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P48052 (CBPA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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:
Carboxypeptidase A2

EC=3.4.17.15
Gene names
Name:CPA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues.

Cofactor

Binds 1 zinc ion per subunit.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase M14 family.

Sequence caution

The sequence AAA74425.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH07009.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH14571.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH15140.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence EAL24092.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 11496Activation peptide
PRO_0000004353
Chain115 – 419305Carboxypeptidase A2
PRO_0000004354

Regions

Region179 – 1824Substrate binding By similarity
Region254 – 2552Substrate binding By similarity
Region307 – 3082Substrate binding By similarity

Sites

Active site3801Nucleophile
Metal binding1791Zinc; catalytic
Metal binding1821Zinc; catalytic
Metal binding3061Zinc; catalytic
Binding site2371Substrate By similarity

Amino acid modifications

Disulfide bond248 ↔ 271
Disulfide bond320 ↔ 354

Natural variations

Natural variant821E → G. Ref.3 Ref.6
Corresponds to variant rs17850135 [ dbSNP | Ensembl ].
VAR_031204

Experimental info

Sequence conflict191L → S AA sequence Ref.7
Sequence conflict391K → N AA sequence Ref.7
Sequence conflict3041T → I in AAA74425. Ref.4

Secondary structure

...................................................................... 419
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P48052 [UniParc].

Last modified April 20, 2010. Version 3.
Checksum: 00269F2AE50CA38D

FASTA41947,030
        10         20         30         40         50         60 
MAMRLILFFG ALFGHIYCLE TFVGDQVLEI VPSNEEQIKN LLQLEAQEHL QLDFWKSPTT 

        70         80         90        100        110        120 
PGETAHVRVP FVNVQAVKVF LESQGIAYSI MIEDVQVLLD KENEEMLFNR RRERSGNFNF 

       130        140        150        160        170        180 
GAYHTLEEIS QEMDNLVAEH PGLVSKVNIG SSFENRPMNV LKFSTGGDKP AIWLDAGIHA 

       190        200        210        220        230        240 
REWVTQATAL WTANKIVSDY GKDPSITSIL DALDIFLLPV TNPDGYVFSQ TKNRMWRKTR 

       250        260        270        280        290        300 
SKVSGSLCVG VDPNRNWDAG FGGPGASSNP CSDSYHGPSA NSEVEVKSIV DFIKSHGKVK 

       310        320        330        340        350        360 
AFITLHSYSQ LLMFPYGYKC TKLDDFDELS EVAQKAAQSL RSLHGTKYKV GPICSVIYQA 

       370        380        390        400        410 
SGGSIDWSYD YGIKYSFAFE LRDTGRYGFL LPARQILPTA EETWLGLKAI MEHVRDHPY 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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 GLY-82.
Tissue: Brain and Pancreas.
[4]"The sequence and conformation of human pancreatic procarboxypeptidase A2. cDNA cloning, sequence analysis, and three-dimensional model."
Catasus L., Vendrell J., Aviles F.X., Carreira S., Puigserver A., Billeter M.
J. Biol. Chem. 270:6651-6657(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-419, 3D-STRUCTURE MODELING.
Tissue: Pancreas.
[5]"Expression and characterization of human pancreatic preprocarboxypeptidase A1 and preprocarboxypeptidase A2."
Laethem R.M., Blumenkopf T.A., Cory M., Elwell L., Moxham C.P., Ray P.H., Walton L.M., Smith G.K.
Arch. Biochem. Biophys. 332:8-18(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-419, CHARACTERIZATION.
[6]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-419, VARIANT GLY-82.
[7]"Purification and properties of five different forms of human procarboxypeptidases."
Pascual R., Burgos F.J., Salva M., Soriano F., Mendez E., Aviles F.X.
Eur. J. Biochem. 179:609-616(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-45, CHARACTERIZATION.
[8]"Separation of human pancreatic carboxypeptidase A isoenzymes by high performance liquid chromatography."
Linder D., Linder M., Schade H., Sziegoleit A.
Biomed. Chromatogr. 7:143-145(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 115-144.
Tissue: Pancreas.
[9]"The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen."
Garcia-Saez I., Reverter D., Vendrell J., Aviles F.X., Coll M.
EMBO J. 16:6906-6913(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[10]"Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2."
Reverter D., Garcia-Saez I., Catasus L., Vendrell J., Coll M., Aviles F.X.
FEBS Lett. 420:7-10(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-419.
[11]"Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2."
Reverter D., Fernandez-Catalan C., Baumgartner R., Pfander R., Huber R., Bode W., Vendrell J., Holak T.A., Aviles F.X.
Nat. Struct. Biol. 7:322-328(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 118-419.
[12]"A large scale test of computational protein design: folding and stability of nine completely redesigned globular proteins."
Dantas G., Kuhlman B., Callender D., Wong M., Baker D.
J. Mol. Biol. 332:449-460(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[13]"NMR solution structure of the activation domain of human procarboxypeptidase A2."
Jimenez M.A., Villegas V., Santoro J., Serrano L., Vendrell J., Aviles F.X., Rico M.
Protein Sci. 12:296-305(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 19-96.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC024085 Genomic DNA. No translation available.
CH236950 Genomic DNA. Translation: EAL24092.1. Sequence problems.
BC007009 mRNA. Translation: AAH07009.1. Different initiation.
BC014571 mRNA. Translation: AAH14571.1. Different initiation.
BC015140 mRNA. Translation: AAH15140.1. Different initiation.
U19977 mRNA. Translation: AAA74425.1. Different initiation.
BT007403 mRNA. Translation: AAP36067.1.
PIRA56171.
RefSeqNP_001860.2. NM_001869.2.
UniGeneHs.490038.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AYEX-ray1.80A19-419[»]
1DTDX-ray1.65A118-419[»]
1O6XNMR-A19-96[»]
ProteinModelPortalP48052.
SMRP48052. Positions 19-419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-125621.
STRING9606.ENSP00000222481.

Chemistry

BindingDBP48052.

Protein family/group databases

MEROPSM14.002.

PTM databases

PhosphoSiteP48052.

Polymorphism databases

DMDM294862522.

Proteomic databases

PaxDbP48052.
PRIDEP48052.

Protocols and materials databases

DNASU1358.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000222481; ENSP00000222481; ENSG00000158516.
GeneID1358.
KEGGhsa:1358.
UCSCuc003vpq.3. human.

Organism-specific databases

CTD1358.
GeneCardsGC07P129906.
HGNCHGNC:2297. CPA2.
HPAHPA020342.
HPA021317.
MIM600688. gene.
neXtProtNX_P48052.
PharmGKBPA26817.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2866.
HOVERGENHBG050815.
InParanoidP48052.
KOK01298.
OMAKAIMEHV.
OrthoDBEOG7RZ5Q9.
PhylomeDBP48052.
TreeFamTF317197.

Enzyme and pathway databases

SABIO-RKP48052.

Gene expression databases

ArrayExpressP48052.
BgeeP48052.
CleanExHS_CPA2.
GenevestigatorP48052.

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.
PROSITEPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP48052.
GeneWikiCarboxypeptidase_A2.
GenomeRNAi1358.
NextBio5501.
PROP48052.
SOURCESearch...

Entry information

Entry nameCBPA2_HUMAN
AccessionPrimary (citable) accession number: P48052
Secondary accession number(s): A4D1M4 expand/collapse secondary AC list , C9JIK1, Q53XS1, Q96A12, Q96QN3, Q9UCF1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: April 20, 2010
Last modified: April 16, 2014
This is version 147 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 7

Human chromosome 7: entries, gene names and cross-references to MIM