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Database: UniProt
Entry: A0ZWW7_DROSI
LinkDB: A0ZWW7_DROSI
Original site: A0ZWW7_DROSI 
ID   A0ZWW7_DROSI            Unreviewed;      1387 AA.
AC   A0ZWW7;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Thiolester containing protein II isoform D {ECO:0000313|EMBL:CAJ18863.1};
DE   Flags: Fragment;
GN   Name=TepII {ECO:0000313|EMBL:CAJ18863.1};
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240 {ECO:0000313|EMBL:CAJ18863.1};
RN   [1] {ECO:0000313|EMBL:CAJ18863.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Kenya line KY228 {ECO:0000313|EMBL:CAJ18863.1};
RA   Kim K.W.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAJ18863.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Kenya line KY228 {ECO:0000313|EMBL:CAJ18863.1};
RX   PubMed=17103056; DOI=10.1007/s00239-006-0005-2;
RA   Jiggins F.M., Kim K.W.;
RT   "Contrasting evolutionary patterns in Drosophila immune receptors.";
RL   J. Mol. Evol. 63:769-780(2006).
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DR   EMBL; AM050191; CAJ18863.1; -; Genomic_DNA.
DR   ChiTaRS; Tep2; fly.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
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; 2.60.40.2950; -; 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; IPR001599; Macroglobln_a2.
DR   InterPro; IPR019742; MacrogloblnA2_CS.
DR   InterPro; IPR002890; MG2.
DR   InterPro; IPR041555; MG3.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11412:SF176; GH01829P-RELATED; 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; 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; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR   PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Thioester bond {ECO:0000256|ARBA:ARBA00022966}.
FT   DOMAIN          422..556
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          657..749
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   DOMAIN          1275..1365
FT                   /note="Alpha-macroglobulin receptor-binding"
FT                   /evidence="ECO:0000259|SMART:SM01361"
FT   COILED          749..776
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAJ18863.1"
SQ   SEQUENCE   1387 AA;  154488 MW;  9E7F45779E077F30 CRC64;
     LYSVVGPGTL RSNSKYNVVV SVHKADAPSQ IKVSLNGPSY NETKQIELPP MSTQNVEFEV
     PKLATGNYNL TAEGLSGVVF KNSTKLNYAD EKPSVFVQTD KATYKPADLV QFRILFLDEN
     TRPAKIEKPI SVIITDGGQN RIKQLSDVKL TKGVFSGELQ LSEQPVLGTW KISVSVDGDN
     RETKSFEVDK YVLPKFEVIV DTPKAAVIED KVIKATIRAK YTYGKPVKGK ATVSMERSYG
     YFGNLGENDY KQEKTIDVDG KGHVEFDIIS WTQRGQYLPP LKIFAVVTEE LTGNKQNATA
     TVVLHQQRYM IEAYERPDHF EANKSFIYQV VVKNVDGSPV TSSAKNVKIG FTNTFSYFNE
     MPPVSRINYE APVNENGIAT FNVTLPDSES RYYRIFASFD RSINQLGSIS KFEPTMISRE
     PLKIQVNTKK PRLGERVSFD VVSIEDLPYF VYTIVARGNV ILSDYVDVPD GKKTFTVKFT
     PTFSMVPKAT IYVHYVVNND LQFEEKTIDF EKEFSNSIDI SAPTNAKPSE EVKLRIKTDA
     DSFVGLLGVD QSVLLLKSGN DLSQDDIFNS LNKYQTSTPW MNGYGRYPGQ TSGLVTLTNA
     NYPYNTEFPD YVEDDPGIYA FENNLEALPP MPAIANFPPD TGNTIQPVEI RKNFADVWIW
     QSIGRXXXXX XLTLTKKIPD TITSWVVTGF SLNPTSGIAL TKSPSKIRVF QPFFVSTNLP
     YSVKRGEVIA IPVVIFNYLD KTLDADVVMD NSDQEYEFTE ATNEVLEKAI DEVRRVKRVT
     IPANSGKSVS FMIRPKSVGF TTLKITATSA LAGDTIHQKL KVEPEGVTQF ENRAVFINLK
     DQPEMSQSLD AEIPSEVVPQ SEFIEFSVVG DLLGPTLQNL DNLVRMPYGC GEQNMVNFVP
     NILVLKYLEV TGRKLPSVES KARKFLEIGY QRELTYKHDD GSYSAFGKSD ASGSTWLTAY
     VMRSFHQAGT YTDIDPKVIT AGLDFLVSKQ KESGEFPEVG KLFDNANQNP LALTSFVLLA
     FFENHELIPK YQSAIEKAVR YVAEEADKTD DQYSLAIAAV ALQLAKHPQA EKVLAKLESM
     ARNENDRMWW SKTTESTGED GRVFHWKPRS NDVEITSYVL LALLEKDPAE KALPIIKWLI
     SQRNSNGGFS STQDTVIGLQ ALTKFAYKTG SGSGTMDIEF SSAGESNNTI KLNPENSLVL
     QTHVLPKSTR KVDFTAKGTG SAMVQLSYRY NLAQKEKKPS FKVTPTVKDT PNQLLVVDIC
     AEYVPLEDAD KEKDSNMAVM EIALPSGFVG DDESLSKIQA VDRVKRVETK NSDSTVVVYF
     DSLTPGDVHC LPLEASKAHA VAKQKPASVS LYDYYDTDRK ATEYYQVKSS LCDICEGADC
     GEGCKKD
//
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