(data stored in ACNUC16324 zone)

HOGENOM: CAEELII_PE1092

ID   CAEELII_PE1092                       STANDARD;      PRT;   848 AA.
AC   CAEELII_PE1092; O16796; Q8ITZ3;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Neprilysin-2; EC=3.4.24 -; (CAEELII.PE1092).
GN   Name=nep-2; ORFNames=F18A12.8;
OS   CAENORHABDITIS ELEGANS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Pseudocoelomata; Nematoda;
OC   Chromadorea; Rhabditida; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CAEELII.PE1092.
CC       Caenorhabditis elegans chromosome II WS210  sequence 1..15279323
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:NEPL2_CAEEL
CC   -!- FUNCTION: Probable cell surface protease (By similarity).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
CC       protein.
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         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the peptidase M13 family.
CC   -!- GENE_FAMILY: HOG000245574 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Caenorhabditis_elegans;F18A12.8;F18A12.8A;F18A12.8A.
DR   EMBL; AF016688; - ;
DR   UniProtKB/Swiss-Prot; O16796; Q8ITZ3; -.
DR   EMBL; AF016688; AAB66079.2; -; Genomic_DNA.
DR   EMBL; AF016688; AAN65322.1; -; Genomic_DNA.
DR   PIR; C88099; C88099.
DR   RefSeq; NP_494538.1; NM_062137.2.
DR   RefSeq; NP_871928.1; NM_182128.2.
DR   UniGene; Cel.8808; -.
DR   HSSP; P08473; 1DMT.
DR   ProteinModelPortal; O16796; -.
DR   SMR; O16796; 163-848.
DR   MEROPS; M13.013; -.
DR   PRIDE; O16796; -.
DR   EnsemblMetazoa; F18A12.8a.1; F18A12.8a.1; F18A12.8.
DR   EnsemblMetazoa; F18A12.8a.2; F18A12.8a.2; F18A12.8.
DR   GeneID; 173685; -.
DR   KEGG; cel:F18A12.8; -.
DR   UCSC; T05A8.4; c. elegans.
DR   CTD; 173672; -.
DR   WormBase; F18A12.8a; CE23669; WBGene00017557; -.
DR   WormBase; F18A12.8b; CE32629; WBGene00017557; -.
DR   eggNOG; meNOG06744; -.
DR   GeneTree; EMGT00050000001270; -.
DR   InParanoid; O16796; -.
DR   OMA; QAVISEP; -.
DR   PhylomeDB; O16796; -.
DR   NextBio; 880655; -.
DR   ArrayExpress; O16796; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
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:InterPro.
DR   InterPro; IPR024079; MetalloPept_cat_dom.
DR   InterPro; IPR000718; Peptidase_M13.
DR   InterPro; IPR018497; Peptidase_M13_C.
DR   InterPro; IPR008753; Peptidase_M13_N.
DR   Gene3D; G3DSA:3.40.390.10; G3DSA:3.40.390.10; 2.
DR   PANTHER; PTHR11733; Peptidase_M13; 1.
DR   Pfam; PF01431; Peptidase_M13; 1.
DR   Pfam; PF05649; Peptidase_M13_N; 1.
DR   PRINTS; PR00786; NEPRILYSIN.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   HOGENOMDNA; CAEELII.PE1092; -.
KW   F18A12.81140200367fold_1320000031; F18A12.8a14.210.62fold_1320000031;
KW   AF016688;
KW   Alternative splicing; Complete proteome; Glycoprotein; Hydrolase;
KW   Membrane; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Zinc.
SQ   SEQUENCE   848 AA;  UNKNOWN MW;  UNKNOWN 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
//

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