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Database: UniProt
Entry: A0A182QNI5_9DIPT
LinkDB: A0A182QNI5_9DIPT
Original site: A0A182QNI5_9DIPT 
ID   A0A182QNI5_9DIPT        Unreviewed;      1313 AA.
AC   A0A182QNI5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Alpha-2-macroglobulin domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Anopheles farauti.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF013745-PA, ECO:0000313|Proteomes:UP000075886};
RN   [1] {ECO:0000313|Proteomes:UP000075886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., 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 farauti FAR1 (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AFAF013745-PA}
RP   IDENTIFICATION.
RC   STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF013745-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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DR   EMBL; AXCN02002079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 69004.A0A182QNI5; -.
DR   EnsemblMetazoa; AFAF013745-RA; AFAF013745-PA; AFAF013745.
DR   VEuPathDB; VectorBase:AFAF013745; -.
DR   OrthoDB; 3416528at2759; -.
DR   Proteomes; UP000075886; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   CDD; cd02891; A2M_like; 1.
DR   Gene3D; 1.50.10.20; -; 1.
DR   Gene3D; 2.60.120.1540; -; 1.
DR   Gene3D; 2.60.40.1930; -; 2.
DR   Gene3D; 2.60.40.1940; -; 1.
DR   Gene3D; 2.60.40.690; 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; 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; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11412:SF176; GH01829P-RELATED; 1.
DR   PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR   Pfam; PF00207; A2M; 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; SM01361; A2M_recep; 1.
DR   SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Thioester bond {ECO:0000256|ARBA:ARBA00022966}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1313
FT                   /note="Alpha-2-macroglobulin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008133225"
FT   DOMAIN          617..707
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   DOMAIN          1220..1309
FT                   /note="Alpha-macroglobulin receptor-binding"
FT                   /evidence="ECO:0000259|SMART:SM01361"
SQ   SEQUENCE   1313 AA;  148321 MW;  7D5411D5EC98FD17 CRC64;
     MRSYAFVYWL LLCTFVGTTF GYEWSSVSIL NVHTDAGRDN VSLILANLDD VPSTFEIENI
     GMEDGDVFVS TTVDPKQVQL YVLPREWNTG NSLDAVQLDI TTDGTRLEGQ IMLTQQPKVL
     IQLNNVLHTP GDYVTFRILL TDELNRPLAS TEQPFNMTIN LVHETQHTVR SLAIQLHAGS
     IYSYQHLLKD NRDLGEWKIT VTIGEETTSK RFQVVLHSNP IHKIALKTGR LNTIRDEALR
     INVEALYTFG KPIRGMLTLH AGGDRTVEHK SAIDGSKIVT IPMEELLTEQ SRNGVSSKTI
     RINATVATHN GLTGRSYHQS KTIPVYVQPY KIVLEPLVDF KAGQNVTVLV RAVQANGDPL
     DDIGSFSNRL SVSVRQETEE TVLTNHFKQL LNDDGTAVLM IPTHEFTENL TVRVQYREVK
     ASLVLEPLAY IPRLHVHFKT ASSILKQSEG FTLTIASSHP MDTVLAVVHL HSGVNVPLMI
     DCSWKNYHEQ YISQRVAEVR RVYVFARFDE VLVQASTPYL EAPMRHVVHL AIENSTIKVR
     TKEHSSRVGI AVYEGLLDAE QLENIYAHGM FNGTVYPETQ DVKPLNEVIE SSPPEKPEDG
     NDNDVKLNSN APIINRVILW QDKLVRKHEA TFHAYIPPHV NQWTVSAFAF SPTAGLGIAE
     PVQWHRKQDI EIYLHVPYSA KKLEEVTVDV YIVNNVNRQH SAVLVELLNT ANEFHFLNND
     GRIDAIKKTV LGRLKPYEVQ RAEFLIRPKK VGSITITANA YAQDIVVARA EKILRTIPES
     LEQTDEIMRM FSLDNSEQNF DNIKLTIPHQ VDAGSEKIIF SLHEQQQTSA SFLVNLLLDR
     LVQADPFTTA IKAALTLEVL ALGGVEWTER SITAADLINQ SVRKILSYAN EDGSFTIPDD
     HAPASACWDT VISLQALTFA NKQMETVELE GAIRKTLDWL KHRQNKDGGF CADDQANGVE
     ITAHILMTFM NAGKSMQHYV TIIDSMRNYL LSSTSGLKDP YLLALVGHVL QQSAKSVTRE
     QERALIDVTL TYIVEELFQQ KKQNPSKSKM WWSSSTVSDM DVTSYALMFL SSKRFILNAG
     PTVNWIKRQP FRRTEPTITP NSHLALRALI EYAKRTIFLR EQYMATIVAT NNTHELLRHQ
     MTHENTEHVI DLPANTRSVS FSIKGTVTGA FVINYSYLQS VTTKFQKFNI NVQRYESSNE
     DYTDWKVCIR FMPKGTFDKT NMVSCEISFP TGYIVLDDSV DEINDLADVV STALRNDETL
     FTITFEEIGV MEKCFNVTGF RRNVETRRLP GMIRVFDVTD ANNVAFTQFD TQT
//
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