ID A0A182W9H7_9DIPT Unreviewed; 1328 AA.
AC A0A182W9H7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 2.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Thioester-containing protein 1 {ECO:0008006|Google:ProtNLM};
OS Anopheles minimus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN007005-PA, ECO:0000313|Proteomes:UP000075920};
RN [1] {ECO:0000313|Proteomes:UP000075920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles minimus MINIMUS1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMIN007005-PA}
RP IDENTIFICATION.
RC STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN007005-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR STRING; 112268.A0A182W9H7; -.
DR EnsemblMetazoa; AMIN007005-RA; AMIN007005-PA; AMIN007005.
DR VEuPathDB; VectorBase:AMIN007005; -.
DR OrthoDB; 3431519at2759; -.
DR Proteomes; UP000075920; 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; -; 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; 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 629..720
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1236..1325
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1328 AA; 151465 MW; 4BB1391C8391A01D CRC64;
MWQFISSRIL TVIIFIGAAH GMLVVGPKFI RANQNYTVAI SNLHPSLRKV NLKLCIDGHT
DGGSKVLIET KTIEVGWNTN EQITFNIPEN LPAGNYKFTV DGQRGFSFHK ETDLKYLRKS
IAGLIQISKP VFKPGDTVQF RVIVLDPELR PPARVNTIHV RIYDPQKNVI RQWPWARLQT
GVFENELQIA PTPMLGIWNI SVLMNGEELV SKTFEVKEYV LSSFDVNVYP SIIPLESHQA
LLLTIKADYH FGKPVIGLAK VELYLEDDEL DQRKEIEVYG KRLVELRFKE KLSLYEPQQN
VRVRTTFIEK HTNRTVVKDA PITVYKHKYR VELIKESPQF RPAYSFKCAL QFRFHDGTPA
TGITGEVKVD EIGYHETATS DNNGLIKLVL LPNKDINEMT ISYSNEDGFF YEEQVGKANV
VTDTYFKLKL TNPVKLNEML QLTVRCNKQM TFFVYYVVSK GNIIDTGYIS SRNQNDYILK
ATEKMLPKAR IIVATVVNRI MVYDVVDIHF EELHNNFNMS IDEQIVQPGQ QVELRMTGRP
GAYVGLAAYD KGLLYYNHDL FWEDFMQVFD GFHSVEENAY DKFHSAGLFR MLGDDIIIKV
AEDISARDGL LKIFPFSKSE WHRTKFPESW LWQNDTIGRF GIRTIAVAVP DTTTSWYLTG
FSIDPEYGFG IIKKPIQLTT IQPFYIVENL PYSIKRGEVV ELHFTLFNYL GGEHIADVTL
YNVDNQLEFV ERPLEELNYT KSVTVPSNIG VPISFSVKAR KLGEVVICVK ATILAGWKTD
ALEKVIQVTP ESLVQSYMHS RSFCSDTYIN QTFSFYTDID KKADNESKKI EFRLIPNLLP
AVLNNLDGLL ALPSGNGEQN MLHLGPNIVV LDYLRAIGSK DQNLIDKATS LIRQGYHKQM
RYRRLDGSFG VLQNLTGGTF LTAFVAKSMQ TASKYISEVD MVKIEKAFDW LATKQRSSGR
FYEVDTVNYN DMRGGLRNGI SLTSYVVTAL LENENARVKH AVVIQRAMNY LSSQMESINN
AYDLSIATYA LMLNGHIMKD KAFQMLLQMS TLKNNNVERF WQTPNSIEAT AYALLSFVIA
EKYVDGIPVM RWLANQRYVT GSLPRTQDTF VGLKALTKMA EKISPSRNNY TIQFKIRERF
QKLFLQYTNG TKMIHINSEA SDVINFELPE LLNQFGLSVS GNGCGSFNLF YQYSINLMNI
RNQFVLELQK QNTGSNYELQ LNVCASFIPT ITDRHSNMVT VEVTLPSGYV VDRNPISEQT
AAIAKLAFDV RYGGTSVVVY YANMDDKQNC FTVNAFPQGK VTLKRPAYVV VYDTINPNWN
AIKMYEMD
//