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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi86 – 861Zinc; catalyticBy similarity
Metal bindingi89 – 891Zinc; catalyticBy similarity
Metal bindingi216 – 2161Zinc; catalyticBy similarity
Active sitei308 – 3081Proton donor/acceptorBy similarity

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

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti178 – 1781G → D in CPND. 1 Publication
Corresponds to variant rs61751507 [ dbSNP | Ensembl ].
VAR_042415

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiCPN1.
MIMi212070. phenotype.
PharmGKBiPA26829.

Chemistry

ChEMBLiCHEMBL4713.
GuidetoPHARMACOLOGYi1597.

Polymorphism and mutation databases

BioMutaiCPN1.
DMDMi115896.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 458438Carboxypeptidase N catalytic chainPRO_0000004394Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 1041 Publication
Disulfide bondi271 ↔ 3111 Publication
Glycosylationi400 – 4001O-linked (GalNAc...)1 Publication
Glycosylationi402 – 4021O-linked (GalNAc...)1 Publication
Glycosylationi409 – 4091O-linked (GalNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP15169.
PaxDbiP15169.
PeptideAtlasiP15169.
PRIDEiP15169.

PTM databases

iPTMnetiP15169.
PhosphoSiteiP15169.

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 interactions.
IntActiP15169. 2 interactions.
STRINGi9606.ENSP00000359446.

Chemistry

BindingDBiP15169.

Structurei

Secondary structure

1
458
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 4114Combined sources
Helixi43 – 453Combined sources
Beta strandi46 – 538Combined sources
Beta strandi59 – 657Combined sources
Beta strandi78 – 836Combined sources
Helixi91 – 10919Combined sources
Helixi112 – 1209Combined sources
Beta strandi122 – 1276Combined sources
Helixi131 – 1399Combined sources
Turni140 – 1434Combined sources
Turni146 – 1505Combined sources
Helixi159 – 1613Combined sources
Helixi167 – 17610Combined sources
Helixi189 – 1924Combined sources
Helixi195 – 20612Combined sources
Beta strandi209 – 2168Combined sources
Beta strandi218 – 2258Combined sources
Helixi248 – 26114Combined sources
Beta strandi262 – 2643Combined sources
Helixi265 – 2673Combined sources
Helixi276 – 2783Combined sources
Beta strandi279 – 2813Combined sources
Helixi282 – 2854Combined sources
Helixi292 – 2998Combined sources
Beta strandi303 – 31412Combined sources
Helixi317 – 3193Combined sources
Helixi320 – 33617Combined sources
Beta strandi341 – 3477Combined sources
Beta strandi358 – 3614Combined sources
Beta strandi364 – 3696Combined sources
Beta strandi374 – 3785Combined sources
Beta strandi382 – 3909Combined sources
Beta strandi397 – 4037Combined sources
Beta strandi405 – 4073Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NSMX-ray2.10A23-458[»]
ProteinModelPortaliP15169.
SMRiP15169. Positions 21-418.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15169.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 340320CatalyticAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421C → R AA sequence (PubMed:3408501).Curated
Sequence conflicti390 – 3901T → E AA sequence (PubMed:3408501).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti178 – 1781G → D in CPND. 1 Publication
Corresponds to variant rs61751507 [ dbSNP | Ensembl ].
VAR_042415

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2NSMX-ray2.10A23-458[»]
ProteinModelPortaliP15169.
SMRiP15169. Positions 21-418.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107761. 6 interactions.
IntActiP15169. 2 interactions.
STRINGi9606.ENSP00000359446.

Chemistry

BindingDBiP15169.
ChEMBLiCHEMBL4713.
GuidetoPHARMACOLOGYi1597.

Protein family/group databases

MEROPSiM14.004.

PTM databases

iPTMnetiP15169.
PhosphoSiteiP15169.

Polymorphism and mutation databases

BioMutaiCPN1.
DMDMi115896.

Proteomic databases

MaxQBiP15169.
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.
GeneCardsiCPN1.
HGNCiHGNC:2312. CPN1.
HPAiHPA040323.
MalaCardsiCPN1.
MIMi212070. phenotype.
603103. gene.
neXtProtiNX_P15169.
PharmGKBiPA26829.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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: September 7, 2016
This is version 168 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.