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P15088 (CBPA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mast cell carboxypeptidase A

Short name=MC-CPA
EC=3.4.17.1
Alternative name(s):
Carboxypeptidase A3
Gene names
Name:CPA3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Cytoplasmic vesiclesecretory vesicle. Note: Secretory granules.

Sequence similarities

Belongs to the peptidase M14 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515
Propeptide16 – 10994Activation peptide
PRO_0000004395
Chain110 – 417308Mast cell carboxypeptidase A
PRO_0000004396

Sites

Active site3781Nucleophile By similarity
Metal binding1761Zinc By similarity
Metal binding1791Zinc By similarity
Metal binding3041Zinc By similarity

Amino acid modifications

Disulfide bond173 ↔ 186 By similarity
Disulfide bond245 ↔ 268 By similarity

Natural variations

Natural variant811A → S.
Corresponds to variant rs2270523 [ dbSNP | Ensembl ].
VAR_048602
Natural variant1711T → M. Ref.1 Ref.2 Ref.4 Ref.5
Corresponds to variant rs12489516 [ dbSNP | Ensembl ].
VAR_033725

Experimental info

Sequence conflict631N → K in AAH12613. Ref.4
Sequence conflict1461G → R in AAB22578. Ref.5
Sequence conflict3011I → T in AAB22578. Ref.5
Sequence conflict3551I → N in AAB22578. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P15088 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: ACB9038758117F9A

FASTA41748,670
        10         20         30         40         50         60 
MRLILPVGLI ATTLAIAPVR FDREKVFRVK PQDEKQADII KDLAKTNELD FWYPGATHHV 

        70         80         90        100        110        120 
AANMMVDFRV SEKESQAIQS ALDQNKMHYE ILIHDLQEEI EKQFDVKEDI PGRHSYAKYN 

       130        140        150        160        170        180 
NWEKIVAWTE KMMDKYPEMV SRIKIGSTVE DNPLYVLKIG EKNERRKAIF TDCGIHAREW 

       190        200        210        220        230        240 
VSPAFCQWFV YQATKTYGRN KIMTKLLDRM NFYILPVFNV DGYIWSWTKN RMWRKNRSKN 

       250        260        270        280        290        300 
QNSKCIGTDL NRNFNASWNS IPNTNDPCAD NYRGSAPESE KETKAVTNFI RSHLNEIKVY 

       310        320        330        340        350        360 
ITFHSYSQML LFPYGYTSKL PPNHEDLAKV AKIGTDVLST RYETRYIYGP IESTIYPISG 

       370        380        390        400        410 
SSLDWAYDLG IKHTFAFELR DKGKFGFLLP ESRIKPTCRE TMLAVKFIAK YILKHTS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27717 mRNA. Translation: AAA35652.1.
M73720 expand/collapse EMBL AC list , 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.
PIRA43929.
RefSeqNP_001861.2. NM_001870.2.
UniGeneHs.646.

3D structure databases

ProteinModelPortalP15088.
SMRP15088. Positions 21-415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000296046.

Chemistry

BindingDBP15088.
ChEMBLCHEMBL2645.

Protein family/group databases

MEROPSM14.010.

PTM databases

PhosphoSiteP15088.

Polymorphism databases

DMDM317373331.

2D gel databases

OGPP15088.

Proteomic databases

PaxDbP15088.
PRIDEP15088.

Protocols and materials databases

DNASU1359.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296046; ENSP00000296046; ENSG00000163751.
GeneID1359.
KEGGhsa:1359.
UCSCuc003ewm.3. human.

Organism-specific databases

CTD1359.
GeneCardsGC03P148583.
H-InvDBHIX0003759.
HGNCHGNC:2298. CPA3.
HPACAB020712.
HPA006479.
HPA008689.
MIM114851. gene.
neXtProtNX_P15088.
PharmGKBPA26818.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2866.
HOGENOMHOG000252968.
HOVERGENHBG050815.
InParanoidP15088.
KOK08780.
OMAWNSIPNT.
OrthoDBEOG7RZ5Q9.
PhylomeDBP15088.
TreeFamTF317197.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

BgeeP15088.
CleanExHS_CPA3.
GenevestigatorP15088.

Family and domain databases

Gene3D3.30.70.340. 1 hit.
InterProIPR000834. Peptidase_M14.
IPR003146. Prot_inh_M14A.
IPR009020. Prot_inh_propept.
[Graphical view]
PfamPF00246. Peptidase_M14. 1 hit.
PF02244. Propep_M14. 1 hit.
[Graphical view]
PRINTSPR00765. CRBOXYPTASEA.
SMARTSM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMSSF54897. SSF54897. 1 hit.
PROSITEPS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCPA3.
GenomeRNAi1359.
NextBio5505.
PROP15088.
SOURCESearch...

Entry information

Entry nameCBPA3_HUMAN
AccessionPrimary (citable) accession number: P15088
Secondary accession number(s): Q96E94
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM