ID A0A4Y0BET4_ANOFN Unreviewed; 1322 AA.
AC A0A4Y0BET4;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Thioester-containing protein {ECO:0008006|Google:ProtNLM};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN018554-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN018554-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN018554-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR STRING; 62324.A0A4Y0BET4; -.
DR EnsemblMetazoa; AFUN018554-RA; AFUN018554-PA; AFUN018554.
DR VEuPathDB; VectorBase:AFUN018554; -.
DR VEuPathDB; VectorBase:AFUN2_011448; -.
DR Proteomes; UP000075900; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
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; 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; 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.
PE 4: Predicted;
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Thioester bond {ECO:0000256|ARBA:ARBA00022966}.
FT DOMAIN 426..556
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 631..722
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1229..1318
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1322 AA; 150832 MW; 1DDD2830E1B57FAB CRC64;
MWQFIRSPIL AVIIFIGAAH GILVVGPKFF RANQGYTVVI SSFNTNLNKG GLMLRIEGHT
DDGQNVLNIT KSVDVRKQMN RMINFYIPKD LAIGNYKITI DGLHGFTFHK EIDLVYLSKA
ISGLIQIDKP VFKPGDWVQF RVIVLDTKLK PSTRIETVQV MIRDPQDKVV RQWSSAELHV
GVFENELQIG STPILGMWKI SVLVDGEVLV SKTFEVKEYV LSSFDVEVVP TVIPLVEHQG
LNLTIAANYH FRKPVKGLAK VELFFQDDQL DQVKEFVVYG MRQVELRCTF VLNKHEDRQY
VLVRTTFTEQ DTNRTVVLVS QPTVYKYPYR VELTKESPQF RPGLPFKCTL QFRHHDGTPA
KGITGRVEVM EIEIDKTVTS DDDGLIQLEL EPIDGLQEMY ISFSNDDGFY FYEKVDKVDV
VTKAFIKLEL KSPVKINRLL QFWVTCNDRM TFFVYYIVSK GNVLESGYMA PNNQNKYPFR
LNASEKMIPK VKIVVATVVN HTLVYDCLDI DFVGLHFDFS IDKQEARPGQ QIELRLSGRS
GAYVGLAAYE KSKLYYNQHH DLFWEDLTRL YNGFGSYNEK EFDMFHNTGL FVSTLDSIKF
NEAHDMATRY ESQTNNRIIE HESNRLNVPE SWLWKNVTIG RSGTNTMIEA VPGTSPSWYL
TGFSIDPVYG LGIIKKPIEF TTILPFYIGE SLPDSIKRGE VVEFQFTLFN NLEGEYNAEV
TLYNVFNQME LIGRSLEDES YTKSVSVPPK VGVPISFLVK ARKLGAMAIR VKASIMLGRE
TDALEKVIQV EPESLVQPKM VTWFFCFDTY KNQTFRIPLD IHNKADNGSV KITLRLTTNL
LTTVFSHVLD NLLAVPSGSG EGNMIKFAPN IVVLDYLHAI GSKDKILIDK ARNLALQGYQ
HQMRYRQTDD SFGVWQNDGG SVFLTAFVAK SMQTASKYSS EVDMTLVEKA YDWLASKQHS
SGKFDEVGFM IFEEMRGGLR NGTRLTSFVV SAFLENDNAK VKHPEVIQKA MSYLSSQVDS
LDDPYELSIV TYALMLNGHS MRDKAFSRLL TMSTFTNNAT EQYWNTDHSI EATGYALMSF
VIGEKYVDGI PVMRWLVKQR YVTGVFSRAQ DIFVGLTALT RFTTKTSPSR NNYTVWLNYG
KSPAYFHISP QASNIIIYEN IPEDIKLLEV NVEGIGVGLL QVTYQYSLNL LNFENRFMLD
LEKQNTTSDD ELRLTVCANF ITKGSNERSH LALIEVTFPN GYVIEQNPIS EQTSINPIQH
TEIRYGGTSV VVYYNNMGIE RNCFTVTAYR RFKVSMKRPA YVIVYDYYDP NLNAIQSYEV
DK
//
