CBPN_RAT
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-AUG-2022, entry version 127.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11021404; DOI=10.1111/j.1348-0421.2000.tb02555.x;
RA Kato T., Sato T., Matsuo S., Yamamoto T., Campbell W., Hotta N., Okada N.,
RA Okada H.;
RT "Molecular cloning and partial characterization of rat procarboxypeptidase
RT 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Protects the body from potent vasoactive and inflammatory
CC peptides containing C-terminal Arg or Lys (such as kinins or
CC anaphylatoxins) which are released into the circulation. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal basic amino acid, preferentially
CC lysine.; EC=3.4.17.3;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
CC -!- SUBUNIT: Tetramer of two catalytic chains and two glycosylated inactive
CC chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Plasma. Expressed in liver.
CC {ECO:0000269|PubMed:11021404}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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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 AlphaFoldDB; Q9EQV8; -.
DR SMR; Q9EQV8; -.
DR STRING; 10116.ENSRNOP00000018221; -.
DR MEROPS; M14.004; -.
DR GlyGen; Q9EQV8; 3 sites.
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; KOG2649; Eukaryota.
DR GeneTree; ENSGT00940000158235; -.
DR HOGENOM; CLU_006722_1_3_1; -.
DR InParanoid; Q9EQV8; -.
DR OMA; MGDYFRL; -.
DR OrthoDB; 101221at2759; -.
DR PhylomeDB; Q9EQV8; -.
DR Reactome; R-RNO-977606; Regulation of Complement cascade.
DR PRO; PR:Q9EQV8; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000013439; Expressed in liver and 5 other tissues.
DR Genevisible; Q9EQV8; RN.
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; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010815; P:bradykinin catabolic process; IMP:RGD.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; IDA:RGD.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0051384; P:response to glucocorticoid; IDA:RGD.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR027063; CPN1.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF80; PTHR11532:SF80; 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; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..457
FT /note="Carboxypeptidase N catalytic chain"
FT /id="PRO_0000042579"
FT REGION 21..340
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 418..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 308
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P14384"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 400
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 402
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 409
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT DISULFID 42..104
FT /evidence="ECO:0000250"
FT DISULFID 271..311
FT /evidence="ECO:0000250|UniProtKB:P14384"
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
