ID A0ZWT1_DROME Unreviewed; 1398 AA.
AC A0ZWT1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Thiolester containing protein II, isoform A {ECO:0000313|EMBL:CAJ00621.1};
DE Flags: Fragment;
GN Name=TepII {ECO:0000313|EMBL:CAJ00621.1};
GN ORFNames=CG7052 {ECO:0000313|EMBL:CAJ00621.1};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:CAJ00621.1};
RN [1] {ECO:0000313|EMBL:CAJ00621.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Gabon line G191 {ECO:0000313|EMBL:CAJ00621.1};
RA Kim K.W.;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAJ00621.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Gabon line G191 {ECO:0000313|EMBL:CAJ00621.1};
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; AJ973633; CAJ00621.1; -; Genomic_DNA.
DR PeptideAtlas; A0ZWT1; -.
DR VEuPathDB; VectorBase:FBgn0041182; -.
DR ChiTaRS; Tep2; fly.
DR ExpressionAtlas; A0ZWT1; baseline and differential.
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 673..760
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1286..1376
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
FT COILED 760..787
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAJ00621.1"
SQ SEQUENCE 1398 AA; 155886 MW; BBA2A8C1E7B9A3E1 CRC64;
IYSVVGPGTL RSNSKYNVVV SVHKADGPSQ IKVSLNGPSY NETKQIELPP MSTQNVEFEV
PKLATGNYNL TAEGLSGVVF KNSTKLNYAD KKPSVFVQTD KATYKPADLV QFRILFLDEN
TRPAKIKKPI SVIITDGAQN RIKQLSDVKP TKGVFSGELQ LSEQPVLGTW KISVSVDGDN
RETKSFEVDK YVLPKFEVVV DTPKAVVIAD KVIKATIRAK YTYGKPVKGK ATVSMERSYG
YFGDLNANGN KQEKTIDVDG KGHVEFDIIH WAQRGQYLPP IKLFAVVTEE LTGNKQNATA
TVVLHQQRYS IEPYERPEHF EANKSFIYQV VVKNVDGSPV TNSAKNVKIG FDKSYSYFHE
PSPKTRINFE APVNENGIAT FNVRLPDSDS RYYRIFASFD GSENTIGSIS KFEPTLMSRE
PLKIQVNTKK PRLGEQVSFD VVSIKDLPYF VYTIVARGNV ILSDYVDVSD GQKSYTVKFT
PTFSMVPKAT IYVYYVVNND LQFEEKTIDF EKEFSNSIDI SAPTNAKPSE EVKLRIKTDA
DSFVGLLGVD QSVLLLKSGN DLSQDDIFNS LNIYQTSTPW MNGYGRYPGQ TSGLVTLTNA
NYPYNTGPLV MSYVFEGSRH PWITRPRYRV GIRGDSGDRI SFLSQSLNDR NLKEILLKQT
PQRTTIRKEF PETWFFENVG EEFTLTKKIP DTITSWVVTG FSLNPTSGIA LTKNPSKIRV
FQPFFVSTNL PYSVKRGEVI AIPVVIFNYL DKTLDADVVM DNSDQEYEFT EATNEVLEKA
IDEVRRVKRV TIPANSGKSV SFMIRPKNVG FTTLKITATS ALAGDAIHQK LKVEPEGVTL
FENRAVFINL KDQPEMSQSL DADIPNEVVP QSEFIEFSVV GDLLGPTLQN LDNLVRMPYG
CGEQNMVNFV PNILVLKYLE VTGRKLPSVE SKARKFLEIG YQRELTYKHD DGSYSAFGKS
DASGSTWLTA YVMRSFHQAG TYTDIDPKVI TAGLDFLVSK QKESGEFPEV GKLFDNANQN
PLALTSFVLL AFFENHELIP KYQSAIKKAV RYVAEEADKT DDQYSLAIAA VALQLAKHPQ
SEKVIAKLES VARKENDRMW WSKATESTGE DGRVFHWKPR SNDVEITSYV LLALLEKDPA
EKALPIIKWL ISQRNSNGGF SSTQDTVIGL QALTKFAYKT GSGSGTMDIE FSSAGESKNT
IKVNPENSLV LQTHDLPKST RKVDFTAKGT GSAMVQLSYR YNLAEKEKKP SFKVTPTVKD
TPNQLLIVDI CAEYVPLEDA DKDKDSNMAV MEIALPSGFV GDSTSLGKIQ AVDRVKRVET
KNSDSTVVVY FDSLTPGDVR CLPLEASKAH AVAKQKPASV SLYDYYDTER KATEYYQVKS
SLCDICEGAD CGEGCKKD
//
