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Carboxypeptidase N catalytic chain (CPN) (EC 3.4.17.3) (Anaphylatoxin inactivator) (Arginine carboxypeptidase) (Carboxypeptidase N polypeptide 1) (Carboxypeptidase N small subunit) (Kininase-1) (Lysine carboxypeptidase) (Plasma carboxypeptidase B) (Serum carboxypeptidase N) (SCPN)

 CBPN_HUMAN              Reviewed;         458 AA.
P15169; B1AP59;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
27-SEP-2017, entry version 176.
RecName: Full=Carboxypeptidase N catalytic chain;
Short=CPN;
EC=3.4.17.3;
AltName: Full=Anaphylatoxin inactivator;
AltName: Full=Arginine carboxypeptidase;
AltName: Full=Carboxypeptidase N polypeptide 1;
AltName: Full=Carboxypeptidase N small subunit;
AltName: Full=Kininase-1;
AltName: Full=Lysine carboxypeptidase;
AltName: Full=Plasma carboxypeptidase B;
AltName: Full=Serum carboxypeptidase N;
Short=SCPN;
Flags: Precursor;
Name=CPN1; Synonyms=ACBP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2912725; DOI=10.1111/j.1432-1033.1989.tb14488.x;
Gebhard W., Schube M., Eulitz M.;
"cDNA cloning and complete primary structure of the small, active
subunit of human carboxypeptidase N (kininase 1).";
Eur. J. Biochem. 178:603-607(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 21-67; 162-190; 329-343 AND 379-416.
PubMed=3408501; DOI=10.1016/0006-291X(88)90284-7;
Skidgel R.A., Bennett C.D., Schilling J.W., Tan F., Weerasinghe D.K.,
Erdoes E.G.;
"Amino acid sequence of the N-terminus and selected tryptic peptides
of the active subunit of human plasma carboxypeptidase N: comparison
with other carboxypeptidases.";
Biochem. Biophys. Res. Commun. 154:1323-1329(1988).
[6]
3D-STRUCTURE MODELING.
PubMed=8267877;
Hendriks D., Vingron M., Vriend G., Wang W., Nalis N., Scharpe S.;
"On the specificity of carboxypeptidase N, a comparative study.";
Biol. Chem. Hoppe-Seyler 374:843-849(1993).
[7]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 21-458, SUBUNIT, DISULFIDE
BONDS, AND GLYCOSYLATION AT THR-400; THR-402 AND THR-409.
PubMed=17157876; DOI=10.1016/j.jmb.2006.11.025;
Keil C., Maskos K., Than M., Hoopes J.T., Huber R., Tan F.,
Deddish P.A., Erdos E.G., Skidgel R.A., Bode W.;
"Crystal structure of the human carboxypeptidase N (kininase I)
catalytic domain.";
J. Mol. Biol. 366:504-516(2007).
[8]
VARIANT CPND ASP-178.
PubMed=12560874; DOI=10.1007/s100380300003;
Cao H., Hegele R.A.;
"DNA polymorphism and mutations in CPN1, including the genomic basis
of carboxypeptidase N deficiency.";
J. Hum. Genet. 48:20-22(2003).
-!- FUNCTION: Protects the body from potent vasoactive and
inflammatory peptides containing C-terminal Arg or Lys (such as
kinins or anaphylatoxins) which are released into the circulation.
-!- CATALYTIC ACTIVITY: Release of a C-terminal basic amino acid,
preferentially lysine.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P00730};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
-!- SUBUNIT: Tetramer of two catalytic chains and two glycosylated
inactive chains. {ECO:0000269|PubMed:17157876}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space.
-!- TISSUE SPECIFICITY: Synthesized in the liver and secreted in
plasma.
-!- DISEASE: Carboxypeptidase N deficiency (CPND) [MIM:212070]:
Patients affected present some combination of angioedema or
chronic urticaria, as well as hay fever or asthma, and have also
slightly depressed serum carboxy peptidase N, suggestive of
autosomal recessive inheritance of this disorder.
{ECO:0000269|PubMed:12560874}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X14329; CAA32507.1; -; mRNA.
EMBL; AK313972; BAG36687.1; -; mRNA.
EMBL; CH471066; EAW49848.1; -; Genomic_DNA.
EMBL; BC027897; AAH27897.1; -; mRNA.
CCDS; CCDS7486.1; -.
PIR; A30798; A30798.
PIR; S02074; S02074.
RefSeq; NP_001299.1; NM_001308.2.
UniGene; Hs.2246; -.
PDB; 2NSM; X-ray; 2.10 A; A=23-458.
PDBsum; 2NSM; -.
ProteinModelPortal; P15169; -.
SMR; P15169; -.
BioGrid; 107761; 6.
IntAct; P15169; 2.
STRING; 9606.ENSP00000359446; -.
BindingDB; P15169; -.
ChEMBL; CHEMBL4713; -.
GuidetoPHARMACOLOGY; 1597; -.
MEROPS; M14.004; -.
iPTMnet; P15169; -.
PhosphoSitePlus; P15169; -.
BioMuta; CPN1; -.
DMDM; 115896; -.
PaxDb; P15169; -.
PeptideAtlas; P15169; -.
PRIDE; P15169; -.
DNASU; 1369; -.
Ensembl; ENST00000370418; ENSP00000359446; ENSG00000120054.
GeneID; 1369; -.
KEGG; hsa:1369; -.
UCSC; uc001kql.3; human.
CTD; 1369; -.
DisGeNET; 1369; -.
EuPathDB; HostDB:ENSG00000120054.11; -.
GeneCards; CPN1; -.
HGNC; HGNC:2312; CPN1.
HPA; HPA040323; -.
MalaCards; CPN1; -.
MIM; 212070; phenotype.
MIM; 603103; gene.
neXtProt; NX_P15169; -.
OpenTargets; ENSG00000120054; -.
PharmGKB; PA26829; -.
eggNOG; KOG2649; Eukaryota.
eggNOG; ENOG410XX0H; LUCA.
GeneTree; ENSGT00760000119124; -.
HOGENOM; HOG000232185; -.
HOVERGEN; HBG003410; -.
InParanoid; P15169; -.
KO; K01292; -.
OMA; RNRNQRI; -.
OrthoDB; EOG091G06A9; -.
PhylomeDB; P15169; -.
TreeFam; TF315592; -.
BRENDA; 3.4.17.3; 2681.
Reactome; R-HSA-264876; Insulin processing.
Reactome; R-HSA-977606; Regulation of Complement cascade.
EvolutionaryTrace; P15169; -.
GeneWiki; CPN1; -.
GenomeRNAi; 1369; -.
PRO; PR:P15169; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000120054; -.
CleanEx; HS_CPN1; -.
ExpressionAtlas; P15169; baseline and differential.
Genevisible; P15169; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
GO; GO:0030141; C:secretory granule; IBA:GO_Central.
GO; GO:0097060; C:synaptic membrane; IBA:GO_Central.
GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0010815; P:bradykinin catabolic process; IEA:Ensembl.
GO; GO:0030070; P:insulin processing; IBA:GO_Central.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
InterPro; IPR008969; CarboxyPept-like_regulatory.
InterPro; IPR027063; CPN1.
InterPro; IPR000834; Peptidase_M14.
PANTHER; PTHR11532:SF62; PTHR11532:SF62; 1.
Pfam; PF00246; Peptidase_M14; 1.
PRINTS; PR00765; CRBOXYPTASEA.
SMART; SM00631; Zn_pept; 1.
SUPFAM; SSF49464; SSF49464; 1.
PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
1: Evidence at protein level;
3D-structure; Carboxypeptidase; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
Reference proteome; Secreted; Signal; Zinc.
SIGNAL 1 20 {ECO:0000269|PubMed:3408501}.
CHAIN 21 458 Carboxypeptidase N catalytic chain.
/FTId=PRO_0000004394.
REGION 21 340 Catalytic.
ACT_SITE 308 308 Proton donor/acceptor.
{ECO:0000250|UniProtKB:P14384}.
METAL 86 86 Zinc; catalytic.
{ECO:0000250|UniProtKB:P00730}.
METAL 89 89 Zinc; catalytic.
{ECO:0000250|UniProtKB:P00730}.
METAL 216 216 Zinc; catalytic.
{ECO:0000250|UniProtKB:P00730}.
CARBOHYD 400 400 O-linked (GalNAc...) threonine.
{ECO:0000305|PubMed:17157876}.
CARBOHYD 402 402 O-linked (GalNAc...) threonine.
{ECO:0000305|PubMed:17157876}.
CARBOHYD 409 409 O-linked (GalNAc...) threonine.
{ECO:0000305|PubMed:17157876}.
DISULFID 42 104 {ECO:0000269|PubMed:17157876}.
DISULFID 271 311 {ECO:0000269|PubMed:17157876}.
VARIANT 178 178 G -> D (in CPND; dbSNP:rs61751507).
{ECO:0000269|PubMed:12560874}.
/FTId=VAR_042415.
CONFLICT 42 42 C -> R (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 390 390 T -> E (in Ref. 5; AA sequence).
{ECO:0000305}.
HELIX 28 41 {ECO:0000244|PDB:2NSM}.
HELIX 43 45 {ECO:0000244|PDB:2NSM}.
STRAND 46 53 {ECO:0000244|PDB:2NSM}.
STRAND 59 65 {ECO:0000244|PDB:2NSM}.
STRAND 78 83 {ECO:0000244|PDB:2NSM}.
HELIX 91 109 {ECO:0000244|PDB:2NSM}.
HELIX 112 120 {ECO:0000244|PDB:2NSM}.
STRAND 122 127 {ECO:0000244|PDB:2NSM}.
HELIX 131 139 {ECO:0000244|PDB:2NSM}.
TURN 140 143 {ECO:0000244|PDB:2NSM}.
TURN 146 150 {ECO:0000244|PDB:2NSM}.
HELIX 159 161 {ECO:0000244|PDB:2NSM}.
HELIX 167 176 {ECO:0000244|PDB:2NSM}.
HELIX 189 192 {ECO:0000244|PDB:2NSM}.
HELIX 195 206 {ECO:0000244|PDB:2NSM}.
STRAND 209 216 {ECO:0000244|PDB:2NSM}.
STRAND 218 225 {ECO:0000244|PDB:2NSM}.
HELIX 248 261 {ECO:0000244|PDB:2NSM}.
STRAND 262 264 {ECO:0000244|PDB:2NSM}.
HELIX 265 267 {ECO:0000244|PDB:2NSM}.
HELIX 276 278 {ECO:0000244|PDB:2NSM}.
STRAND 279 281 {ECO:0000244|PDB:2NSM}.
HELIX 282 285 {ECO:0000244|PDB:2NSM}.
HELIX 292 299 {ECO:0000244|PDB:2NSM}.
STRAND 303 314 {ECO:0000244|PDB:2NSM}.
HELIX 317 319 {ECO:0000244|PDB:2NSM}.
HELIX 320 336 {ECO:0000244|PDB:2NSM}.
STRAND 341 347 {ECO:0000244|PDB:2NSM}.
STRAND 358 361 {ECO:0000244|PDB:2NSM}.
STRAND 364 369 {ECO:0000244|PDB:2NSM}.
STRAND 374 378 {ECO:0000244|PDB:2NSM}.
STRAND 382 390 {ECO:0000244|PDB:2NSM}.
STRAND 397 403 {ECO:0000244|PDB:2NSM}.
STRAND 405 407 {ECO:0000244|PDB:2NSM}.
SEQUENCE 458 AA; 52286 MW; 9BEF3E459E291E39 CRC64;
MSDLLSVFLH LLLLFKLVAP VTFRHHRYDD LVRTLYKVQN ECPGITRVYS IGRSVEGRHL
YVLEFSDHPG IHEPLEPEVK YVGNMHGNEA LGRELMLQLS EFLCEEFRNR NQRIVQLIQD
TRIHILPSMN PDGYEVAAAQ GPNKPGYLVG RNNANGVDLN RNFPDLNTYI YYNEKYGGPN
HHLPLPDNWK SQVEPETRAV IRWMHSFNFV LSANLHGGAV VANYPYDKSF EHRVRGVRRT
ASTPTPDDKL FQKLAKVYSY AHGWMFQGWN CGDYFPDGIT NGASWYSLSK GMQDFNYLHT
NCFEITLELS CDKFPPEEEL QREWLGNREA LIQFLEQVHQ GIKGMVLDEN YNNLANAVIS
VSGINHDVTS GDHGDYFRLL LPGIYTVSAT APGYDPETVT VTVGPAEPTL VNFHLKRSIP
QVSPVRRAPS RRHGVRAKVQ PQARKKEMEM RQLQRGPA


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