(data stored in ACNUC16324 zone)

HOGENOM: RAT2_PE929

ID   RAT2_PE929                           STANDARD;      PRT;   750 AA.
AC   RAT2_PE929; P07861;
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   (RAT2.PE929).
GN   Name=Mme;
OS   RATTUS NORVEGICUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RAT2.PE929.
CC       Rattus norvegicus chromosome 2 RGSC3.4  sequence 1..258207540
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:NEP_RAT
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. Displays UV-
CC       inducible elastase activity toward skin preelastic and elastic
CC       fibers (By similarity). Involved in the degradation of atrial
CC       natriuretic factor (ANF).
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.
CC   -!- ENZYME REGULATION: Inhibited in a dose dependent manner by
CC       sialorphin.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the peptidase M13 family.
CC   -!- GENE_FAMILY: HOG000245574 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Rattus_norvegicus;ENSRNOG00000009514;ENSRNOT00000042576;ENSRNOP00000044578.
DR   EMBL; BC085753; - ;
DR   EMBL; M15944; - ;
DR   UniProtKB/Swiss-Prot; P07861; -.
DR   EMBL; M15944; AAA41116.1; -; mRNA.
DR   EMBL; BC085753; AAH85753.1; -; mRNA.
DR   IPI; IPI00231789; -.
DR   PIR; A29295; HYRTN.
DR   RefSeq; NP_036740.1; NM_012608.2.
DR   UniGene; Rn.33598; -.
DR   ProteinModelPortal; P07861; -.
DR   SMR; P07861; 55-750.
DR   STRING; P07861; -.
DR   MEROPS; M13.001; -.
DR   PRIDE; P07861; -.
DR   Ensembl; ENSRNOT00000042576; ENSRNOP00000044578; ENSRNOG00000009514.
DR   GeneID; 24590; -.
DR   KEGG; rno:24590; -.
DR   UCSC; NM_012608; rat.
DR   CTD; 4311; -.
DR   RGD; 3098; Mme.
DR   eggNOG; roNOG08854; -.
DR   GeneTree; ENSGT00550000074200; -.
DR   InParanoid; P07861; -.
DR   OMA; TYRPEYA; -.
DR   OrthoDB; EOG4XWFXB; -.
DR   PhylomeDB; P07861; -.
DR   NextBio; 603776; -.
DR   ArrayExpress; P07861; -.
DR   Genevestigator; P07861; -.
DR   GermOnline; ENSRNOG00000009514; Rattus norvegicus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001950; C:plasma membrane enriched fraction; IDA:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0042277; F:peptide binding; IDA:RGD.
DR   GO; GO:0006518; P:peptide metabolic process; IMP:RGD.
DR   GO; GO:0006508; P:proteolysis; IDA:RGD.
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; RAT2.PE929; -.
KW   ENSRNOG00000009514820036002503210000011;
KW   Mme; NEP_RAT; BC085753; M15944;
KW   Cell membrane; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Zinc.
SQ   SEQUENCE   750 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MGRSESQMDI TDINAPKPKK KQRWTPLEIS LSVLVLLLTI IAVTMIALYA TYDDGICKSS
     DCIKSAARLI QNMDASAEPC TDFFKYACGG WLKRNVIPET SSRYSNFDIL RDELEVILKD
     VLQEPKTEDI VAVQKAKTLY RSCINESAID SRGGQPLLTL LPDIYGWPVA SQNWEQTYGT
     SWTAEKSIAQ LNSKYGKKVL INFFVGTDDK NSTQHIIHFD QPRLGLPSRD YYECTGIYKE
     ACTAYVDFMI SVARLIRQEQ RLPIDENQLS LEMNKVMELE KEIANATTKP EDRNDPMLLY
     NKMTLAKLQN NFSLEINGKP FSWSNFTNEI MSTVNINIQN EEEVVVYAPE YLTKLKPILT
     KYSPRDLQNL MSWRFIMDLV SSLSRNYKES RNAFRKALYG TTSETATWRR CANYVNGNME
     NAVGRLYVEA AFAGESKHVV EDLIAQIREV FIQTLDDLTW MDAETKKKAE EKALAIKERI
     GYPDDIISNE NKLNNEYLEL NYKEEEYFEN IIQNLKFSQS KQLKKLREKV DKDEWISGAA
     VVNAFYSSGR NQIVFPAGIL QPPFFSARQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD
     GDLVDWWTQQ SANNFKDQSQ CMVYQYGNFT WDLAGGQHLN GINTLGENIA DNGGIGQAYR
     AYQNYVKKNG EEKLLPGLDL NHKQLFFLNF AQVWCGTYRP EYAVNSIKTD VHSPGNFRII
     GTLQNSAEFA DAFHCRKNSY MNPERKCRVW
//

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