(data stored in ACNUC16324 zone)

HOGENOM: RABIT14_52_PE1

ID   RABIT14_52_PE1                       STANDARD;      PRT;   750 AA.
AC   RABIT14_52_PE1; P08049;
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   (RABIT14_52.PE1).
GN   Name=MME;
OS   ORYCTOLAGUS CUNICULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RABIT14_52.PE1.
CC       Oryctolagus cuniculus chromosome 14 oryCun2 partial sequence
CC       49296255..50296254 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:NEP_RABIT
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.
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:Oryctolagus_cuniculus;ENSOCUG00000017924;ENSOCUT00000017925;ENSOCUP00000015401.
DR   EMBL; M16593; - ;
DR   EMBL; X05338; - ;
DR   UniProtKB/Swiss-Prot; P08049; -.
DR   EMBL; X05338; CAA28950.1; -; mRNA.
DR   EMBL; M16593; AAA53694.1; -; mRNA.
DR   PIR; A29451; HYRBN.
DR   RefSeq; NP_001095155.1; NM_001101685.1.
DR   UniGene; Ocu.2011; -.
DR   ProteinModelPortal; P08049; -.
DR   SMR; P08049; 55-750.
DR   STRING; P08049; -.
DR   MEROPS; M13.001; -.
DR   Ensembl; ENSOCUT00000017925; ENSOCUP00000015401; ENSOCUG00000017924.
DR   GeneID; 100009251; -.
DR   CTD; 4311; -.
DR   eggNOG; maNOG15085; -.
DR   GeneTree; ENSGT00550000074200; -.
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; RABIT14_52.PE1; -.
KW   ENSOCUG00000017924820036002503210000011;
KW   NEP_RABIT; M16593; X05338;
KW   Cell membrane; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Protease; Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
SQ   SEQUENCE   750 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MGRSESQMDI TDINTPKPKK KQRWTPLEIS LSVLVLLLTV IAVTMIALYA TYDDGICKSS
     DCIKSAARLI QNMDATAEPC TDFFKYACGG WLKRNVIPET SSRYSNFDIL RDELEVILKD
     VLQEPKTEDI VAVQKAKTLY RSCVNETAID SRGGQPLLKL LPDVYGWPVA TQNWEQTYGT
     SWSAEKSIAQ LNSKYGKKVL INFFVGTDDK NSMNHIIHID QPRLGLPSRD YYECTGIYKE
     ACTAYVDFMI AVAKLIRQEE GLPIDENQIS VEMNKVMELE KEIANATTKS EDRNDPMLLY
     NKMTLAQIQN NFSLEINGKP FSWSNFTNEI MSTVNINIPN EEDVVVYAPE YLIKLKPILT
     KYSPRDLQNL MSWRFIMDLV SSLSRTYKDS RNAFRKALYG TTSESATWRR CANYVNGNME
     NAVGRLYVEA AFAGESKHVV EDLIAQIREV FIQTLDDLTW MDAETKKKAE EKALAIKERI
     GYPDDIVSND NKLNNEYLEL NYKEDEYFEN IIQNLKFSQS KQLKKLREKV DKDEWITGAA
     IVNAFYSSGR NQIVFPAGIL QPPFFSAQQS NSLNYGGIGM VIGHEITHGF DDNGRNFNKD
     GDLVDWWTQQ SANNFKEQSQ CMVYQYGNFS WDLAGGQHLN GINTLGENIA DNGGIGQAYR
     AYQNYVKKNG EEKLLPGIDL NHKQLFFLNF AQVWCGTYRP EYAVNSIKTD VHSPGNFRII
     GSLQNSVEFS EAFQCPKNSY MNPEKKCRVW
//

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