NEPL1_CAEEL
ID NEPL1_CAEEL Reviewed; 754 AA.
AC Q18673; Q23453;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Neprilysin-1;
DE EC=3.4.24.-;
GN Name=nep-1; ORFNames=ZK20.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16081104; DOI=10.1016/j.jmb.2005.06.063;
RA Spanier B., Stuerzenbaum S.R., Holden-Dye L.M., Baumeister R.;
RT "Caenorhabditis elegans neprilysin NEP-1: an effector of locomotion and
RT pharyngeal pumping.";
RL J. Mol. Biol. 352:429-437(2005).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-81; ASN-132; ASN-217; ASN-273;
RP ASN-441 AND ASN-612, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Probable cell surface protease. Required to control the
CC neuronal innervation of pharyngeal pumping.
CC {ECO:0000269|PubMed:16081104}.
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: Membrane; Single-pass type II membrane protein.
CC -!- TISSUE SPECIFICITY: Specifically expressed in pharyngeal cells and a
CC single head neuron. {ECO:0000269|PubMed:16081104}.
CC -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01233, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z69904; CAA93782.2; -; Genomic_DNA.
DR EMBL; Z69902; CAA93782.2; JOINED; Genomic_DNA.
DR PIR; T20003; T20003.
DR RefSeq; NP_496490.2; NM_064089.5.
DR AlphaFoldDB; Q18673; -.
DR SMR; Q18673; -.
DR STRING; 6239.ZK20.6; -.
DR MEROPS; M13.013; -.
DR iPTMnet; Q18673; -.
DR EPD; Q18673; -.
DR PaxDb; Q18673; -.
DR PeptideAtlas; Q18673; -.
DR EnsemblMetazoa; ZK20.6.1; ZK20.6.1; WBGene00013926.
DR GeneID; 174787; -.
DR KEGG; cel:CELE_ZK20.6; -.
DR UCSC; ZK20.6.1; c. elegans.
DR CTD; 174787; -.
DR WormBase; ZK20.6; CE39118; WBGene00013926; nep-1.
DR eggNOG; KOG3624; Eukaryota.
DR GeneTree; ENSGT00940000166608; -.
DR HOGENOM; CLU_006187_8_0_1; -.
DR InParanoid; Q18673; -.
DR OMA; EKLGGWP; -.
DR OrthoDB; 282463at2759; -.
DR PhylomeDB; Q18673; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:Q18673; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00013926; Expressed in embryo and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
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; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..754
FT /note="Neprilysin-1"
FT /id="PRO_0000248421"
FT TRANSMEM 5..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 63..754
FT /note="Peptidase M13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT ACT_SITE 588
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 653
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT BINDING 587
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 591
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 649
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 87..739
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 95..699
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 151..414
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 624..751
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
SQ SEQUENCE 754 AA; 86945 MW; 49447968E4D15860 CRC64;
MYTRFGPPIV FLISCYALIL CGTVDALPRA PYFNDDINKT TTTSEDKTVG NTVVEEEKKT
YTVGDSEGYQ EASRLLQKSL NLSLDPCDDF FEYACRAWVD SHPIPDDLTS YSQFTATREK
VLAEMRKLYE DNTSIPTSKS IALIKQIYNT CMDTEKHNAV GARDLLEKIK TYGYWPMVHN
EKWRESTFDL TKLLSNTIQS RDVSVFFDFG PAEDSRNVSR RLLSFDQGSL GLGYSTRDYY
LDEKKYEKQM KAYRKYTIGK VRYYTEDAGM AVNESKIESD VDEIIAFEKE WAQILVAEED
RRNYTKLYNV RRFDDLKEYM SIIDWKKLTL STTPFLVHSY LKTNPSIIIS DVEYLQKMNT
LLQNTDPRIV TNYILLRWAG SWSQEIGKKY EDLQQEFAFQ MYGRKQRQPR WKDCVSSAGG
KLSYASGSMY VRKYFDANAK NTTLDMITDL QEAFRNMMHA NDWMDAETKK YALEKADQML
KQIGYPDFIL NDEKLDDWYK GLEGAPEDSF SQLVEKSIQW RNNFYYRRLL EPVNRFEFIS
SAAVVNAFYS PTRNAIAFPA GILQQPFFDA RFPKALNYGG IGAVIGHEIT HGFDDTGRQF
DNVGNLRDWW DNTTSSKFNE RTQCIIEQYA DVKLRGTDLR INGKLTQGEN IADNGGIKQA
FKAYKSYLEK HGGQEARLPQ FESLTNEQLF FVGYAQVWCG AKTPETKTLL LLTDPHSPET
ARVNTVLTNQ PEFAEAFKCP AGSPMNPTKR CVVW
