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Database: UniProt
Entry: A0A3Q1J6W2_ANATE
LinkDB: A0A3Q1J6W2_ANATE
Original site: A0A3Q1J6W2_ANATE 
ID   A0A3Q1J6W2_ANATE        Unreviewed;      1386 AA.
AC   A0A3Q1J6W2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Alpha-2-macroglobulin-like protein 1 {ECO:0008006|Google:ProtNLM};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000027034.2, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000027034.2}
RP   IDENTIFICATION.
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; ENSATET00000027462.2; ENSATEP00000027034.2; ENSATEG00000019407.2.
DR   GeneTree; ENSGT00940000162996; -.
DR   Proteomes; UP000265040; Unplaced.
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; 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; IPR041555; MG3.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR   PANTHER; PTHR11412:SF150; ZGC:171445 PROTEIN-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; 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:UP000265040};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}.
FT   DOMAIN          415..558
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          685..774
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   DOMAIN          1296..1380
FT                   /note="Alpha-macroglobulin receptor-binding"
FT                   /evidence="ECO:0000259|SMART:SM01361"
SQ   SEQUENCE   1386 AA;  153088 MW;  35D38BF2C85D5721 CRC64;
     MIQADFHQPF NTRWETIHTL CFIGFKFSGA KTKFCASLLQ PNESLLMTVT LISEETNTTL
     LTNTSTATVC KIFSQVPLVQ EEAIYNLTVE VQGGTFYSKE VRKVMIKVYQ PVIFVQTDKP
     IYLPGQTGNL LSVLVKYNLF WLNETSNSKI LQLSYSLNSD AREGNYEIIV SMGENKVYQN
     FKVEKYVLPK FAVTINSSDE VGIGQKEIKA QVCANYTYGQ PVPGSVTIGM CRLLQQYIND
     QIVPGLTSPC HNETKQVCLL YHMQSLYVLN LRATVEEQGT GVLQSEEKTI SISYVVGRLS
     FIDTPKIYNK TSNVQGKVSV KAVYYNNTPI PELPVYLFEG EMWSSHQLQN LTTDSKGIAT
     FSLSTANYSG DIHLQVSSTP SLEYPGYRTP YYETGDQMLS IAQPVSPDTK SGSFLVVKEK
     DKPLSCNVEE IIYIQYTIVG EAQGSVDVIY LVLSRGAIIT QGFKNVQVQV NEGDVSFKLK
     VSPDMAPDVQ IVAYAVLPSA TVIADSADFS TEKCFSQNVS LEFFPPSAVP GEQTVLQVKA
     EPGSLCGVSA VDQSVFIKEP GKKLDADEIF NLLPVTKASY IPYEVLDPTV CLTVRARRNI
     LPYRQWADAY TVFQNVGLKM ATNLFIQMPS CLKFKGREYY PGDFLHAKYK GTNLVAVLAI
     PAPERMDSFT NGPPVVTVRT FFPETWLWKL VDVGTSGIKN LPLTVPDTIT TWETEAFCLS
     PLGFGLAPSK EITVFQPFFL DLTLPYSIIR GEQFELKATA FNYLTSCIML TVTPARSSDY
     TLTPFSGYQY ASCLCSSERK TISWIMVPST LGTVNVSVTA MALASQTACN GNKVSVPERG
     RVDTVTKALV VKAEGSEMSK TYNWLLCPKG QNLLEEVDIQ LPKNVIVGSA RASLSVLGDI
     LGRALKNLNG LLQMPYGCGE QNMALLAPNI YILQYLKNTQ QLTPAIKEKA TNFLTSGYQR
     QLNYKDDAGA YSTFGSGPGN TWLTAFVLRS FTKAQTFIYI DPTTIEESLT WLENKQQKNG
     CFEQSGKLFN NRMKGGVSDE VTLTAYITAA FLEMNISVNS PVITKSLSCL KESISDLSNT
     YTTALLAYVF TLAGDVKTRS RLLQHLDTVA LKQGGFLYWS QTAAETSASL SVEISSYVLL
     AKLGASPTAQ DLGYSSSIVR WLTGQQNYYG GFSSTQDTVV ALQALALYST LVFSPQGSST
     VTVQSPSGQL TFDVNQDNKL LYQEKTLQDT IGKYSLEVKG TACASVQISL TYNIPTPIKV
     TTLAVEVKPE AGNCKSIRPK LTLKIKSLYS GKEKSTNMVI LDIKMLSGFV PDSESLRSLR
     NGTLVNNVQQ VDDHILVYIQ EVRGIYTVDH TLVLVQELPV QNLKPAVVKI YDYYQTSKTF
     IPCLQP
//
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