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Entry: A0ZWV0_DROSI
LinkDB: A0ZWV0_DROSI
Original site: A0ZWV0_DROSI 
ID   A0ZWV0_DROSI            Unreviewed;      1375 AA.
AC   A0ZWV0;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Thiolester containing protein II isoform C {ECO:0000313|EMBL:CAJ18846.1};
DE   Flags: Fragment;
GN   Name=TepII {ECO:0000313|EMBL:CAJ18846.1};
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:CAJ18846.1};
RN   [1] {ECO:0000313|EMBL:CAJ18846.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Kenya line KY219 {ECO:0000313|EMBL:CAJ18846.1};
RA   Kim K.W.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAJ18846.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Kenya line KY219 {ECO:0000313|EMBL:CAJ18846.1};
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; AM050188; CAJ18846.1; -; 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          638..729
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   DOMAIN          1255..1345
FT                   /note="Alpha-macroglobulin receptor-binding"
FT                   /evidence="ECO:0000259|SMART:SM01361"
FT   COILED          729..756
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAJ18846.1"
SQ   SEQUENCE   1375 AA;  153036 MW;  F76939F5D05CB20F CRC64;
     LYSVVGPGTL RSNSKYNVVV SVHKADGPSQ IKVSLNGPSY NETKQIELPP MSTQNVEFEV
     PKLSTGNYNL TAEGLSGVVF KNSTKLNYAD EKPSVFVQTD KATYKPADLV QFRILFLDEN
     TRPAKIEKPI SVIITDGAQN RIKQLSDVKL TKGVFSGELQ LSEQPVLGTW KISVSVDGDN
     RETKSFEVDK YVLPKFEVIV DTPKAAVIDD KVIKATIRAK YTYGKPVKGK ATVSMERSYG
     YFGNPGGNDY KQEKTIDVDG KGHVEFDIIS WTQRGQYLPP VKLFAVVTEE LTGNKQNATA
     TVVLHQQRYM IEAYERPDHF EANKSFIYQV VVKNVDGSPV TSSAKNVKIG FTNTFSYFNE
     MPPVSRINYE APVNENGIAT FNVTLPDSKS RYYRIFASFD RSMSHLGSIS NFEPTIISRE
     PLKIQVNTKK PRLGERVSFD VVSIEDLPYF VYTIVARGNV ILSDYVDVPD GKKTFTVKFT
     PTFSMVPKAT IYVHYVVNND LQFEEKTIDF EKEFSNSIDI SAPTNAKPSE EVKLRIKTDA
     DSFVGLLGVD QSVLLLKSGN DLSQDDIFNS LNKYQTSTPW MNGYGRYPGQ TSGLVTLTNA
     NYPYNTDFAI AFSLAEEAPG MGSPPTSPPK IRKEFPENWI FYNAEXXXXX XLTLTKKIPD
     TITSWVVTGF SLNPTSGIAL TKSPSKIRVF QPFFVSTNLP YSVKRGEVIA IPVVIFNYLD
     KTLDADVIMD NSDQEYEFTE ATNEVLEKAI DEVRRVKRVT IPANSGKSVS FMIRPKSVGF
     TTLKITATSA LAGDTIHQKL KVEPEGVTQF ENRAVFINLK DQPEMSQSLD AEIPTEVVPQ
     SEFIEFSXXX XLLGPTLQNL DNLVRMPYGC GEQNMVNFVP NILVLKYLEV TGRKLPSVES
     KARKFLEIGY QRELTYKHDD GSYSAFGKSD ASGSTWLTAY VMRSFHQAGT YTDIDPKVIT
     AGLDFLVSKQ KESGEFPEVG KLFDNANQNQ LALTSFVLLA FFENHELIPK YQGAIEKAVR
     YVAEEADKTD DQYSLAIAAV ALQLAKHPQA EKVLAKLESM ARNENDRMWW SKTTESTGED
     GRVFHWKPRS NDVEITSYVL LALLEKDPAE KALPIIKWLI SQRNSNGGFS STQDTVIGLQ
     ALTKFAYKTG SGSGTMDIEF SSAGESNNTI KVNPENSLVL QTHVLPKSTR KVDFTAKGTG
     SAMVQLSYRY NLAQKEKKPS FKVTPTVKDT PNQLLVVDIC AEYVPLEDAD KEKDSNMAVM
     EIALPSGFVG DDESLGKIQA VDRVKRVETK NSDSTVVVYF DSLTPGDVRC LPLEASKAHA
     VAKQKPASVS LYDYYDTDRK ATEYYQVKSS LCDICEGADC GEGCKKDWGP GVKRW
//
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