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Protein

Carboxypeptidase N catalytic chain

Gene

CPN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Release of a C-terminal basic amino acid, preferentially lysine.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi86Zinc; catalyticBy similarity1
Metal bindingi89Zinc; catalyticBy similarity1
Metal bindingi216Zinc; catalyticBy similarity1
Active sitei308Proton donor/acceptorBy similarity1

GO - Molecular functioni

  • metallocarboxypeptidase activity Source: ProtInc
  • serine-type carboxypeptidase activity Source: GO_Central
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000120054-MONOMER.
BRENDAi3.4.17.3. 2681.
ReactomeiR-HSA-264876. Insulin processing.

Protein family/group databases

MEROPSiM14.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase N catalytic chain (EC:3.4.17.3)
Short name:
CPN
Alternative name(s):
Anaphylatoxin inactivator
Arginine carboxypeptidase
Carboxypeptidase N polypeptide 1
Carboxypeptidase N small subunit
Kininase-1
Lysine carboxypeptidase
Plasma carboxypeptidase B
Serum carboxypeptidase N
Short name:
SCPN
Gene namesi
Name:CPN1
Synonyms:ACBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:2312. CPN1.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Carboxypeptidase N deficiency (CPND)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionPatients 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.
See also OMIM:212070
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042415178G → D in CPND. 1 PublicationCorresponds to variant rs61751507dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi1369.
MalaCardsiCPN1.
MIMi212070. phenotype.
OpenTargetsiENSG00000120054.
PharmGKBiPA26829.

Chemistry databases

ChEMBLiCHEMBL4713.
GuidetoPHARMACOLOGYi1597.

Polymorphism and mutation databases

BioMutaiCPN1.
DMDMi115896.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 201 PublicationAdd BLAST20
ChainiPRO_000000439421 – 458Carboxypeptidase N catalytic chainAdd BLAST438

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi42 ↔ 1041 Publication
Disulfide bondi271 ↔ 3111 Publication
Glycosylationi400O-linked (GalNAc...)1 Publication1
Glycosylationi402O-linked (GalNAc...)1 Publication1
Glycosylationi409O-linked (GalNAc...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP15169.
PeptideAtlasiP15169.
PRIDEiP15169.

PTM databases

iPTMnetiP15169.
PhosphoSitePlusiP15169.

Expressioni

Tissue specificityi

Synthesized in the liver and secreted in plasma.

Gene expression databases

BgeeiENSG00000120054.
CleanExiHS_CPN1.
ExpressionAtlasiP15169. baseline and differential.
GenevisibleiP15169. HS.

Organism-specific databases

HPAiHPA040323.

Interactioni

Subunit structurei

Tetramer of two catalytic chains and two glycosylated inactive chains.1 Publication

Protein-protein interaction databases

BioGridi107761. 6 interactors.
IntActiP15169. 2 interactors.
STRINGi9606.ENSP00000359446.

Chemistry databases

BindingDBiP15169.

Structurei

Secondary structure

1458
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi28 – 41Combined sources14
Helixi43 – 45Combined sources3
Beta strandi46 – 53Combined sources8
Beta strandi59 – 65Combined sources7
Beta strandi78 – 83Combined sources6
Helixi91 – 109Combined sources19
Helixi112 – 120Combined sources9
Beta strandi122 – 127Combined sources6
Helixi131 – 139Combined sources9
Turni140 – 143Combined sources4
Turni146 – 150Combined sources5
Helixi159 – 161Combined sources3
Helixi167 – 176Combined sources10
Helixi189 – 192Combined sources4
Helixi195 – 206Combined sources12
Beta strandi209 – 216Combined sources8
Beta strandi218 – 225Combined sources8
Helixi248 – 261Combined sources14
Beta strandi262 – 264Combined sources3
Helixi265 – 267Combined sources3
Helixi276 – 278Combined sources3
Beta strandi279 – 281Combined sources3
Helixi282 – 285Combined sources4
Helixi292 – 299Combined sources8
Beta strandi303 – 314Combined sources12
Helixi317 – 319Combined sources3
Helixi320 – 336Combined sources17
Beta strandi341 – 347Combined sources7
Beta strandi358 – 361Combined sources4
Beta strandi364 – 369Combined sources6
Beta strandi374 – 378Combined sources5
Beta strandi382 – 390Combined sources9
Beta strandi397 – 403Combined sources7
Beta strandi405 – 407Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NSMX-ray2.10A23-458[»]
ProteinModelPortaliP15169.
SMRiP15169.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15169.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 340CatalyticAdd BLAST320

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2649. Eukaryota.
ENOG410XX0H. LUCA.
GeneTreeiENSGT00760000119124.
HOGENOMiHOG000232185.
HOVERGENiHBG003410.
InParanoidiP15169.
KOiK01292.
OMAiDTRIHIM.
OrthoDBiEOG091G06A9.
PhylomeDBiP15169.
TreeFamiTF315592.

Family and domain databases

Gene3Di2.60.40.1120. 1 hit.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR027063. CPN1.
IPR000834. Peptidase_M14.
[Graphical view]
PANTHERiPTHR11532:SF7. PTHR11532:SF7. 1 hit.
PfamiPF00246. Peptidase_M14. 1 hit.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 1 hit.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15169-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDLLSVFLH LLLLFKLVAP VTFRHHRYDD LVRTLYKVQN ECPGITRVYS
60 70 80 90 100
IGRSVEGRHL YVLEFSDHPG IHEPLEPEVK YVGNMHGNEA LGRELMLQLS
110 120 130 140 150
EFLCEEFRNR NQRIVQLIQD TRIHILPSMN PDGYEVAAAQ GPNKPGYLVG
160 170 180 190 200
RNNANGVDLN RNFPDLNTYI YYNEKYGGPN HHLPLPDNWK SQVEPETRAV
210 220 230 240 250
IRWMHSFNFV LSANLHGGAV VANYPYDKSF EHRVRGVRRT ASTPTPDDKL
260 270 280 290 300
FQKLAKVYSY AHGWMFQGWN CGDYFPDGIT NGASWYSLSK GMQDFNYLHT
310 320 330 340 350
NCFEITLELS CDKFPPEEEL QREWLGNREA LIQFLEQVHQ GIKGMVLDEN
360 370 380 390 400
YNNLANAVIS VSGINHDVTS GDHGDYFRLL LPGIYTVSAT APGYDPETVT
410 420 430 440 450
VTVGPAEPTL VNFHLKRSIP QVSPVRRAPS RRHGVRAKVQ PQARKKEMEM

RQLQRGPA
Length:458
Mass (Da):52,286
Last modified:April 1, 1990 - v1
Checksum:i9BEF3E459E291E39
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti42C → R AA sequence (PubMed:3408501).Curated1
Sequence conflicti390T → E AA sequence (PubMed:3408501).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042415178G → D in CPND. 1 PublicationCorresponds to variant rs61751507dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14329 mRNA. Translation: CAA32507.1.
AK313972 mRNA. Translation: BAG36687.1.
CH471066 Genomic DNA. Translation: EAW49848.1.
BC027897 mRNA. Translation: AAH27897.1.
CCDSiCCDS7486.1.
PIRiA30798.
S02074.
RefSeqiNP_001299.1. NM_001308.2.
UniGeneiHs.2246.

Genome annotation databases

EnsembliENST00000370418; ENSP00000359446; ENSG00000120054.
GeneIDi1369.
KEGGihsa:1369.
UCSCiuc001kql.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14329 mRNA. Translation: CAA32507.1.
AK313972 mRNA. Translation: BAG36687.1.
CH471066 Genomic DNA. Translation: EAW49848.1.
BC027897 mRNA. Translation: AAH27897.1.
CCDSiCCDS7486.1.
PIRiA30798.
S02074.
RefSeqiNP_001299.1. NM_001308.2.
UniGeneiHs.2246.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NSMX-ray2.10A23-458[»]
ProteinModelPortaliP15169.
SMRiP15169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107761. 6 interactors.
IntActiP15169. 2 interactors.
STRINGi9606.ENSP00000359446.

Chemistry databases

BindingDBiP15169.
ChEMBLiCHEMBL4713.
GuidetoPHARMACOLOGYi1597.

Protein family/group databases

MEROPSiM14.004.

PTM databases

iPTMnetiP15169.
PhosphoSitePlusiP15169.

Polymorphism and mutation databases

BioMutaiCPN1.
DMDMi115896.

Proteomic databases

PaxDbiP15169.
PeptideAtlasiP15169.
PRIDEiP15169.

Protocols and materials databases

DNASUi1369.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370418; ENSP00000359446; ENSG00000120054.
GeneIDi1369.
KEGGihsa:1369.
UCSCiuc001kql.3. human.

Organism-specific databases

CTDi1369.
DisGeNETi1369.
GeneCardsiCPN1.
HGNCiHGNC:2312. CPN1.
HPAiHPA040323.
MalaCardsiCPN1.
MIMi212070. phenotype.
603103. gene.
neXtProtiNX_P15169.
OpenTargetsiENSG00000120054.
PharmGKBiPA26829.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2649. Eukaryota.
ENOG410XX0H. LUCA.
GeneTreeiENSGT00760000119124.
HOGENOMiHOG000232185.
HOVERGENiHBG003410.
InParanoidiP15169.
KOiK01292.
OMAiDTRIHIM.
OrthoDBiEOG091G06A9.
PhylomeDBiP15169.
TreeFamiTF315592.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000120054-MONOMER.
BRENDAi3.4.17.3. 2681.
ReactomeiR-HSA-264876. Insulin processing.

Miscellaneous databases

EvolutionaryTraceiP15169.
GeneWikiiCPN1.
GenomeRNAii1369.
PROiP15169.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000120054.
CleanExiHS_CPN1.
ExpressionAtlasiP15169. baseline and differential.
GenevisibleiP15169. HS.

Family and domain databases

Gene3Di2.60.40.1120. 1 hit.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR027063. CPN1.
IPR000834. Peptidase_M14.
[Graphical view]
PANTHERiPTHR11532:SF7. PTHR11532:SF7. 1 hit.
PfamiPF00246. Peptidase_M14. 1 hit.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 1 hit.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCBPN_HUMAN
AccessioniPrimary (citable) accession number: P15169
Secondary accession number(s): B1AP59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 2, 2016
This is version 170 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.