ID   NEP_TRILK               Reviewed;         722 AA.
AC   W4VS99;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Neprilysin-1;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
OS   Trittame loki (Brush-footed trapdoor spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Barychelidae; Trittame.
OX   NCBI_TaxID=1295018;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=24351713; DOI=10.3390/toxins5122488;
RA   Undheim E.A., Sunagar K., Herzig V., Kely L., Low D.H., Jackson T.N.,
RA   Jones A., Kurniawan N., King G.F., Ali S.A., Antunes A., Ruder T.,
RA   Fry B.G.;
RT   "A proteomics and transcriptomics investigation of the venom from the
RT   barychelid spider Trittame loki (brush-foot trapdoor).";
RL   Toxins 5:2488-2503(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Contains 5 disulfide bonds. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01233, ECO:0000305}.
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DR   EMBL; GAQE01000047; JAB84507.1; -; Transcribed_RNA.
DR   AlphaFoldDB; W4VS99; -.
DR   SMR; W4VS99; -.
DR   ArachnoServer; AS001535; Neprilysin-1-Trittame loki.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd08662; M13; 1.
DR   Gene3D; 1.10.1380.10; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR000718; Peptidase_M13.
DR   InterPro; IPR018497; Peptidase_M13_C.
DR   InterPro; IPR042089; Peptidase_M13_dom_2.
DR   InterPro; IPR008753; Peptidase_M13_N.
DR   PANTHER; PTHR11733; PTHR11733; 1.
DR   Pfam; PF01431; Peptidase_M13; 1.
DR   Pfam; PF05649; Peptidase_M13_N; 1.
DR   PRINTS; PR00786; NEPRILYSIN.
DR   PROSITE; PS51885; NEPRILYSIN; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Secreted; Signal; Zinc.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..722
FT                   /note="Neprilysin-1"
FT                   /id="PRO_0000429203"
FT   DOMAIN          32..722
FT                   /note="Peptidase M13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   ACT_SITE        553
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   ACT_SITE        618
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   BINDING         552
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         556
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         614
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        424
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        609
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        33..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   DISULFID        56..707
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   DISULFID        64..667
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   DISULFID        120..378
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   DISULFID        589..719
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
SQ   SEQUENCE   722 AA;  82056 MW;  25BBD6BE9140774B CRC64;
     MAVALLVALC VVSSRMALPS EAVPFYRQDS EVCNSPVCQK AAQTLLESMD TSVDPCQDFY
     QYACGEWIRK HPIPEEKFRI SPLDALYDNV LDTVAEILKN ATSENHATSV LKSANYFQAC
     MDAEARETQG VEPLKNLLTS LGGWPMATPG WSGANYHWQT QVATVTRNLG IRPIIDVFVD
     ADANRTSQHI INLDQADFGL GRNQLINLTS SSRTQEIVAG YRNYIIASAK LLNPNADDIQ
     LANDADEIIQ FESTLAQFST PPEERRDASS WYHKMTVAEV QTVTENTYFQ WTEFLNTVLK
     EFPQVMPETE VILYERDYTK NVLKLAHETN PRILANYIGW IVLMKEGYHT TRQFRENKFQ
     FEKVQIGIEK EEKLERVCTD HTIGLLGYAV GRLYVDKFFT EEEKQDIDEL VENIRSAYKS
     TLRNNTWMDH VTRNKAIDKL EAMINKMAYP TWIKNDNELN EYYRSVPAIN RDEFFSSLLK
     VTKVVKAIQL GKWNKPTDRI KDWITTPAVV NAFYSPDSNS MSFPAGILNW PLYQYGTSPA
     LNYGAIGAII GHEMSHGFDD QGGQTDPEGN LVDWWLEETK AKFNQKADCF RKQYSSYLEP
     TTNMHLNGNN TVGENIADNG AVRNAFIAYK MHLLHSQNNH VMRKKTLPGL SATAEQLFFL
     GYSTMWCGAE RKESLEWSIQ YDSHTPSEFR AVVPLTNSRS FAEAFGCASG TPMNPTHKCL
     LW