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Database: UniProt
Entry: Q9EQV8
LinkDB: Q9EQV8
Original site: Q9EQV8 
ID   CBPN_RAT                Reviewed;         457 AA.
AC   Q9EQV8;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   19-FEB-2014, entry version 83.
DE   RecName: Full=Carboxypeptidase N catalytic chain;
DE            Short=CPN;
DE            EC=3.4.17.3;
DE   AltName: Full=Carboxypeptidase N polypeptide 1;
DE   AltName: Full=Carboxypeptidase N small subunit;
DE   Flags: Precursor;
GN   Name=Cpn1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=11021404;
RA   Kato T., Sato T., Matsuo S., Yamamoto T., Campbell W., Hotta N.,
RA   Okada N., Okada H.;
RT   "Molecular cloning and partial characterization of rat
RT   procarboxypeptidase R and carboxypeptidase N.";
RL   Microbiol. Immunol. 44:719-728(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Protects the body from potent vasoactive and
CC       inflammatory peptides containing C-terminal Arg or Lys (such as
CC       kinins or anaphylatoxins) which are released into the circulation
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Release of a C-terminal basic amino acid,
CC       preferentially lysine.
CC   -!- CATALYTIC ACTIVITY: Release of C-terminal arginine or lysine
CC       residues from polypeptides.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Tetramer of two catalytic chains and two glycosylated
CC       inactive chains (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Plasma. Expressed in liver.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
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DR   EMBL; AB042599; BAB18618.1; -; mRNA.
DR   EMBL; BC088124; AAH88124.1; -; mRNA.
DR   RefSeq; NP_445978.1; NM_053526.2.
DR   UniGene; Rn.145303; -.
DR   UniGene; Rn.162532; -.
DR   ProteinModelPortal; Q9EQV8; -.
DR   SMR; Q9EQV8; 21-418.
DR   STRING; 10116.ENSRNOP00000018221; -.
DR   MEROPS; M14.004; -.
DR   PaxDb; Q9EQV8; -.
DR   PRIDE; Q9EQV8; -.
DR   Ensembl; ENSRNOT00000018221; ENSRNOP00000018221; ENSRNOG00000013439.
DR   GeneID; 365466; -.
DR   KEGG; rno:365466; -.
DR   CTD; 1369; -.
DR   RGD; 70931; Cpn1.
DR   eggNOG; COG2866; -.
DR   GeneTree; ENSGT00730000110373; -.
DR   HOGENOM; HOG000232185; -.
DR   HOVERGEN; HBG003410; -.
DR   InParanoid; Q9EQV8; -.
DR   KO; K01292; -.
DR   OMA; RAVIQWI; -.
DR   OrthoDB; EOG7B8S32; -.
DR   NextBio; 687508; -.
DR   PRO; PR:Q9EQV8; -.
DR   Genevestigator; Q9EQV8; -.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0004180; F:carboxypeptidase activity; IDA:RGD.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0010815; P:bradykinin catabolic process; IMP:RGD.
DR   GO; GO:0006508; P:proteolysis; IDA:RGD.
DR   GO; GO:0051384; P:response to glucocorticoid; IDA:RGD.
DR   Gene3D; 2.60.40.1120; -; 1.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR014766; CarboxyPept_regulatory_dom.
DR   InterPro; IPR027063; CPN1.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11532:SF7; PTHR11532:SF7; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF49464; SSF49464; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Complete proteome; Disulfide bond; Glycoprotein;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24    457       Carboxypeptidase N catalytic chain.
FT                                /FTId=PRO_0000042579.
FT   REGION       21    340       Catalytic (By similarity).
FT   ACT_SITE    151    151       By similarity.
FT   ACT_SITE    308    308       Nucleophile (By similarity).
FT   METAL        86     86       Zinc; catalytic (By similarity).
FT   METAL        89     89       Zinc; catalytic (By similarity).
FT   METAL       216    216       Zinc; catalytic (By similarity).
FT   CARBOHYD    400    400       O-linked (GalNAc...) (By similarity).
FT   CARBOHYD    402    402       O-linked (GalNAc...) (By similarity).
FT   CARBOHYD    409    409       O-linked (GalNAc...) (By similarity).
FT   DISULFID     42    104       By similarity.
FT   DISULFID    271    311       By similarity.
SQ   SEQUENCE   457 AA;  51981 MW;  6C8FC2C5325186D9 CRC64;
     MPDLPSAFLP LLLLSKFVTP VTFRHHRYDD LVRTLYKVHN QCPDITRLYN IGRSVKGRYL
     YVLEFSDYPG THEPLEPEVK YVGNMHGNEV LGRELLLQLS EFLCEEFRNR NQRILRLIQD
     TRIHILPSMN PDGYEVAAAQ GPNTSGYLVG RNNANGVDLN RNFPDLNTYF YYNSKYGGPN
     HHLPLPDNWK SQVEPETRAV IQWIRSLNFV LSANMHGGAV VANYPYDKSL EHRFRSPHRT
     SNSPTPDDEL FQTLAKVYSY AHGWMHQGWN CGDYFPDGIT NGASWYSLSK GMQDFNYLHT
     NCFEITLELS CNKFPRQEEL QREWLGNREA LIQFLEQVHQ GIKGMVLDEN YNNLTGAVIS
     VTGINHDVTS GEHGDYFRLL LPGTYSVTAK ASGYEPKTVT VTVGPAGPTL VDFQLKRSTT
     QVHPVQKAPG RGQGSRAKQP RTSRKKDQAA KRHRGPA
//
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