(data stored in ACNUC16324 zone)

HOGENOM: PONPY3_165_PE1

ID   PONPY3_165_PE1                       STANDARD;      PRT;   750 AA.
AC   PONPY3_165_PE1; Q5RE69; Q5R5K3; Q5RFQ2;
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; EC=3.4.24.11;AltName:
DE   Full=Atriopeptidase;AltName: Full=Enkephalinase;AltName: Full=Neutral
DE   endopeptidase 24 11; Short=NEP; Short=Neutral endopeptidase;AltName:
DE   Full=Skin fibroblast elastase; Short=SFE;AltName: CD_antigen=CD10;
DE   (PONPY3_165.PE1).
GN   Name=MME;
OS   PONGO PYGMAEUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Ponginae; Pongo.
OX   NCBI_TaxID=9600;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PONPY3_165.PE1.
CC       Pongo pygmaeus chromosome 3 PPYG2 partial sequence 157801620..158629780
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:NEP_PONAB
CC   -!- FUNCTION: Thermolysin-like specificity, but is almost confined on
CC       acting on polypeptides of up to 30 amino acids. Biologically
CC       important in the destruction of opioid peptides such as Met- and
CC       Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave
CC       angiotensin-1, angiotensin-2 and angiotensin 1-9 (By similarity).
CC       Involved in the degradation of atrial natriuretic factor (ANF).
CC       Displays UV-inducible elastase activity toward skin preelastic and
CC       elastic fibers (By similarity).
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage of polypeptides between
CC       hydrophobic residues, particularly with Phe or Tyr at P1'.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M13 family.
CC   -!- GENE_FAMILY: HOG000245574 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Pongo_pygmaeus;ENSPPYG00000014224;ENSPPYT00000016535;ENSPPYP00000015904.
DR   EMBL; CR857100; - ;
DR   EMBL; CR857668; - ;
DR   EMBL; CR860855; - ;
DR   UniProtKB/Swiss-Prot; Q5RE69; Q5R5K3; Q5RFQ2; -.
DR   EMBL; CR857100; CAH89405.1; -; mRNA.
DR   EMBL; CR857668; CAH89938.1; -; mRNA.
DR   EMBL; CR860855; CAH92963.1; -; mRNA.
DR   RefSeq; NP_001126748.1; NM_001133276.1.
DR   UniGene; Pab.18628; -.
DR   HSSP; P08473; 1DMT.
DR   ProteinModelPortal; Q5RE69; -.
DR   SMR; Q5RE69; 55-750.
DR   MEROPS; M13.001; -.
DR   Ensembl; ENSPPYT00000016535; ENSPPYP00000015904; ENSPPYG00000014224.
DR   GeneID; 100173750; -.
DR   KEGG; pon:100173750; -.
DR   CTD; 4311; -.
DR   InParanoid; Q5RE69; -.
DR   OMA; TYRPEYA; -.
DR   OrthoDB; EOG4XWFXB; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; 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: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; PONPY3_165.PE1; -.
KW   ENSPPYG00000014224820036002503210000011;
KW   Q5R5K3_PONPY; Q5RE69_PONPY; Q5RFQ2_PONPY; CR857100; CR857668; CR860855;
KW   Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Protease; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Zinc.
SQ   SEQUENCE   750 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MGKSESQMDI TDINTPKPKK KQRWTPLEIS LSVLVLLLTI IAVTMIALYA TYDDGICKSS
     DCIKSAARLI QNMDATAEPC TDFFKYACGG WLKRNVIPET SSRYGNFDIL RDELEVVLKD
     VLQEPKTEDI VAVQKAKTLY RSCINESAID SRGGEPLLKL LPDVYGWPVA TENWEQKYGA
     SWTAEKAIAQ LNSKYGKKVL INLFVGTDDK NSVNHVIHID QPRLGLPSRD YYECTGIYKE
     ACTAYVDFMI SVARLIRQEE RLPIDENQLA LEMNKVMELE KEIANATAKP EDRNDPMLLY
     KKMTLAQIQN NFSLEINGKP FSWLNFTNEI MSTVNISITN EEDVVVYAPE YLTKLKPILT
     KYSARDLQNL MSWRFIMDLV SSLSRTYKES RNAFRKALYG TTSETATWRR CANYVNGNME
     NAVGRLYVEA AFAGESKHVV EDLIAQIREV FIQTLDDLTW MDAETKKRAE EKALAIKERI
     GYPDDIVSND NKLNNEYLEL NYKEDEYFEN IIQNLKFSQS KQLKKLREKV DKDEWISGAA
     VVNAFYSSGR NQIVFPAGIL QPPFFSAQQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD
     GDLVDWWTQQ SASNFKEQSQ CMVYQYGNFS WDLAGGQHLN GINTLGENIA DNGGLGQAYR
     AYQNYIKKNG EEKLLPGLDL NHKQLFFLNF AQVWCGTYRP EYAVNSIKTD VHSPGNFRII
     GTLQNSAEFS EAFHCRKNSY MNPEKKCRVW
//

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