ID A0A182TH12_9DIPT Unreviewed; 547 AA.
AC A0A182TH12;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 2.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Serpin domain-containing protein {ECO:0000259|SMART:SM00093};
OS Anopheles melas.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34690 {ECO:0000313|EnsemblMetazoa:AMEC002164-PA, ECO:0000313|Proteomes:UP000075902};
RN [1] {ECO:0000313|Proteomes:UP000075902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM1001059 {ECO:0000313|Proteomes:UP000075902};
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 melas CM1001059_A (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMEC002164-PA}
RP IDENTIFICATION.
RC STRAIN=CM1001059 {ECO:0000313|EnsemblMetazoa:AMEC002164-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the serpin family.
CC {ECO:0000256|RuleBase:RU000411}.
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DR AlphaFoldDB; A0A182TH12; -.
DR STRING; 34690.A0A182TH12; -.
DR EnsemblMetazoa; AMEC002164-RA; AMEC002164-PA; AMEC002164.
DR VEuPathDB; VectorBase:AMEC002164; -.
DR Proteomes; UP000075902; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 2.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461:SF342; SERINE PROTEASE INHIBITOR 28DC; 1.
DR PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR Pfam; PF00079; Serpin; 2.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; Serpins; 1.
PE 3: Inferred from homology;
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..547
FT /note="Serpin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017677527"
FT DOMAIN 61..546
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
SQ SEQUENCE 547 AA; 61705 MW; 14D209E473DB1133 CRC64;
MRSHYSASWT LALVLLVSSL LAVSAANNRG QPAAAGQQAN RLDAPTANTK LVSDSVTNLA
AKIANALSNQ KSKTEIFSPV SIAGALSLLL LGSGGQTQQE LLTVMGLNKG QLSFQDIHLS
FGRLFQDLVS NDPSLEPLVT WRLNDKCNRY NEDEEDEEDD FINSQSPSNE VDLLIQIGNG
IFSQKGTKFD ERYDKLAKDL YQSELKPLDF VGDETGSVRY INSWVHNQTH GRIADIVSHI
SPDTILMIVN TLYFRGLWEE AFQPMATRNR RFFPNGPDGP DSFDIPMMAK SHCMPYYFWQ
EENVRVLGVP YRQNVTMYIF MPINSTRELV QSMQSKITAN RVNDIVTKMK MKSVTVMFPK
MHISNSISLK NVLQQLGVYT LFERKEADLN RLLASNTTDR FGGDPLDLLE VLQDTKENAI
FLLQQRIPDC IIEERIGIER GNCLKDHCAF GGKTCVCCIE QDDSFRRRRR RDAFTPSKND
PIFVNEMLHK VDLTVNERGT EGGAATATLI DRISSQINFI VNGPFMMVIR EETTRLPLFY
GNIYNPK
//