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Database: UniProt
Entry: B5AZN2_ANOAR
LinkDB: B5AZN2_ANOAR
Original site: B5AZN2_ANOAR 
ID   B5AZN2_ANOAR            Unreviewed;      1291 AA.
AC   B5AZN2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=TEP1 {ECO:0000313|EMBL:ACG68535.1};
DE   Flags: Fragment;
OS   Anopheles arabiensis (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7173 {ECO:0000313|EMBL:ACG68535.1};
RN   [1] {ECO:0000313|EMBL:ACG68535.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ToMB10_S {ECO:0000313|EMBL:ACG68535.1};
RX   PubMed=18840262; DOI=10.1186/1471-2148-8-274;
RA   Obbard D.J., Callister D.M., Jiggins F.M., Soares D.C., Yan G.,
RA   Little T.J.;
RT   "The evolution of TEP1, an exceptionally polymorphic immunity gene in
RT   Anopheles gambiae.";
RL   BMC Evol. Biol. 8:274-274(2008).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   EMBL; EU881835; ACG68535.1; -; Genomic_DNA.
DR   VEuPathDB; VectorBase:AARA008889; -.
DR   VEuPathDB; VectorBase:AARA21_010641; -.
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; -; 2.
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; 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; IPR040839; MG4.
DR   InterPro; IPR049135; TEP1_CUB2.
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; PF17789; MG4; 1.
DR   Pfam; PF07678; TED_complement; 1.
DR   Pfam; PF21412; TEP1_CUB2; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Thioester bond {ECO:0000256|ARBA:ARBA00022966}.
FT   DOMAIN          376..508
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          583..674
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   DOMAIN          1180..1269
FT                   /note="Alpha-macroglobulin receptor-binding"
FT                   /evidence="ECO:0000259|SMART:SM01361"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACG68535.1"
SQ   SEQUENCE   1291 AA;  146765 MW;  1884ACE73F6EE273 CRC64;
     VDLLLKLEGE TDNGLSVLNV TKMVDVRRNM NRMINFNMPE DLTAGNYKIT IDGQRGFSFH
     KEAELVYLSK SISGLIQVDK PVFKPGDTVN FRVIVLDTEL KPPARVKSVY VTIRDPQRNV
     IRKWSTAKLY AGVFESDLQI APTPMLGVWN ISVEVEGEEL VSKTFEVKEY VLSTFDVQVM
     PSVIPLEEHQ ALNLTIEANY HFGKPVQGVA KVELYLEDDK LNQKKELTVY GKGQVELRFD
     NFAMDADQQD VRVKVSFIEQ YTNRTVVKQS EITVYRYAYR VELIKESPQF RPGLPFKCAL
     QFTHHDGTPA KGISGKVEVS DVGFETTTMS DNDGLIKLEL QPSEGTEQLG INFNAVDGFF
     FYEDVNKVET VTDAYIKLEL KSPIKRNKLM RFMVTCTERM TFFVYYVMSK GNIIDAGFMR
     PNKQTKYLLQ LNATEKMIPK AKILIATVAG RTVVYDYADL DFQELRNNFD LSIDEQEIKP
     GRQIELSMSG RPGAYVGLAA YDKALLLFNK NHDLFWEDIG QVFDGFHAIN ENEFDIFHSL
     GLFARTLDDI LFDSANEKTG RNALQSGKPI GKLVSYRTNF QESWLWKNVS IGRSGSRKLI
     EVVPDTTTSW YLTGFSIDPV YGLGIIKKPI QFTTVQPFYI VENLPYSIKR GEAVVLQFTL
     FNNLGAEYIA DVTLYNVANQ TEFVGRPDTD LSYTKSVSVP PKVGVPISFL IKARKLGEMA
     VRVKASIMLG HETDALEKVI RVMPESLAQP KMDTSFFCFD DYKNQTFPFN LDINKKADNG
     SKKIEFRLNP NLLTMVIKNL DNLLAVPTGC GEQNMVKFVP NILVLDYLYA TGSKEQHLID
     KATNLLRQGY QNQMRYRQTD GSFGVWEKSG SSVFLTAFVA TSMQTASKYM NDIDAAMVEK
     ALDWLASKQH SSGRFDETGK VWHKDMQGGL RNGVALTSYV LTALLENDIA KVKHVVVIQN
     GMNYLSNQLA LINNPYDLSI ATYAMMLNGH TMKKEALDKL IDMSISDNNK KERYWGTTNQ
     IETTAYALLS FVMAEKYLDG IPVMNWLVNQ RYVTGSFPRT QDTFVGLKAL TKLAEKISPS
     RNDYTVQLKY KKNTKYFNIN SEQIDVQNFL EIPEDTKKLE INVGGIGFGL LEVIYQFDLN
     LVNFEHRFKL DLEKQNTGSD YELRLRVCAN YIPELTDSQS NMALIEVTLP SGYVVDRNPI
     SEQTTVNPIQ NMEIRYGGTS VVLYYYNMGT ERNCFTVTAY RRFKVALKRP AYVVVYDYYN
     TNLNAIKVYE VDKQNVCEIC EEEDCPAECK K
//
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