NPL21_CAEEL
ID NPL21_CAEEL Reviewed; 769 AA.
AC Q22523;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Neprilysin-21;
DE EC=3.4.24.-;
GN Name=nep-21; ORFNames=T16A9.4;
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-307, 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 -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01233, ECO:0000305}.
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DR EMBL; Z77135; CAB00879.1; -; Genomic_DNA.
DR PIR; T24949; T24949.
DR RefSeq; NP_506520.1; NM_074119.4.
DR AlphaFoldDB; Q22523; -.
DR SMR; Q22523; -.
DR STRING; 6239.T16A9.4b.1; -.
DR MEROPS; M13.A31; -.
DR iPTMnet; Q22523; -.
DR PaxDb; Q22523; -.
DR EnsemblMetazoa; T16A9.4a.1; T16A9.4a.1; WBGene00011794.
DR GeneID; 179925; -.
DR UCSC; T16A9.4; c. elegans.
DR CTD; 179925; -.
DR WormBase; T16A9.4a; CE18259; WBGene00011794; nep-21.
DR eggNOG; KOG3624; Eukaryota.
DR HOGENOM; CLU_006187_8_0_1; -.
DR InParanoid; Q22523; -.
DR PhylomeDB; Q22523; -.
DR PRO; PR:Q22523; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00011794; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q22523; baseline and differential.
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; IPR030082; Nep-21.
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 PANTHER; PTHR11733:SF192; PTHR11733:SF192; 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 Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..769
FT /note="Neprilysin-21"
FT /id="PRO_0000078234"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..769
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 85..769
FT /note="Peptidase M13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT ACT_SITE 602
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 667
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT BINDING 601
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 605
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 663
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 86..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 109..754
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 117..714
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 173..428
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 638..766
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
SQ SEQUENCE 769 AA; 88349 MW; EF6552CE49AA3928 CRC64;
MKPENGAATW HPAKRSCLGR LTTLETLLLV FLGLLITALL SVLFLWLWVL DGYKTFTDGR
PIYPLPFENS SVAVDRSAKN HNDVVCTSRE CVRLAGFLAE NLNSKINPCE DFYEFACGNY
GLNKNLPANK PLRHTISDVQ SRLNKQVKSM LQSPISANEK PWDKVAKGYY QKCLDEEELE
STGVEAMRDI AKRIGGWPTL EGDKWQEWSH SWEEQIALVL NLTGVNAVIL EMAVTHDPSN
SSRSVIELDQ PKWGAGSRYP YLSGANDPML RNYTTLMKMT AVALGADPAI AEKEMNEAME
FELKLVNFSA DDMVRRDPER GNNRFELWQL KSVFPFINFE KYLKTVFKEL VALSPNHTVI
VREIDYFVGI QHVLQSTPKR VLANYISWRL VQGFSPFLPP SAREPFYQFK ANQTGMFNSP
PPDRWEDCVT LSVIMMDMPV GRLFVENFFE KERAMKKMTE LTSYLKNEFI KQLHVLDWMD
EITRRRAISK ANMIEYKSGF PMVLFNDTWM EKNWGMIIKP REYLLHLTIR VKLVRFTEEL
LRLDQPLDRS MWFQSPAQVD AYYAPNNNEM IFPAGIMQFP FLTLGVPNYI TYGMVGAVIG
HEVSHAFDDQ GGQYDEMGNL NDWWDAETEE KFIEKTRCFV RQYENVHVVE ADIHLNGQLS
LGENIADNGG VKTAFNAYKA WKSNTTGISE PALPGFQNFT SQQMFFLAYA NNWCSLVRPK
HYIQIILTDV HAPSKYRAMI PLQNRPEFAK AFQCPIGSPM NPERKCQVW
