Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Carboxypeptidase O

Gene

CPO

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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

Cofactori

Zn2+By similarityNote: 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
Complete GO annotation...

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
Complete GO annotation...

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.

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.
GeneTreeiENSGT00760000119103.
HOGENOMiHOG000252967.
HOVERGENiHBG050815.
InParanoidiQ8IVL8.
OMAiWHSDSAG.
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

        10         20         30         40         50
MKPLLETLYL LGMLVPGGLG YDRSLAQHRQ EIVDKSVSPW SLETYSYNIY
60 70 80 90 100
HPMGEIYEWM REISEKYKEV VTQHFLGVTY ETHPMYYLKI SQPSGNPKKI
110 120 130 140 150
IWMDCGIHAR EWIAPAFCQW FVKEILQNHK DNSSIRKLLR NLDFYVLPVL
160 170 180 190 200
NIDGYIYTWT TDRLWRKSRS PHNNGTCFGT DLNRNFNASW CSIGASRNCQ
210 220 230 240 250
DQTFCGTGPV SEPETKAVAS FIESKKDDIL CFLTMHSYGQ LILTPYGYTK
260 270 280 290 300
NKSSNHPEMI QVGQKAANAL KAKYGTNYRV GSSADILYAS SGSSRDWARD
310 320 330 340 350
IGIPFSYTFE LRDSGTYGFV LPEAQIQPTC EETMEAVLSV LDDVYAKHWH
360 370
SDSAGRVTSA TMLLGLLVSC MSLL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

STRINGi9606.ENSP00000272852.

Protein family/group databases

MEROPSiM14.021.

PTM databases

PhosphoSiteiQ8IVL8.

Polymorphism databases

DMDMi74723635.

Proteomic databases

PaxDbiQ8IVL8.
PRIDEiQ8IVL8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi130749.
GeneCardsiGC02P207804.
HGNCiHGNC:21011. CPO.
MIMi609563. gene.
neXtProtiNX_Q8IVL8.
PharmGKBiPA164741367.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2866.
GeneTreeiENSGT00760000119103.
HOGENOMiHOG000252967.
HOVERGENiHBG050815.
InParanoidiQ8IVL8.
OMAiWHSDSAG.
OrthoDBiEOG7RZ5Q9.
PhylomeDBiQ8IVL8.
TreeFamiTF317197.

Miscellaneous databases

GenomeRNAii130749.
NextBioi82806.
PROiQ8IVL8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IVL8.
CleanExiHS_CPO.
GenevestigatoriQ8IVL8.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: March 4, 2015
This is version 94 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.