P15088 (CBPA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mast cell carboxypeptidase A
Short name=MC-CPA
EC=3.4.17.1

Alternative name(s):
Carboxypeptidase A3

Gene names

Name:

CPA3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	417 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 vesicle › secretory vesicle. Note: Secretory granules.
Sequence similarities	Belongs to the peptidase M14 family.

Ontologies

Keywords
Cellular component	Cytoplasmic vesicle
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Carboxypeptidase Hydrolase Metalloprotease Protease
PTM	Disulfide bond Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Traceable author statement Ref.6. Source: UniProtKB regulation of angiotensin levels in blood Inferred from electronic annotation. Source: Compara
Cellular_component	secretory granule Non-traceable author statement Ref.1. Source: UniProtKB transport vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metallocarboxypeptidase activity Non-traceable author statement Ref.1. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 15	15
	Propeptide	16 – 109	94	Activation peptide		PRO_0000004395
	Chain	110 – 417	308	Mast cell carboxypeptidase A		PRO_0000004396
Sites
	Active site	378	1	Nucleophile By similarity
	Metal binding	176	1	Zinc By similarity
	Metal binding	179	1	Zinc By similarity
	Metal binding	304	1	Zinc By similarity
Amino acid modifications
	Disulfide bond	173 ↔ 186		By similarity
	Disulfide bond	245 ↔ 268		By similarity
Natural variations
	Natural variant	81	1	A → S. Corresponds to variant rs2270523 [ dbSNP | Ensembl ].		VAR_048602
	Natural variant	171	1	T → M. Ref.1 Ref.2 Ref.4 Ref.5 Corresponds to variant rs12489516 [ dbSNP | Ensembl ].		VAR_033725
Experimental info
	Sequence conflict	63	1	N → K in AAH12613. Ref.4
	Sequence conflict	146	1	G → R in AAB22578. Ref.5
	Sequence conflict	301	1	I → T in AAB22578. Ref.5
	Sequence conflict	355	1	I → N in AAB22578. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P15088 [UniParc]. Last modified January 11, 2011. Version 2. Checksum: ACB9038758117F9A	FASTA	417	48,670
	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

References

	« Hide 'large scale' referencesShow '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. , 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 , 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.
IPI	IPI00009829.
PIR	A43929.
RefSeq	NP_001861.2. NM_001870.2.
UniGene	Hs.646.
3D structure databases
ProteinModelPortal	P15088.
SMR	P15088. Positions 21-415.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000296046.
Protein family/group databases
MEROPS	M14.010.
PTM databases
PhosphoSite	P15088.
Polymorphism databases
DMDM	115887.
2D gel databases
OGP	P15088.
Proteomic databases
PaxDb	P15088.
PRIDE	P15088.
Protocols and materials databases
DNASU	1359.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000296046; ENSP00000296046; ENSG00000163751.
GeneID	1359.
KEGG	hsa:1359.
UCSC	uc003ewm.3. human.
Organism-specific databases
CTD	1359.
GeneCards	GC03P148583.
H-InvDB	HIX0003759.
HGNC	HGNC:2298. CPA3.
HPA	CAB020712. HPA006479. HPA008689.
MIM	114851. gene.
neXtProt	NX_P15088.
PharmGKB	PA26818.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2866.
HOGENOM	HOG000252968.
HOVERGEN	HBG050815.
InParanoid	P15088.
KO	K08780.
OMA	VKFIAKY.
OrthoDB	EOG4CG086.
PhylomeDB	P15088.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
Bgee	P15088.
CleanEx	HS_CPA3.
Genevestigator	P15088.
GermOnline	ENSG00000163751. Homo sapiens.
Family and domain databases
Gene3D	3.30.70.340. 1 hit.
InterPro	IPR000834. Peptidase_M14. IPR003146. Prot_inh_M14A. IPR009020. Prot_inh_propept. [Graphical view]
Pfam	PF00246. Peptidase_M14. 1 hit. PF02244. Propep_M14. 1 hit. [Graphical view]
PRINTS	PR00765. CRBOXYPTASEA.
SMART	SM00631. Zn_pept. 1 hit. [Graphical view]
SUPFAM	SSF54897. Prot_inh_propept. 1 hit.
PROSITE	PS00132. CARBOXYPEPT_ZN_1. False negative. PS00133. CARBOXYPEPT_ZN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P15088.
ChEMBL	CHEMBL2645.
GenomeRNAi	1359.
NextBio	5505.
SOURCE	Search...

Entry information

Entry name

CBPA3_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.