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Protein

Mast cell carboxypeptidase A

Gene

CPA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi176 – 1761ZincBy similarity
Metal bindingi179 – 1791ZincBy similarity
Metal bindingi304 – 3041ZincBy similarity
Active sitei378 – 3781NucleophileBy similarity

GO - Molecular functioni

  1. metallocarboxypeptidase activity Source: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. angiotensin maturation Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.17.1. 2681.
ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.

Protein family/group databases

MEROPSiM14.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Mast cell carboxypeptidase A (EC:3.4.17.1)
Short name:
MC-CPA
Alternative name(s):
Carboxypeptidase A3
Gene namesi
Name:CPA3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:2298. CPA3.

Subcellular locationi

  1. Cytoplasmic vesiclesecretory vesicle

  2. Note: Secretory granules.

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. secretory granule Source: UniProtKB
  3. transport vesicle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26818.

Polymorphism and mutation databases

BioMutaiCPA3.
DMDMi317373331.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Add
BLAST
Propeptidei16 – 10994Activation peptide1 PublicationPRO_0000004395Add
BLAST
Chaini110 – 417308Mast cell carboxypeptidase APRO_0000004396Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi173 ↔ 186By similarity
Disulfide bondi245 ↔ 268By similarity

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP15088.
PRIDEiP15088.

2D gel databases

OGPiP15088.

PTM databases

PhosphoSiteiP15088.

Expressioni

Gene expression databases

BgeeiP15088.
CleanExiHS_CPA3.
GenevestigatoriP15088.

Organism-specific databases

HPAiCAB020712.
HPA006479.
HPA008689.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000296046.

Structurei

3D structure databases

SMRiP15088. Positions 21-415.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2866.
GeneTreeiENSGT00760000119103.
HOGENOMiHOG000252968.
HOVERGENiHBG050815.
InParanoidiP15088.
KOiK08780.
OMAiWNSIPNT.
OrthoDBiEOG7RZ5Q9.
PhylomeDBiP15088.
TreeFamiTF317197.

Family and domain databases

Gene3Di3.30.70.340. 1 hit.
InterProiIPR000834. Peptidase_M14.
IPR003146. Prot_inh_M14A.
IPR009020. Prot_inh_propept.
[Graphical view]
PfamiPF00246. Peptidase_M14. 1 hit.
PF02244. Propep_M14. 1 hit.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF54897. SSF54897. 1 hit.
PROSITEiPS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P15088-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLILPVGLI ATTLAIAPVR FDREKVFRVK PQDEKQADII KDLAKTNELD
60 70 80 90 100
FWYPGATHHV AANMMVDFRV SEKESQAIQS ALDQNKMHYE ILIHDLQEEI
110 120 130 140 150
EKQFDVKEDI PGRHSYAKYN NWEKIVAWTE KMMDKYPEMV SRIKIGSTVE
160 170 180 190 200
DNPLYVLKIG EKNERRKAIF TDCGIHAREW VSPAFCQWFV YQATKTYGRN
210 220 230 240 250
KIMTKLLDRM NFYILPVFNV DGYIWSWTKN RMWRKNRSKN QNSKCIGTDL
260 270 280 290 300
NRNFNASWNS IPNTNDPCAD NYRGSAPESE KETKAVTNFI RSHLNEIKVY
310 320 330 340 350
ITFHSYSQML LFPYGYTSKL PPNHEDLAKV AKIGTDVLST RYETRYIYGP
360 370 380 390 400
IESTIYPISG SSLDWAYDLG IKHTFAFELR DKGKFGFLLP ESRIKPTCRE
410
TMLAVKFIAK YILKHTS
Length:417
Mass (Da):48,670
Last modified:January 11, 2011 - v2
Checksum:iACB9038758117F9A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631N → K in AAH12613 (PubMed:15489334).Curated
Sequence conflicti146 – 1461G → R in AAB22578 (PubMed:1629626).Curated
Sequence conflicti301 – 3011I → T in AAB22578 (PubMed:1629626).Curated
Sequence conflicti355 – 3551I → N in AAB22578 (PubMed:1629626).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti81 – 811A → S.
Corresponds to variant rs2270523 [ dbSNP | Ensembl ].
VAR_048602
Natural varianti171 – 1711T → M.4 Publications
Corresponds to variant rs12489516 [ dbSNP | Ensembl ].
VAR_033725

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27717 mRNA. Translation: AAA35652.1.
M73720
, M73716, M73717, M73718, M73719 Genomic DNA. Translation: AAA59568.1.
AC092979 Genomic DNA. No translation available.
BC012613 mRNA. Translation: AAH12613.1.
S40234 mRNA. Translation: AAB22578.2.
CCDSiCCDS3138.1.
PIRiA43929.
RefSeqiNP_001861.2. NM_001870.2.
UniGeneiHs.646.

Genome annotation databases

EnsembliENST00000296046; ENSP00000296046; ENSG00000163751.
GeneIDi1359.
KEGGihsa:1359.
UCSCiuc003ewm.3. human.

Polymorphism and mutation databases

BioMutaiCPA3.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27717 mRNA. Translation: AAA35652.1.
M73720
, M73716, M73717, M73718, M73719 Genomic DNA. Translation: AAA59568.1.
AC092979 Genomic DNA. No translation available.
BC012613 mRNA. Translation: AAH12613.1.
S40234 mRNA. Translation: AAB22578.2.
CCDSiCCDS3138.1.
PIRiA43929.
RefSeqiNP_001861.2. NM_001870.2.
UniGeneiHs.646.

3D structure databases

SMRiP15088. Positions 21-415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000296046.

Chemistry

BindingDBiP15088.
ChEMBLiCHEMBL2645.

Protein family/group databases

MEROPSiM14.010.

PTM databases

PhosphoSiteiP15088.

Polymorphism and mutation databases

BioMutaiCPA3.
DMDMi317373331.

2D gel databases

OGPiP15088.

Proteomic databases

PaxDbiP15088.
PRIDEiP15088.

Protocols and materials databases

DNASUi1359.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296046; ENSP00000296046; ENSG00000163751.
GeneIDi1359.
KEGGihsa:1359.
UCSCiuc003ewm.3. human.

Organism-specific databases

CTDi1359.
GeneCardsiGC03P148583.
H-InvDBHIX0003759.
HGNCiHGNC:2298. CPA3.
HPAiCAB020712.
HPA006479.
HPA008689.
MIMi114851. gene.
neXtProtiNX_P15088.
PharmGKBiPA26818.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2866.
GeneTreeiENSGT00760000119103.
HOGENOMiHOG000252968.
HOVERGENiHBG050815.
InParanoidiP15088.
KOiK08780.
OMAiWNSIPNT.
OrthoDBiEOG7RZ5Q9.
PhylomeDBiP15088.
TreeFamiTF317197.

Enzyme and pathway databases

BRENDAi3.4.17.1. 2681.
ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.

Miscellaneous databases

GeneWikiiCPA3.
GenomeRNAii1359.
NextBioi5505.
PROiP15088.
SOURCEiSearch...

Gene expression databases

BgeeiP15088.
CleanExiHS_CPA3.
GenevestigatoriP15088.

Family and domain databases

Gene3Di3.30.70.340. 1 hit.
InterProiIPR000834. Peptidase_M14.
IPR003146. Prot_inh_M14A.
IPR009020. Prot_inh_propept.
[Graphical view]
PfamiPF00246. Peptidase_M14. 1 hit.
PF02244. Propep_M14. 1 hit.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF54897. SSF54897. 1 hit.
PROSITEiPS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of cDNAs that encode human mast cell carboxypeptidase A, and comparison of the protein with mouse mast cell carboxypeptidase A and rat pancreatic carboxypeptidases."
    Reynolds D.S., Gurley D.S., Stevens R.L., Sugarbaker D.J., Austen K.F., Serafin W.E.
    Proc. Natl. Acad. Sci. U.S.A. 86:9480-9484(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-171.
    Tissue: Lung.
  2. "Cloning and characterization of the novel gene for mast cell carboxypeptidase A."
    Reynolds D.S., Gurley D.S., Austen K.F.
    J. Clin. Invest. 89:273-282(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-171.
    Tissue: Mast cell.
  3. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-171.
    Tissue: Bone marrow.
  5. "Human skin mast cell carboxypeptidase: functional characterization, cDNA cloning, and genealogy."
    Natsuaki M., Stewart C.B., Vanderslice P., Schwartz L.B., Natsuaki M., Wintroub B.U., Rutter W.J., Goldstein S.M.
    J. Invest. Dermatol. 99:138-145(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 110-417, VARIANT MET-171.
  6. "Human mast cell carboxypeptidase. Purification and characterization."
    Goldstein S.M., Kaempfer C.E., Kealey J.T., Wintroub B.U.
    J. Clin. Invest. 83:1630-1636(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 110-137.

Entry informationi

Entry nameiCBPA3_HUMAN
AccessioniPrimary (citable) accession number: P15088
Secondary accession number(s): Q96E94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 11, 2011
Last modified: April 29, 2015
This is version 143 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.