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Database: UniProt
Entry: D7R6D4_BIOGL
LinkDB: D7R6D4_BIOGL
Original site: D7R6D4_BIOGL 
ID   D7R6D4_BIOGL            Unreviewed;      1445 AA.
AC   D7R6D4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Thioester-containing protein 1.2 {ECO:0000313|EMBL:ADE45339.1};
GN   Name=TEP1 {ECO:0000313|EMBL:ADE45339.1};
OS   Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Planorbidae; Biomphalaria.
OX   NCBI_TaxID=6526 {ECO:0000313|EMBL:ADE45339.1};
RN   [1] {ECO:0000313|EMBL:ADE45339.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Brazil {ECO:0000313|EMBL:ADE45339.1};
RX   PubMed=20838648;
RA   Mone Y., Gourbal B., Duval D., Du Pasquier L., Kieffer-Jaquinod S.,
RA   Mitta G.;
RT   "A large repertoire of parasite epitopes matched by a large repertoire of
RT   host immune receptors in an invertebrate host/parasite model.";
RL   PLoS Negl. Trop. Dis. 4:E813-E813(2010).
CC   -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC       macroglobulin) family. {ECO:0000256|ARBA:ARBA00010952}.
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DR   EMBL; HM038103; ADE45339.1; -; mRNA.
DR   VEuPathDB; VectorBase:BGLB021854; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
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; 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; IPR002890; MG2.
DR   InterPro; IPR041555; MG3.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11412:SF179; LD23292P; 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; SSF81296; E set domains; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR   PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PE   2: Evidence at transcript level;
KW   Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1445
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003105489"
FT   DOMAIN          463..599
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          718..808
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   DOMAIN          1342..1426
FT                   /note="Alpha-macroglobulin receptor-binding"
FT                   /evidence="ECO:0000259|SMART:SM01361"
SQ   SEQUENCE   1445 AA;  160273 MW;  EC4F0BABEB4C6262 CRC64;
     MRMKLNLILF VFYLVFQECQ GGKYFISAPR NVVPGTAYDI SVDILKQDID NVTVEAILQD
     YSFSIPEGPR SLLTANGTFS PGVRGTLSMP IDFNLHCSYC RILLKGYNPL QFEQDIFIQI
     SSDILSILIQ TDKAIYKPKE RVNFRILAAY YNLQLYTGTF HYEILDPYDN KINVLSGVSG
     TFGVVEGFFD LSDQPSFGTW KINVRTETVS GAESQFFEVA EYDLPRFQVD VGLPPFALLS
     DTTLSGSVEA KYTFGQPVYG LVLLQIGENV DTIDKCNVNR KVTEISFEIK GKGNFSVPLE
     DIRRSVHLNE KKKIKITAFV TEASTGIKLN GSSVITYYGN RYQIKFLEMT PAVFKPGLQY
     TAYVQVTTPD GLPPTDSNLS LSVYTSVTYQ MTVPDQELYS PSSFSGSYPL PGQNMSLPAN
     GILSIDIDIP LNATSIDIKV SLNKETTAEK RISKSYSMSN NYLQLSLLSK LVKAESDVLI
     KITSTEAIDS LAYEIRSRSD HVKSGVLELS GQREFNATFK VEPSWAPIAQ LLMYYIRRDS
     NEVVTDSLAF NVEGMFKNKV NVAFKENETD INKNVSLELS ADSDSQIYVL AVDQSVLLLK
     TGNDLTPNKV KDSFISKFHK GAIPTDSNFA LSYSGSSINE VFSNMGLVIA TDLNIFAPFR
     PIALGRFPSS GFDRQGMMGA PMAMSFRDDN AMESASFEMD VATSTKPVER VRSFFPESWL
     WTSVKSINGH ATLTTTVPDT ITSWIVSAFA TNSDTGLGVA PTTSKLRVFR PFFVSLTYPR
     SVTRNEQFIV QATVFNYLPV DLMVTVSLKE NPFLTPITPG PGNQASNIQV RANEQGIVYF
     SLSALTVGSL DIEVSARSNM AADAIVRQIL IKHEGAPVVY NNPILINLSN NQSTFEKNIA
     FTLPDSLVPE SQRIRVKVTG DLIGSTVQSL TSLLTLPTGC GEQSLVKFTP NIHIGRYLKA
     TNQLSEELNK KIIDLLNDGY QRQLTYKRYD NGFSAFGNYD ISSSTWLTAL VVTSFAEAQE
     FIFVDKEIIL KASMLLIDRQ NIDGSFNEFG KVLDRNTQGT TAGPALTAFV LVALLKAKEL
     ADVQDCKNNN KCRYYLLGNA TLNATRNLER LMLADSIDDQ FSLAVASYAF AEAKSQLAQS
     TFEKLLTFVK QEGGLEYWSA NSTVNNEELN RFINWRPPRL QARPIDILIT SYAILTYSSL
     GRLDEALPSV RWLTLQKNAQ GGFVSTQDTV VGLQALSSYG SKSFRPDTNI TIYVSDMNTH
     LTMNVNSENA LSLQIQEIQS NSQDFSITAS GSGLALLDIE YSFNVLKELS KPVFDVNTVL
     LDDKLDSFNI MVCTKFLMKH DTGMVVQELS IPSGFVPDLS TLGQVAGVKR SERKGSIVAI
     YFDKISGSSL CYSIVMTREA KVAKSQKSYV RTYDYYEPAN QATVFYQPRT LRDSTVCDVC
     LNCCP
//
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