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P15088

- CBPA3_HUMAN

UniProt

P15088 - CBPA3_HUMAN

Protein

Mast cell carboxypeptidase A

Gene

CPA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi176 – 1761ZincBy similarity
    Metal bindingi179 – 1791ZincBy similarity
    Metal bindingi304 – 3041ZincBy similarity
    Active sitei378 – 3781NucleophileBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. angiotensin maturation Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.

    Protein family/group databases

    MEROPSiM14.010.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mast cell carboxypeptidase A (EC:3.4.17.1)
    Short name:
    MC-CPA
    Alternative name(s):
    Carboxypeptidase A3
    Gene namesi
    Name:CPA3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:2298. CPA3.

    Subcellular locationi

    Cytoplasmic vesiclesecretory vesicle
    Note: Secretory granules.

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. secretory granule Source: UniProtKB
    3. transport vesicle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasmic vesicle

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26818.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1515Add
    BLAST
    Propeptidei16 – 10994Activation peptide1 PublicationPRO_0000004395Add
    BLAST
    Chaini110 – 417308Mast cell carboxypeptidase APRO_0000004396Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi173 ↔ 186By similarity
    Disulfide bondi245 ↔ 268By similarity

    Keywords - PTMi

    Disulfide bond, Zymogen

    Proteomic databases

    PaxDbiP15088.
    PRIDEiP15088.

    2D gel databases

    OGPiP15088.

    PTM databases

    PhosphoSiteiP15088.

    Expressioni

    Gene expression databases

    BgeeiP15088.
    CleanExiHS_CPA3.
    GenevestigatoriP15088.

    Organism-specific databases

    HPAiCAB020712.
    HPA006479.
    HPA008689.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000296046.

    Structurei

    3D structure databases

    ProteinModelPortaliP15088.
    SMRiP15088. Positions 21-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M14 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2866.
    HOGENOMiHOG000252968.
    HOVERGENiHBG050815.
    InParanoidiP15088.
    KOiK08780.
    OMAiWNSIPNT.
    OrthoDBiEOG7RZ5Q9.
    PhylomeDBiP15088.
    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.
    PROSITEiPS00133. CARBOXYPEPT_ZN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15088-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRLILPVGLI ATTLAIAPVR FDREKVFRVK PQDEKQADII KDLAKTNELD    50
    FWYPGATHHV AANMMVDFRV SEKESQAIQS ALDQNKMHYE ILIHDLQEEI 100
    EKQFDVKEDI PGRHSYAKYN NWEKIVAWTE KMMDKYPEMV SRIKIGSTVE 150
    DNPLYVLKIG EKNERRKAIF TDCGIHAREW VSPAFCQWFV YQATKTYGRN 200
    KIMTKLLDRM NFYILPVFNV DGYIWSWTKN RMWRKNRSKN QNSKCIGTDL 250
    NRNFNASWNS IPNTNDPCAD NYRGSAPESE KETKAVTNFI RSHLNEIKVY 300
    ITFHSYSQML LFPYGYTSKL PPNHEDLAKV AKIGTDVLST RYETRYIYGP 350
    IESTIYPISG SSLDWAYDLG IKHTFAFELR DKGKFGFLLP ESRIKPTCRE 400
    TMLAVKFIAK YILKHTS 417
    Length:417
    Mass (Da):48,670
    Last modified:January 11, 2011 - v2
    Checksum:iACB9038758117F9A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti63 – 631N → K in AAH12613. (PubMed:15489334)Curated
    Sequence conflicti146 – 1461G → R in AAB22578. (PubMed:1629626)Curated
    Sequence conflicti301 – 3011I → T in AAB22578. (PubMed:1629626)Curated
    Sequence conflicti355 – 3551I → N in AAB22578. (PubMed:1629626)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti81 – 811A → S.
    Corresponds to variant rs2270523 [ dbSNP | Ensembl ].
    VAR_048602
    Natural varianti171 – 1711T → M.4 Publications
    Corresponds to variant rs12489516 [ dbSNP | Ensembl ].
    VAR_033725

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27717 mRNA. Translation: AAA35652.1.
    M73720
    , M73716, M73717, M73718, M73719 Genomic DNA. Translation: AAA59568.1.
    AC092979 Genomic DNA. No translation available.
    BC012613 mRNA. Translation: AAH12613.1.
    S40234 mRNA. Translation: AAB22578.2.
    CCDSiCCDS3138.1.
    PIRiA43929.
    RefSeqiNP_001861.2. NM_001870.2.
    UniGeneiHs.646.

    Genome annotation databases

    EnsembliENST00000296046; ENSP00000296046; ENSG00000163751.
    GeneIDi1359.
    KEGGihsa:1359.
    UCSCiuc003ewm.3. human.

    Polymorphism databases

    DMDMi317373331.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27717 mRNA. Translation: AAA35652.1 .
    M73720
    , M73716 , M73717 , M73718 , M73719 Genomic DNA. Translation: AAA59568.1 .
    AC092979 Genomic DNA. No translation available.
    BC012613 mRNA. Translation: AAH12613.1 .
    S40234 mRNA. Translation: AAB22578.2 .
    CCDSi CCDS3138.1.
    PIRi A43929.
    RefSeqi NP_001861.2. NM_001870.2.
    UniGenei Hs.646.

    3D structure databases

    ProteinModelPortali P15088.
    SMRi P15088. Positions 21-415.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000296046.

    Chemistry

    BindingDBi P15088.
    ChEMBLi CHEMBL2645.

    Protein family/group databases

    MEROPSi M14.010.

    PTM databases

    PhosphoSitei P15088.

    Polymorphism databases

    DMDMi 317373331.

    2D gel databases

    OGPi P15088.

    Proteomic databases

    PaxDbi P15088.
    PRIDEi P15088.

    Protocols and materials databases

    DNASUi 1359.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296046 ; ENSP00000296046 ; ENSG00000163751 .
    GeneIDi 1359.
    KEGGi hsa:1359.
    UCSCi uc003ewm.3. human.

    Organism-specific databases

    CTDi 1359.
    GeneCardsi GC03P148583.
    H-InvDB HIX0003759.
    HGNCi HGNC:2298. CPA3.
    HPAi CAB020712.
    HPA006479.
    HPA008689.
    MIMi 114851. gene.
    neXtProti NX_P15088.
    PharmGKBi PA26818.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2866.
    HOGENOMi HOG000252968.
    HOVERGENi HBG050815.
    InParanoidi P15088.
    KOi K08780.
    OMAi WNSIPNT.
    OrthoDBi EOG7RZ5Q9.
    PhylomeDBi P15088.
    TreeFami TF317197.

    Enzyme and pathway databases

    Reactomei REACT_147707. Metabolism of Angiotensinogen to Angiotensins.

    Miscellaneous databases

    GeneWikii CPA3.
    GenomeRNAii 1359.
    NextBioi 5505.
    PROi P15088.
    SOURCEi Search...

    Gene expression databases

    Bgeei P15088.
    CleanExi HS_CPA3.
    Genevestigatori P15088.

    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 PS00133. CARBOXYPEPT_ZN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of cDNAs that encode human mast cell carboxypeptidase A, and comparison of the protein with mouse mast cell carboxypeptidase A and rat pancreatic carboxypeptidases."
      Reynolds D.S., Gurley D.S., Stevens R.L., Sugarbaker D.J., Austen K.F., Serafin W.E.
      Proc. Natl. Acad. Sci. U.S.A. 86:9480-9484(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-171.
      Tissue: Lung.
    2. "Cloning and characterization of the novel gene for mast cell carboxypeptidase A."
      Reynolds D.S., Gurley D.S., Austen K.F.
      J. Clin. Invest. 89:273-282(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-171.
      Tissue: Mast cell.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 MET-171.
      Tissue: Bone marrow.
    5. "Human skin mast cell carboxypeptidase: functional characterization, cDNA cloning, and genealogy."
      Natsuaki M., Stewart C.B., Vanderslice P., Schwartz L.B., Natsuaki M., Wintroub B.U., Rutter W.J., Goldstein S.M.
      J. Invest. Dermatol. 99:138-145(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 110-417, VARIANT MET-171.
    6. "Human mast cell carboxypeptidase. Purification and characterization."
      Goldstein S.M., Kaempfer C.E., Kealey J.T., Wintroub B.U.
      J. Clin. Invest. 83:1630-1636(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 110-137.

    Entry informationi

    Entry nameiCBPA3_HUMAN
    AccessioniPrimary (citable) accession number: P15088
    Secondary accession number(s): Q96E94
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 138 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3