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P15085 (CBPA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 142. 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 A1

EC=3.4.17.1
Gene names
Name:CPA1
Synonyms:CPA
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)

Function

Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro. Ref.2

Catalytic activity

Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro. Ref.2

Cofactor

Binds 1 zinc ion per subunit.

Subunit structure

Monomer. May form a complex with proelastase 2. Ref.12 Ref.13

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase M14 family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionCarboxypeptidase
Hydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Traceable author statement Ref.9. Source: ProtInc

   Cellular_componentextracellular space

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionmetallocarboxypeptidase activity

Traceable author statement Ref.9. Source: ProtInc

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.8 Ref.9
Propeptide17 – 11094Activation peptide
PRO_0000004345
Chain111 – 419309Carboxypeptidase A1
PRO_0000004346

Regions

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

Sites

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

Amino acid modifications

Disulfide bond248 ↔ 271 Ref.12 Ref.13

Natural variations

Natural variant2081A → T.
Corresponds to variant rs34474469 [ dbSNP | Ensembl ].
VAR_048593
Natural variant2761H → R. Ref.4 Ref.7
Corresponds to variant rs17849959 [ dbSNP | Ensembl ].
VAR_054311

Experimental info

Sequence conflict139 – 1413NPH → HPG AA sequence Ref.10

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P15085 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: 439FAFFFAEE958B1

FASTA41947,140
        10         20         30         40         50         60 
MRGLLVLSVL LGAVFGKEDF VGHQVLRISV ADEAQVQKVK ELEDLEHLQL DFWRGPAHPG 

        70         80         90        100        110        120 
SPIDVRVPFP SIQAVKIFLE SHGISYETMI EDVQSLLDEE QEQMFAFRSR ARSTDTFNYA 

       130        140        150        160        170        180 
TYHTLEEIYD FLDLLVAENP HLVSKIQIGN TYEGRPIYVL KFSTGGSKRP AIWIDTGIHS 

       190        200        210        220        230        240 
REWVTQASGV WFAKKITQDY GQDAAFTAIL DTLDIFLEIV TNPDGFAFTH STNRMWRKTR 

       250        260        270        280        290        300 
SHTAGSLCIG VDPNRNWDAG FGLSGASSNP CSETYHGKFA NSEVEVKSIV DFVKDHGNIK 

       310        320        330        340        350        360 
AFISIHSYSQ LLMYPYGYKT EPVPDQDELD QLSKAAVTAL ASLYGTKFNY GSIIKAIYQA 

       370        380        390        400        410 
SGSTIDWTYS QGIKYSFTFE LRDTGRYGFL LPASQIIPTA KETWLALLTI MEHTLNHPY 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and sequence analysis of human pancreatic procarboxypeptidase A1."
Catasus L., Villegas V., Pascual R., Aviles F.X., Wicker-Planquart C., Puigserver A.
Biochem. J. 287:299-303(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.
[2]"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], FUNCTION, CATALYTIC ACTIVITY.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas.
[4]"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], VARIANT ARG-276.
[5]"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].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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 ARG-276.
Tissue: Pancreas.
[8]"Further studies on the human pancreatic binary complexes involving procarboxypeptidase A."
Moulard M., Michon T., Kerfelec B., Chapus C.
FEBS Lett. 261:179-183(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-43 AND 114-135, INTERACTION WITH PROELASTASE 2.
[9]"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 17-42.
[10]"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 113-143.
Tissue: Pancreas.
[11]"Human carboxypeptidase A identifies a BglII RFLP and maps to 7q31-qter."
Stewart E.A., Craik C.S., Hake L., Bowcock A.M.
Am. J. Hum. Genet. 46:795-800(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 330-396.
[12]"Direct interaction between a human digestive protease and the mucoadhesive poly(acrylic acid)."
Pallares I., Fernandez D., Comellas-Bigler M., Fernandez-Recio J., Ventura S., Aviles F.X., Bode W., Vendrell J.
Acta Crystallogr. D 64:784-791(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 111-419 IN COMPLEX WITH POLYACRYLIC ACID AND ZINC IONS, SUBUNIT, DISULFIDE BOND.
[13]"Mammalian metallopeptidase inhibition at the defense barrier of Ascaris parasite."
Sanglas L., Aviles F.X., Huber R., Gomis-Rueth F.X., Arolas J.L.
Proc. Natl. Acad. Sci. U.S.A. 106:1743-1747(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 112-418 IN COMPLEX WITH ASCARIS CARBOXYPEPTIDASE INHIBITOR AND ZINC IONS, SUBUNIT, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X67318 mRNA. Translation: CAA47732.1.
AK291493 mRNA. Translation: BAF84182.1.
BT007313 mRNA. Translation: AAP35977.1.
CH236950 Genomic DNA. Translation: EAL24089.1.
CH471070 Genomic DNA. Translation: EAW83763.1.
BC005279 mRNA. Translation: AAH05279.1.
PIRS29127.
RefSeqNP_001859.1. NM_001868.2.
UniGeneHs.2879.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V77X-ray1.60A/B111-419[»]
3FJUX-ray1.60A112-418[»]
ProteinModelPortalP15085.
SMRP15085. Positions 17-419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107749. 1 interaction.
DIPDIP-48699N.
IntActP15085. 1 interaction.
STRING9606.ENSP00000011292.

Chemistry

BindingDBP15085.
ChEMBLCHEMBL2088.

Protein family/group databases

MEROPSM14.001.

PTM databases

PhosphoSiteP15085.

Polymorphism databases

DMDM399196.

Proteomic databases

PaxDbP15085.
PeptideAtlasP15085.
PRIDEP15085.

Protocols and materials databases

DNASU1357.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000011292; ENSP00000011292; ENSG00000091704.
ENST00000579597; ENSP00000462830; ENSG00000264509.
GeneID1357.
KEGGhsa:1357.
UCSCuc003vpx.3. human.

Organism-specific databases

CTD1357.
GeneCardsGC07P130020.
HGNCHGNC:2296. CPA1.
HPACAB025197.
HPA021836.
HPA052215.
MIM114850. gene.
neXtProtNX_P15085.
PharmGKBPA26816.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2866.
HOGENOMHOG000252967.
HOVERGENHBG050815.
InParanoidP15085.
KOK08779.
OMASYETMIE.
PhylomeDBP15085.
TreeFamTF317197.

Gene expression databases

ArrayExpressP15085.
BgeeP15085.
CleanExHS_CPA1.
GenevestigatorP15085.

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

ChiTaRSCPA1. human.
EvolutionaryTraceP15085.
GeneWikiCarboxypeptidase_A1.
GenomeRNAi1357.
NextBio5497.
PROP15085.
SOURCESearch...

Entry information

Entry nameCBPA1_HUMAN
AccessionPrimary (citable) accession number: P15085
Secondary accession number(s): A4D1M1 expand/collapse secondary AC list , Q53XU0, Q9BS67, Q9UCF2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 1, 1993
Last modified: February 19, 2014
This is version 142 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

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