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Database: UniProt
Entry: A0ZWW9_DROSI
LinkDB: A0ZWW9_DROSI
Original site: A0ZWW9_DROSI 
ID   A0ZWW9_DROSI            Unreviewed;      1378 AA.
AC   A0ZWW9;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Thiolester containing protein II isoform B {ECO:0000313|EMBL:CAJ18865.1};
DE   Flags: Fragment;
GN   Name=TepII {ECO:0000313|EMBL:CAJ18865.1};
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:CAJ18865.1};
RN   [1] {ECO:0000313|EMBL:CAJ18865.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Kenya line KY236 {ECO:0000313|EMBL:CAJ18865.1};
RA   Kim K.W.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAJ18865.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Kenya line KY236 {ECO:0000313|EMBL:CAJ18865.1};
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; AM050192; CAJ18865.1; -; 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          649..740
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   DOMAIN          1266..1356
FT                   /note="Alpha-macroglobulin receptor-binding"
FT                   /evidence="ECO:0000259|SMART:SM01361"
FT   COILED          740..767
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAJ18865.1"
SQ   SEQUENCE   1378 AA;  153768 MW;  A641BF28C5A6130A CRC64;
     LYSVVGPGTL RSNSKYNVVV SVHKADAPSQ IKVSLNGPSY NETKQIELPP MSTQNVEFEV
     PKLATGNYNL TAEGLSGVVF KNSTKLNYAD EKPSVFVQTD KATYKPADLV QFRILFLDEN
     TRPAKIEKPI SVIITDGAQN RIKQLNDVKL TKGVFSGELQ LSEQPVLGTW KISVSVDGDN
     RETKSFEVDK YVLPKFEVIV DTPKAAVIED KVIKATIRAK YTYGKPVKGK ATVSMERSYG
     YFGNLGENDY KQEKTIDVDG KGHVEFDIIS WTQRGQYLPP VKLFAVVTEE LTGNKQNATA
     TVVLHQQRYM IEAYERPDHF EANKSFIYQV VVKNVDGSPV TSSAKNVKIG FTNTFSYFIE
     MPPVSRINYE APVNENGIAT FNVTLPDSES RYYRIFASFD RSINQLGSIS KFEPTMISRE
     PLKIQVNTKK PRLGERVSFD VVSIEDLPYF VYTIVARGNV ILSDYVDVPD GKKTFTVKFT
     PTFSMVPKAT IYVHYVVNND LQFEEKTIDF EKEFSNSIDI SAPTNAKPSE EVKLRIKTDA
     DSFVGLLGVD QSVLLLKSGN DLSQDDIFNS LNKYQTSTPW MNGYGRYPGQ TSGLVTLTNA
     NYPYNTERRI FIRPGIGFPR PLFNRVTVTG SLAQNVLTEP QVRKEFPENW IFNIFEXXXX
     XXLTLTKKIP DTITSWVVTG FSLNPTSGIA LTKSPSKIRV FQPFFVSTNL PYSVKRGEVI
     AIPVVIFNYL DKTLDADVVM DNSDQEYEFT EATNEVLEKA IDEVRRVKRV TIPANSGKSV
     SFMIRPKSVG FTTLKITATS ALAGDTIHQK LKVEPEGVTQ FENRAVFINL KDQPEMSQSL
     DAEIPSEVVP QSEFIEFSXX XXLLGPTLQN LDNLVRMPYG CGEQNMVNFV PNILVLKYLE
     VTGRKLPSVE SKARKFLEIG YQRELTYKHD DGSYSAFGKS DASGSTWLTA YVMRSFHQAG
     TYTDIDPKVI TAGLDFLVSK QKESGEFPEV GKLFDNANQN PLALTSFVLL AFFENHELIP
     KYQGAIEKAV RYVAEEADKT DDQYSLAIAA VALQLAKHPQ AEKVLAKLES MARNENDRMW
     WSKTTESTGE DGRVFHWKPR SNDVEITSYV LLALLEKDPA EKALPIIKWL ISQRNSNGGF
     SSTQDTVIGL QALTKFAYKT GSGSGTMDIE FSAAGESNNT IKVNPENSLV LQTHVLPKST
     RKVDFTAKGT GSAMVQLSYR YNLAQKEKKP SFKVTPTVKD TPNQLLVVDI CAEYVPLEDA
     DKEKDSNMAV MEIALPSGFV GDDESLSKIQ AVDRVKRVET KNSDSTVVVY FDSLTPGDVH
     CLPLEASKAH AVAKQKPASV SLYDYYDTER KATEYYQVKS SLCEICEGAD CGEGCKKD
//
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