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 03-APR-2013, entry version 77.
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 IPI; IPI00190500; -.
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 Ensembl; ENSRNOT00000018221; ENSRNOP00000018221; ENSRNOG00000013439.
DR GeneID; 365466; -.
DR KEGG; rno:365466; -.
DR CTD; 1369; -.
DR RGD; 70931; Cpn1.
DR eggNOG; COG2866; -.
DR GeneTree; ENSGT00680000099712; -.
DR HOGENOM; HOG000232185; -.
DR HOVERGEN; HBG003410; -.
DR InParanoid; Q9EQV8; -.
DR KO; K01292; -.
DR OrthoDB; EOG4JM7PN; -.
DR NextBio; 687508; -.
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:0006508; P:proteolysis; IDA:RGD.
DR GO; GO:0051384; P:response to glucocorticoid stimulus; 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; CarboxypepD_reg; 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
//
