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P48052

- CBPA2_HUMAN

UniProt

P48052 - CBPA2_HUMAN

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Protein
Carboxypeptidase A2
Gene
CPA2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi179 – 1791Zinc; catalytic
Metal bindingi182 – 1821Zinc; catalytic
Binding sitei237 – 2371Substrate By similarity
Metal bindingi306 – 3061Zinc; catalytic
Active sitei380 – 3801Nucleophile

GO - Molecular functioni

  1. carboxypeptidase activity Source: UniProtKB
  2. metallocarboxypeptidase activity Source: UniProtKB
  3. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. vacuolar protein catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RKP48052.

Protein family/group databases

MEROPSiM14.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase A2 (EC:3.4.17.15)
Gene namesi
Name:CPA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:2297. CPA2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26817.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed prediction
Add
BLAST
Propeptidei19 – 11496Activation peptide
PRO_0000004353Add
BLAST
Chaini115 – 419305Carboxypeptidase A2
PRO_0000004354Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi248 ↔ 271
Disulfide bondi320 ↔ 354

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP48052.
PRIDEiP48052.

PTM databases

PhosphoSiteiP48052.

Expressioni

Gene expression databases

ArrayExpressiP48052.
BgeeiP48052.
CleanExiHS_CPA2.
GenevestigatoriP48052.

Organism-specific databases

HPAiHPA020342.
HPA021317.

Interactioni

Protein-protein interaction databases

MINTiMINT-125621.
STRINGi9606.ENSP00000222481.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 305
Helixi35 – 4612
Helixi48 – 503
Beta strandi53 – 564
Beta strandi65 – 695
Helixi71 – 733
Helixi74 – 8310
Beta strandi88 – 936
Helixi95 – 11218
Turni113 – 1153
Beta strandi120 – 1223
Helixi126 – 13914
Turni141 – 1433
Beta strandi144 – 1518
Beta strandi157 – 1637
Beta strandi166 – 1683
Beta strandi171 – 1755
Helixi183 – 19917
Turni200 – 2023
Helixi204 – 2129
Beta strandi214 – 2196
Helixi223 – 2319
Helixi253 – 2553
Beta strandi257 – 2604
Beta strandi263 – 2675
Helixi284 – 29613
Beta strandi299 – 3068
Beta strandi311 – 3155
Beta strandi317 – 3193
Helixi326 – 34116
Turni342 – 3443
Beta strandi349 – 3524
Helixi353 – 3564
Helixi364 – 3718
Beta strandi375 – 3806
Beta strandi384 – 3874
Helixi393 – 3953
Helixi396 – 41621

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AYEX-ray1.80A19-419[»]
1DTDX-ray1.65A118-419[»]
1O6XNMR-A19-96[»]
ProteinModelPortaliP48052.
SMRiP48052. Positions 19-419.

Miscellaneous databases

EvolutionaryTraceiP48052.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni179 – 1824Substrate binding By similarity
Regioni254 – 2552Substrate binding By similarity
Regioni307 – 3082Substrate binding By similarity

Sequence similaritiesi

Belongs to the peptidase M14 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2866.
HOVERGENiHBG050815.
InParanoidiP48052.
KOiK01298.
OMAiKAIMEHV.
OrthoDBiEOG7RZ5Q9.
PhylomeDBiP48052.
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.
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.

P48052-1 [UniParc]FASTAAdd to Basket

« Hide

MAMRLILFFG ALFGHIYCLE TFVGDQVLEI VPSNEEQIKN LLQLEAQEHL    50
QLDFWKSPTT PGETAHVRVP FVNVQAVKVF LESQGIAYSI MIEDVQVLLD 100
KENEEMLFNR RRERSGNFNF GAYHTLEEIS QEMDNLVAEH PGLVSKVNIG 150
SSFENRPMNV LKFSTGGDKP AIWLDAGIHA REWVTQATAL WTANKIVSDY 200
GKDPSITSIL DALDIFLLPV TNPDGYVFSQ TKNRMWRKTR SKVSGSLCVG 250
VDPNRNWDAG FGGPGASSNP CSDSYHGPSA NSEVEVKSIV DFIKSHGKVK 300
AFITLHSYSQ LLMFPYGYKC TKLDDFDELS EVAQKAAQSL RSLHGTKYKV 350
GPICSVIYQA SGGSIDWSYD YGIKYSFAFE LRDTGRYGFL LPARQILPTA 400
EETWLGLKAI MEHVRDHPY 419
Length:419
Mass (Da):47,030
Last modified:April 20, 2010 - v3
Checksum:i00269F2AE50CA38D
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti82 – 821E → G.2 Publications
Corresponds to variant rs17850135 [ dbSNP | Ensembl ].
VAR_031204

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191L → S AA sequence 1 Publication
Sequence conflicti39 – 391K → N AA sequence 1 Publication
Sequence conflicti304 – 3041T → I in AAA74425. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS5817.2.
PIRiA56171.
RefSeqiNP_001860.2. NM_001869.2.
UniGeneiHs.490038.

Genome annotation databases

EnsembliENST00000222481; ENSP00000222481; ENSG00000158516.
GeneIDi1358.
KEGGihsa:1358.
UCSCiuc003vpq.3. human.

Polymorphism databases

DMDMi294862522.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS5817.2.
PIRi A56171.
RefSeqi NP_001860.2. NM_001869.2.
UniGenei Hs.490038.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AYE X-ray 1.80 A 19-419 [» ]
1DTD X-ray 1.65 A 118-419 [» ]
1O6X NMR - A 19-96 [» ]
ProteinModelPortali P48052.
SMRi P48052. Positions 19-419.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-125621.
STRINGi 9606.ENSP00000222481.

Chemistry

BindingDBi P48052.

Protein family/group databases

MEROPSi M14.002.

PTM databases

PhosphoSitei P48052.

Polymorphism databases

DMDMi 294862522.

Proteomic databases

PaxDbi P48052.
PRIDEi P48052.

Protocols and materials databases

DNASUi 1358.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000222481 ; ENSP00000222481 ; ENSG00000158516 .
GeneIDi 1358.
KEGGi hsa:1358.
UCSCi uc003vpq.3. human.

Organism-specific databases

CTDi 1358.
GeneCardsi GC07P129906.
HGNCi HGNC:2297. CPA2.
HPAi HPA020342.
HPA021317.
MIMi 600688. gene.
neXtProti NX_P48052.
PharmGKBi PA26817.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2866.
HOVERGENi HBG050815.
InParanoidi P48052.
KOi K01298.
OMAi KAIMEHV.
OrthoDBi EOG7RZ5Q9.
PhylomeDBi P48052.
TreeFami TF317197.

Enzyme and pathway databases

SABIO-RK P48052.

Miscellaneous databases

EvolutionaryTracei P48052.
GeneWikii Carboxypeptidase_A2.
GenomeRNAii 1358.
NextBioi 5501.
PROi P48052.
SOURCEi Search...

Gene expression databases

ArrayExpressi P48052.
Bgeei P48052.
CleanExi HS_CPA2.
Genevestigatori P48052.

Family and domain databases

Gene3Di 3.30.70.340. 1 hit.
InterProi IPR000834. Peptidase_M14.
IPR003146. Prot_inh_M14A.
IPR009020. Prot_inh_propept.
[Graphical view ]
Pfami PF00246. Peptidase_M14. 1 hit.
PF02244. Propep_M14. 1 hit.
[Graphical view ]
PRINTSi PR00765. CRBOXYPTASEA.
SMARTi SM00631. Zn_pept. 1 hit.
[Graphical view ]
SUPFAMi SSF54897. SSF54897. 1 hit.
PROSITEi PS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiCBPA2_HUMAN
AccessioniPrimary (citable) accession number: P48052
Secondary accession number(s): A4D1M4
, C9JIK1, Q53XS1, Q96A12, Q96QN3, Q9UCF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: April 20, 2010
Last modified: July 9, 2014
This is version 149 of the entry and version 3 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 7
    Human chromosome 7: 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

External Data

Dasty 3

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