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
//