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P15085

- CBPA1_HUMAN

UniProt

P15085 - CBPA1_HUMAN

Protein

Carboxypeptidase A1

Gene

CPA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (01 Jul 1993)
      Previous versions | rss
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    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

    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

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    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

    ArrayExpressiP15085.
    BgeeiP15085.
    CleanExiHS_CPA1.
    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.
    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

    MRGLLVLSVL LGAVFGKEDF VGHQVLRISV ADEAQVQKVK ELEDLEHLQL    50
    DFWRGPAHPG SPIDVRVPFP SIQAVKIFLE SHGISYETMI EDVQSLLDEE 100
    QEQMFAFRSR ARSTDTFNYA TYHTLEEIYD FLDLLVAENP HLVSKIQIGN 150
    TYEGRPIYVL KFSTGGSKRP AIWIDTGIHS REWVTQASGV WFAKKITQDY 200
    GQDAAFTAIL DTLDIFLEIV TNPDGFAFTH STNRMWRKTR SHTAGSLCIG 250
    VDPNRNWDAG FGLSGASSNP CSETYHGKFA NSEVEVKSIV DFVKDHGNIK 300
    AFISIHSYSQ LLMYPYGYKT EPVPDQDELD QLSKAAVTAL ASLYGTKFNY 350
    GSIIKAIYQA SGSTIDWTYS QGIKYSFTFE LRDTGRYGFL LPASQIIPTA 400
    KETWLALLTI MEHTLNHPY 419
    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.
    PharmGKBi PA26816.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2866.
    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

    ArrayExpressi P15085.
    Bgeei P15085.
    CleanExi HS_CPA1.
    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

    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 1, 2014
    This is version 145 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