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P15085

- CBPA1_HUMAN

UniProt

P15085 - CBPA1_HUMAN

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Protein

Carboxypeptidase A1

Gene

CPA1

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

Functioni

Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.1 Publication

Catalytic activityi

Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.1 Publication

Cofactori

Binds 1 zinc ion per subunit.

Sites

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

GO - Molecular functioni

  1. metallocarboxypeptidase activity Source: ProtInc
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. proteolysis Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM14.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase A1 (EC:3.4.17.1)
Gene namesi
Name:CPA1
Synonyms:CPA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:2296. CPA1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

Orphaneti676. Hereditary chronic pancreatitis.
PharmGKBiPA26816.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16162 PublicationsAdd
BLAST
Propeptidei17 – 11094Activation peptidePRO_0000004345Add
BLAST
Chaini111 – 419309Carboxypeptidase A1PRO_0000004346Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi248 ↔ 2712 Publications

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

MaxQBiP15085.
PaxDbiP15085.
PeptideAtlasiP15085.
PRIDEiP15085.

PTM databases

PhosphoSiteiP15085.

Expressioni

Gene expression databases

BgeeiP15085.
CleanExiHS_CPA1.
ExpressionAtlasiP15085. baseline.
GenevestigatoriP15085.

Organism-specific databases

HPAiCAB025197.
HPA021836.
HPA052215.

Interactioni

Subunit structurei

Monomer. May form a complex with proelastase 2.2 Publications

Protein-protein interaction databases

BioGridi107749. 1 interaction.
DIPiDIP-48699N.
IntActiP15085. 1 interaction.
STRINGi9606.ENSP00000011292.

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni114 – 1163
Helixi125 – 13814
Turni140 – 1423
Beta strandi143 – 1508
Beta strandi156 – 1627
Beta strandi171 – 1766
Helixi183 – 19917
Turni200 – 2023
Helixi204 – 2129
Beta strandi214 – 2196
Helixi223 – 2319
Helixi253 – 2553
Beta strandi257 – 2604
Beta strandi263 – 2686
Helixi284 – 29613
Beta strandi299 – 3068
Beta strandi311 – 3155
Helixi326 – 34116
Turni342 – 3443
Beta strandi349 – 3524
Helixi353 – 3564
Helixi364 – 3707
Beta strandi374 – 3807
Beta strandi384 – 3874
Helixi393 – 3953
Helixi396 – 41621

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V77X-ray1.60A/B111-419[»]
3FJUX-ray1.60A112-418[»]
ProteinModelPortaliP15085.
SMRiP15085. Positions 17-419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15085.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the peptidase M14 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2866.
GeneTreeiENSGT00760000119103.
HOGENOMiHOG000252967.
HOVERGENiHBG050815.
InParanoidiP15085.
KOiK08779.
OMAiSYETMIE.
PhylomeDBiP15085.
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.

P15085-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRGLLVLSVL LGAVFGKEDF VGHQVLRISV ADEAQVQKVK ELEDLEHLQL
60 70 80 90 100
DFWRGPAHPG SPIDVRVPFP SIQAVKIFLE SHGISYETMI EDVQSLLDEE
110 120 130 140 150
QEQMFAFRSR ARSTDTFNYA TYHTLEEIYD FLDLLVAENP HLVSKIQIGN
160 170 180 190 200
TYEGRPIYVL KFSTGGSKRP AIWIDTGIHS REWVTQASGV WFAKKITQDY
210 220 230 240 250
GQDAAFTAIL DTLDIFLEIV TNPDGFAFTH STNRMWRKTR SHTAGSLCIG
260 270 280 290 300
VDPNRNWDAG FGLSGASSNP CSETYHGKFA NSEVEVKSIV DFVKDHGNIK
310 320 330 340 350
AFISIHSYSQ LLMYPYGYKT EPVPDQDELD QLSKAAVTAL ASLYGTKFNY
360 370 380 390 400
GSIIKAIYQA SGSTIDWTYS QGIKYSFTFE LRDTGRYGFL LPASQIIPTA
410
KETWLALLTI MEHTLNHPY
Length:419
Mass (Da):47,140
Last modified:July 1, 1993 - v2
Checksum:i439FAFFFAEE958B1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1413NPH → HPG AA sequence (PubMed:8318831)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti208 – 2081A → T.
Corresponds to variant rs34474469 [ dbSNP | Ensembl ].
VAR_048593
Natural varianti276 – 2761H → R.2 Publications
Corresponds to variant rs17849959 [ dbSNP | Ensembl ].
VAR_054311

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS5820.1.
PIRiS29127.
RefSeqiNP_001859.1. NM_001868.2.
UniGeneiHs.2879.

Genome annotation databases

EnsembliENST00000011292; ENSP00000011292; ENSG00000091704.
GeneIDi1357.
KEGGihsa:1357.
UCSCiuc003vpx.3. human.

Polymorphism databases

DMDMi399196.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS5820.1.
PIRi S29127.
RefSeqi NP_001859.1. NM_001868.2.
UniGenei Hs.2879.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V77 X-ray 1.60 A/B 111-419 [» ]
3FJU X-ray 1.60 A 112-418 [» ]
ProteinModelPortali P15085.
SMRi P15085. Positions 17-419.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107749. 1 interaction.
DIPi DIP-48699N.
IntActi P15085. 1 interaction.
STRINGi 9606.ENSP00000011292.

Chemistry

BindingDBi P15085.
ChEMBLi CHEMBL2088.

Protein family/group databases

MEROPSi M14.001.

PTM databases

PhosphoSitei P15085.

Polymorphism databases

DMDMi 399196.

Proteomic databases

MaxQBi P15085.
PaxDbi P15085.
PeptideAtlasi P15085.
PRIDEi P15085.

Protocols and materials databases

DNASUi 1357.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000011292 ; ENSP00000011292 ; ENSG00000091704 .
GeneIDi 1357.
KEGGi hsa:1357.
UCSCi uc003vpx.3. human.

Organism-specific databases

CTDi 1357.
GeneCardsi GC07P130020.
HGNCi HGNC:2296. CPA1.
HPAi CAB025197.
HPA021836.
HPA052215.
MIMi 114850. gene.
neXtProti NX_P15085.
Orphaneti 676. Hereditary chronic pancreatitis.
PharmGKBi PA26816.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2866.
GeneTreei ENSGT00760000119103.
HOGENOMi HOG000252967.
HOVERGENi HBG050815.
InParanoidi P15085.
KOi K08779.
OMAi SYETMIE.
PhylomeDBi P15085.
TreeFami TF317197.

Miscellaneous databases

ChiTaRSi CPA1. human.
EvolutionaryTracei P15085.
GeneWikii Carboxypeptidase_A1.
GenomeRNAii 1357.
NextBioi 5497.
PROi P15085.
SOURCEi Search...

Gene expression databases

Bgeei P15085.
CleanExi HS_CPA1.
ExpressionAtlasi P15085. baseline.
Genevestigatori P15085.

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. "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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiCBPA1_HUMAN
AccessioniPrimary (citable) accession number: P15085
Secondary accession number(s): A4D1M1
, Q53XU0, Q9BS67, Q9UCF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 1, 1993
Last modified: October 29, 2014
This is version 146 of the entry and version 2 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