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Database: UniProt
Entry: A0A0L7RGE6_9HYME
LinkDB: A0A0L7RGE6_9HYME
Original site: A0A0L7RGE6_9HYME 
ID   A0A0L7RGE6_9HYME        Unreviewed;      1279 AA.
AC   A0A0L7RGE6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Atrial natriuretic peptide-converting enzyme {ECO:0000313|EMBL:KOC69873.1};
GN   ORFNames=WH47_07083 {ECO:0000313|EMBL:KOC69873.1};
OS   Habropoda laboriosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Habropoda.
OX   NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC69873.1, ECO:0000313|Proteomes:UP000053825};
RN   [1] {ECO:0000313|EMBL:KOC69873.1, ECO:0000313|Proteomes:UP000053825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0110345459 {ECO:0000313|EMBL:KOC69873.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Habropoda laboriosa.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR   EMBL; KQ414598; KOC69873.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L7RGE6; -.
DR   STRING; 597456.A0A0L7RGE6; -.
DR   Proteomes; UP000053825; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00112; LDLa; 5.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 5.
DR   Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR017448; SRCR-like_dom.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   PANTHER; PTHR24252:SF8; ACROSIN; 1.
DR   PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR   Pfam; PF00057; Ldl_recept_a; 5.
DR   Pfam; PF15494; SRCR_2; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00192; LDLa; 5.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 5.
DR   SUPFAM; SSF56487; SRCR-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS01209; LDLRA_1; 4.
DR   PROSITE; PS50068; LDLRA_2; 5.
DR   PROSITE; PS50287; SRCR_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053825};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        239..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          919..975
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          1041..1273
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          641..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        743..758
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        769..787
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        781..796
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        801..813
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        808..826
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        820..835
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        859..874
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        876..888
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        883..901
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        895..910
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   1279 AA;  143209 MW;  885465427B237002 CRC64;
     MSTADGMDNP AFASEEECTT EAKLDDGQQQ VTLDQDHKSE GGPVENGHQR SQFVSQQYVE
     AGRTSPDAPY RNETRIDLPE NNDKTVVEPK MNGVHGNGNN NDASFLNNSA TSVQINDTGK
     KEQIEAVNLE LVSMRPYAGN NLQTKGQEAC EVPADPYEEY FVPVNEHRKY ISRGPEAEVE
     TTVAGVRFDL GPGVGREGLS LRDPAAGLVD YSHWLTALRG EKLYVTKDKR SRSSYWRRMA
     CWGCGLLVLL VAVIIAILAA TGVILTQEAS EPLENLQQTN SRQFGDVRTA GSQEYVKDPP
     SSPPPATSSF PPWPTTDETI YDTVPSALEG LLKLDDFRWN DDLSDPKSRV YRQVSSEIEE
     RLKNMMQQPA DNDTVVKVYD ISRNGEVRFR ISYPPQSMPE ETQQIIEQTL QLSSNMIGQY
     HLNSLKVNKL VDQCRTGGFG CSEWCEYNYS KGLFVCSCKT GKVLDNDGKT CIDENDLSNV
     EMDDEIPESN TEAVHDYVQG RSRGPGTVFE PRRPDNWDHL DFTTEKTSAG YGSSQNENEH
     EFHMHDSSAE PVATTEQNRV FKEESDPVHW AHDHSMHDDS MHDDSMHDHS MHDHSMHDHS
     MHDHPMDDHS MHDQSMHDHA MHDHSMHDHS MHDHSMHNHS MHNHSMHDHS MHDQSMHDHS
     MHDHSMHDHS AHEHLEQNTY TTITPTMYTK IPDAVVESTS HIDVSFLNLP PNVVFSKCTA
     GQFQCVNGTS RDGAYCVQLS AKCDSENDCS DGSDELNCEE EGCPGNFQCA SGQCLKRDLV
     CNKIVDCNDG SDEKNCEHWK CQFDEFRCPS GRCIPSIWQC DGRPDCEDHR DEYNCAESCG
     NDKYLCPTEK WCIPLTWHCN GISECANGED EKLCDCALDQ FKCQTGGCVP ENQVCDGIEH
     CPDHSDEWGC LMTNMTMERN LTEGQKEDEG NGNQEFGDRS SLLKIRQYNG EYRLVCSDGW
     SEELSNSYCQ ALGFSGSEST ELKAWDKNQK ILRLKSNPNH RMPLVTNLEQ MEFCVSDKVV
     QVSCQEFSCG SHYGEGPTAR LVGGTPASEG QWSGVALLKK PKHGAACTAS VLGPMHVLAS
     YSCIHRHKQS SGWQLFTGEN LLKAHPVRNI IPYPQVKYNQ FLYNNDIALV ELEKPLTFSR
     NVSAVCLPKH PIQPRQICVM VGWGFSVNGE VDLQKYLNFL PLPTLETEKC NATSHYAGFI
     TKDNICAGFT DTDKGPCYND EGAPLMCVSE SGGGSAKWEI QGLLSHHSRC SRGHPAIYSS
     VEPALSWLRH SVPALQTQS
//
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