; 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; PF17789; MG4; 1.
DR   Pfam; PF07678; TED_complement; 2.
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.
PE   3: Inferred from homology;
KW   Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}.
FT   DOMAIN          256..385
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          480..570
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   DOMAIN          952..1025
FT                   /note="Alpha-macroglobulin receptor-binding"
FT                   /evidence="ECO:0000259|SMART:SM01361"
SQ   SEQUENCE   1025 AA;  116024 MW;  B865627F47B2D819 CRC64;
     DPQNNRIFQW QNVTSFRNIT QLSFQLISEP IFGDYWIVVK KNSGKTVTHQ FAVKRYVLPK
     FEVTVSAPQI VTISDDEFQV DVCAKYTFGQ PVQGKTQIRV CREYFSSSNC EKNDNEICEQ
     FIAQTCSTLL CSSFLTGVQI GEETSVFITQ LLGTVNFENM DTFYRRGISY FGTLKFSGPN
     NVPMVNKLLQ LELNDEFIGN YTTDENGEAQ FSIDTSDIFD PEFNLKSCYL PSWLTPQYSD
     ASFLVSRFYS RTNSFLKIVP EPKQLECNQQ KVVTVLYSLN SEAYEDGSNV KFFYLVTWNG
     NFSFPISISA DLAPVAVLFV YTLHPSGEIV ADSVRFQIDK CFKHKVNIKF SKEQGLPGSN
     ASLYLQAAPD SFCALRAVDR SVLLLKSEQQ LSAESVYNKV PSIELYGYFY RGLNLDDGKE
     DPCIPQREMF YNGLYYMPVS NYGDGDIYNI VMVRSLRNLE NISSQFLAII QTVRTNFPET
     WIWDLVSVDS SGSANLSFLI PDTITQWEAS GFCVNGDVGF GVSSTTTLEV SQPFFVEIAS
     PFSVVQNEQF DLIVNVFNYL DTCVEVSCKV NITVVAESKQ SSACPNKGME QQKLNWKDTV
     VKSFLVEVWI WDILGLAMQN LVVLQTPYGS GEQNAALLAS DTYVLDYLKS TEQLTEEVQS
     KAFFLLSNGY QRQLSFKNSD GSYSVFWQQN QKGSIWLSAL TYQTLERMKN YVFIDENVQK
     QTLIWLSSQQ KTNGCFKNDG QLFNHFPALR SALFCLEEAL DSGVTNGYNH AILAYTFALA
     GEEQKVESLL QTLDQSATKI NNVIYWERER KPKTEEFPSF IPWAPSAETE KTCYVLLAVV
     SRKIPDLTYA SKIVQWLAQQ MDSHGGFSST QVIHVGLILI ALTFSKDQNT VTFSREGSSE
     IFQVNSDNRL LVQRSELTKA PGEYTVDVEG HGCTFIQCFL KIFRYTGIHN KSSIVVTDVK
     MLSGFTPAMS SIEEVNNRSL ICQHKDSYID FTFSVEQSNL VFNIQPAPVM VYDYYEKGRQ
     ATAMP
//