NPL11_CAEEL
ID NPL11_CAEEL Reviewed; 848 AA.
AC O16796; Q8ITZ3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Neprilysin-11;
DE EC=3.4.24.-;
GN Name=nep-11; ORFNames=F18A12.8;
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], AND ALTERNATIVE SPLICING.
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-726, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-726, AND IDENTIFICATION BY MASS
RP 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. {ECO:0000250}.
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: Cell membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=O16796-1; Sequence=Displayed;
CC Name=b;
CC IsoId=O16796-2; Sequence=VSP_020295;
CC -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01233, ECO:0000305}.
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DR EMBL; FO080567; CCD64733.1; -; Genomic_DNA.
DR EMBL; FO080567; CCD64734.1; -; Genomic_DNA.
DR PIR; C88099; C88099.
DR RefSeq; NP_494538.1; NM_062137.3. [O16796-1]
DR RefSeq; NP_871928.1; NM_182128.3.
DR AlphaFoldDB; O16796; -.
DR SMR; O16796; -.
DR BioGRID; 39042; 1.
DR STRING; 6239.F18A12.8a; -.
DR MEROPS; M13.A16; -.
DR iPTMnet; O16796; -.
DR EPD; O16796; -.
DR PaxDb; O16796; -.
DR PeptideAtlas; O16796; -.
DR PRIDE; O16796; -.
DR EnsemblMetazoa; F18A12.8a.1; F18A12.8a.1; WBGene00017557. [O16796-1]
DR EnsemblMetazoa; F18A12.8b.1; F18A12.8b.1; WBGene00017557.
DR GeneID; 173685; -.
DR KEGG; cel:CELE_F18A12.8; -.
DR UCSC; T05A8.4; c. elegans. [O16796-1]
DR CTD; 173685; -.
DR WormBase; F18A12.8a; CE23669; WBGene00017557; nep-11. [O16796-1]
DR WormBase; F18A12.8b; CE32629; WBGene00017557; nep-11.
DR eggNOG; KOG3624; Eukaryota.
DR GeneTree; ENSGT00940000164877; -.
DR HOGENOM; CLU_006187_4_0_1; -.
DR InParanoid; O16796; -.
DR OMA; RGARDYY; -.
DR OrthoDB; 282463at2759; -.
DR PhylomeDB; O16796; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:O16796; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00017557; Expressed in larva 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 Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Zinc.
FT CHAIN 1..848
FT /note="Neprilysin-11"
FT /id="PRO_0000248422"
FT TOPO_DOM 1..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..848
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 160..848
FT /note="Peptidase M13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT REGION 108..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 683
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 748
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT BINDING 682
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 686
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 744
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 726
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT DISULFID 161..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 184..833
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 192..793
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 247..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 719..845
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT VAR_SEQ 791..843
FT /note="FWCGKKKEAAAMQQVLTDEHSPEVFRVIGVLSNMQAFADVYKCPRNAPVNPD
FT H -> VSCLPVLKFVVKLAKMNQSFTKNPSD (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020295"
SQ SEQUENCE 848 AA; 97062 MW; 4548FFEE5A915DA4 CRC64;
MPFGNDPPDY VHLRSNESQM QLITISENSD IPTPSGSPCF NAPARDEAPS VIFIPGKKFQ
GTFRWWKSRT TMEKLLLPVL LLFCLLTAVL LAVIINTDKR IEAMKTDHAT QTEHAGFGDP
TENPTKTAED PRVPPIVPEA PTSPEPEVTT STEKPKEPEV CSTPGCVRAA THFLNAMNTS
VDPCDDFFEF ACGQWNDQHP IPDDMYGFGT FAYAREQVRQ QLRVLLEQEV VTESESINMA
RATYRSCMNK TQLDELMTGP LFETLTELGE WPLLQENWDK TKFNFTSLLV NSRRDYGVDV
FFQLYIYADS KNTSRNTLFI DQSTLALGRG TRDYYLNTTL FSSHMTAYRK YLRQIAHLLK
TDGNLTRSES EMNADIEKII DFEIELAKII VAEDERRNNT RLYNKRQIQD LYNLLPQVDW
VPFFQSIAPS DLTHLFHNET EIIICEIEYL QHVSELIEKT DVGLLTNYVL WRVVQSNVRY
LDERFEDIKQ DFLKVMTGQQ QSPPRWKDCA QVPSTVLPLA AGAIYVQAHF QESDKHEALR
MIMHLRNSFA DLVRQNDWMD EETKAVAIEK ANSMINNIGY PDVTNDLPKL DKQYLGLSIS
DSDTYYYIMK KSVVWMQSRE FQKLTKPFDK HEFDISPAVV NAFYSPEKNA ITFPAGILQP
PFFSGTFPKA VNYGAIGAVI GHEITHGFDD QGSQYDKDGN LHNWWSESSL NSFDTRRRCI
VEQYGNYTVP KTNFRVNGKL TQGENIADNG GVKEAFQAYQ KYVTENGEEP RLPGLQQYTN
EQIFFVSYAH FWCGKKKEAA AMQQVLTDEH SPEVFRVIGV LSNMQAFADV YKCPRNAPVN
PDHKCIVW
