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Q8IVL8

- CBPO_HUMAN

UniProt

Q8IVL8 - CBPO_HUMAN

Protein

Carboxypeptidase O

Gene

CPO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Probable carboxypeptidase which may cleave proteins with C-terminal acidic residues.By similarity

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi108 – 1081ZincBy similarity
    Metal bindingi111 – 1111ZincBy similarity
    Metal bindingi236 – 2361ZincBy similarity
    Active sitei288 – 2881Proton donorBy similarity
    Active sitei310 – 3101NucleophileBy similarity

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM14.021.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carboxypeptidase O (EC:3.4.17.-)
    Short name:
    CPO
    Gene namesi
    Name:CPO
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:21011. CPO.

    Subcellular locationi

    Secreted Curated

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164741367.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 374354Carboxypeptidase OPRO_0000252401Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi132 – 1321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi174 – 1741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi251 – 2511N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ8IVL8.
    PRIDEiQ8IVL8.

    PTM databases

    PhosphoSiteiQ8IVL8.

    Expressioni

    Gene expression databases

    BgeeiQ8IVL8.
    CleanExiHS_CPO.
    GenevestigatoriQ8IVL8.

    Organism-specific databases

    HPAiHPA040533.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000272852.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IVL8.
    SMRiQ8IVL8. Positions 45-337.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M14 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2866.
    HOGENOMiHOG000252967.
    HOVERGENiHBG050815.
    InParanoidiQ8IVL8.
    OMAiYYLKISQ.
    OrthoDBiEOG7RZ5Q9.
    PhylomeDBiQ8IVL8.
    TreeFamiTF317197.

    Family and domain databases

    InterProiIPR000834. Peptidase_M14.
    [Graphical view]
    PfamiPF00246. Peptidase_M14. 1 hit.
    [Graphical view]
    PRINTSiPR00765. CRBOXYPTASEA.
    SMARTiSM00631. Zn_pept. 1 hit.
    [Graphical view]
    PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8IVL8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPLLETLYL LGMLVPGGLG YDRSLAQHRQ EIVDKSVSPW SLETYSYNIY    50
    HPMGEIYEWM REISEKYKEV VTQHFLGVTY ETHPMYYLKI SQPSGNPKKI 100
    IWMDCGIHAR EWIAPAFCQW FVKEILQNHK DNSSIRKLLR NLDFYVLPVL 150
    NIDGYIYTWT TDRLWRKSRS PHNNGTCFGT DLNRNFNASW CSIGASRNCQ 200
    DQTFCGTGPV SEPETKAVAS FIESKKDDIL CFLTMHSYGQ LILTPYGYTK 250
    NKSSNHPEMI QVGQKAANAL KAKYGTNYRV GSSADILYAS SGSSRDWARD 300
    IGIPFSYTFE LRDSGTYGFV LPEAQIQPTC EETMEAVLSV LDDVYAKHWH 350
    SDSAGRVTSA TMLLGLLVSC MSLL 374
    Length:374
    Mass (Da):42,529
    Last modified:March 1, 2003 - v1
    Checksum:i404C373BB841AAD2
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti85 – 851M → I.1 Publication
    Corresponds to variant rs13420911 [ dbSNP | Ensembl ].
    VAR_027850
    Natural varianti134 – 1341S → R.1 Publication
    Corresponds to variant rs11903403 [ dbSNP | Ensembl ].
    VAR_027851
    Natural varianti273 – 2731K → N in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036012

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ422118 mRNA. Translation: CAD19478.1.
    AC019052 Genomic DNA. Translation: AAX93277.1.
    BC112076 mRNA. Translation: AAI12077.1.
    BC112078 mRNA. Translation: AAI12079.1.
    BK000189 mRNA. Translation: DAA00036.1.
    CCDSiCCDS2372.1.
    RefSeqiNP_775100.1. NM_173077.2.
    UniGeneiHs.684103.

    Genome annotation databases

    EnsembliENST00000272852; ENSP00000272852; ENSG00000144410.
    GeneIDi130749.
    KEGGihsa:130749.
    UCSCiuc002vby.2. human.

    Polymorphism databases

    DMDMi74723635.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ422118 mRNA. Translation: CAD19478.1 .
    AC019052 Genomic DNA. Translation: AAX93277.1 .
    BC112076 mRNA. Translation: AAI12077.1 .
    BC112078 mRNA. Translation: AAI12079.1 .
    BK000189 mRNA. Translation: DAA00036.1 .
    CCDSi CCDS2372.1.
    RefSeqi NP_775100.1. NM_173077.2.
    UniGenei Hs.684103.

    3D structure databases

    ProteinModelPortali Q8IVL8.
    SMRi Q8IVL8. Positions 45-337.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000272852.

    Protein family/group databases

    MEROPSi M14.021.

    PTM databases

    PhosphoSitei Q8IVL8.

    Polymorphism databases

    DMDMi 74723635.

    Proteomic databases

    PaxDbi Q8IVL8.
    PRIDEi Q8IVL8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000272852 ; ENSP00000272852 ; ENSG00000144410 .
    GeneIDi 130749.
    KEGGi hsa:130749.
    UCSCi uc002vby.2. human.

    Organism-specific databases

    CTDi 130749.
    GeneCardsi GC02P207804.
    HGNCi HGNC:21011. CPO.
    HPAi HPA040533.
    MIMi 609563. gene.
    neXtProti NX_Q8IVL8.
    PharmGKBi PA164741367.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2866.
    HOGENOMi HOG000252967.
    HOVERGENi HBG050815.
    InParanoidi Q8IVL8.
    OMAi YYLKISQ.
    OrthoDBi EOG7RZ5Q9.
    PhylomeDBi Q8IVL8.
    TreeFami TF317197.

    Miscellaneous databases

    GenomeRNAii 130749.
    NextBioi 82806.
    PROi Q8IVL8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8IVL8.
    CleanExi HS_CPO.
    Genevestigatori Q8IVL8.

    Family and domain databases

    InterProi IPR000834. Peptidase_M14.
    [Graphical view ]
    Pfami PF00246. Peptidase_M14. 1 hit.
    [Graphical view ]
    PRINTSi PR00765. CRBOXYPTASEA.
    SMARTi SM00631. Zn_pept. 1 hit.
    [Graphical view ]
    PROSITEi PS00132. CARBOXYPEPT_ZN_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A new Zn-carboxypeptidase highly expressed in ovary."
      Obaya A.J., Lopez-Otin C.
      Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Ovary.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [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], VARIANTS ILE-85 AND ARG-134.
    4. "Identification and characterization of three members of the human metallocarboxypeptidase gene family."
      Wei S., Segura S., Vendrell J., Aviles F.X., Lanoue E., Day R., Feng Y., Fricker L.D.
      J. Biol. Chem. 277:14954-14964(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION, PUTATIVE FUNCTION.
    5. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-273.

    Entry informationi

    Entry nameiCBPO_HUMAN
    AccessioniPrimary (citable) accession number: Q8IVL8
    Secondary accession number(s): Q2M277, Q7RTW7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 17, 2006
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 90 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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