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Q8IVL8 (CBPO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carboxypeptidase O

Short name=CPO
EC=3.4.17.-
Gene names
Name:CPO
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Probable carboxypeptidase which may cleave proteins with C-terminal acidic residues By similarity. Ref.4

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Secreted Potential.

Sequence similarities

Belongs to the peptidase M14 family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionCarboxypeptidase
Hydrolase
Metalloprotease
Protease
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetallocarboxypeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 374354Carboxypeptidase O
PRO_0000252401

Sites

Active site2881Proton donor By similarity
Active site3101Nucleophile By similarity
Metal binding1081Zinc By similarity
Metal binding1111Zinc By similarity
Metal binding2361Zinc By similarity

Amino acid modifications

Glycosylation1321N-linked (GlcNAc...) Potential
Glycosylation1741N-linked (GlcNAc...) Potential
Glycosylation1871N-linked (GlcNAc...) Potential
Glycosylation2511N-linked (GlcNAc...) Potential

Natural variations

Natural variant851M → I. Ref.3
Corresponds to variant rs13420911 [ dbSNP | Ensembl ].
VAR_027850
Natural variant1341S → R. Ref.3
Corresponds to variant rs11903403 [ dbSNP | Ensembl ].
VAR_027851
Natural variant2731K → N in a colorectal cancer sample; somatic mutation. Ref.5
VAR_036012

Sequences

Sequence LengthMass (Da)Tools
Q8IVL8 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 404C373BB841AAD2

FASTA37442,529
        10         20         30         40         50         60 
MKPLLETLYL LGMLVPGGLG YDRSLAQHRQ EIVDKSVSPW SLETYSYNIY HPMGEIYEWM 

        70         80         90        100        110        120 
REISEKYKEV VTQHFLGVTY ETHPMYYLKI SQPSGNPKKI IWMDCGIHAR EWIAPAFCQW 

       130        140        150        160        170        180 
FVKEILQNHK DNSSIRKLLR NLDFYVLPVL NIDGYIYTWT TDRLWRKSRS PHNNGTCFGT 

       190        200        210        220        230        240 
DLNRNFNASW CSIGASRNCQ DQTFCGTGPV SEPETKAVAS FIESKKDDIL CFLTMHSYGQ 

       250        260        270        280        290        300 
LILTPYGYTK NKSSNHPEMI QVGQKAANAL KAKYGTNYRV GSSADILYAS SGSSRDWARD 

       310        320        330        340        350        360 
IGIPFSYTFE LRDSGTYGFV LPEAQIQPTC EETMEAVLSV LDDVYAKHWH SDSAGRVTSA 

       370 
TMLLGLLVSC MSLL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-273.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2372.1.
RefSeqNP_775100.1. NM_173077.2.
UniGeneHs.684103.

3D structure databases

ProteinModelPortalQ8IVL8.
SMRQ8IVL8. Positions 45-337.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000272852.

Protein family/group databases

MEROPSM14.021.

PTM databases

PhosphoSiteQ8IVL8.

Polymorphism databases

DMDM74723635.

Proteomic databases

PaxDbQ8IVL8.
PRIDEQ8IVL8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000272852; ENSP00000272852; ENSG00000144410.
GeneID130749.
KEGGhsa:130749.
UCSCuc002vby.2. human.

Organism-specific databases

CTD130749.
GeneCardsGC02P207804.
HGNCHGNC:21011. CPO.
HPAHPA040533.
MIM609563. gene.
neXtProtNX_Q8IVL8.
PharmGKBPA164741367.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2866.
HOGENOMHOG000252967.
HOVERGENHBG050815.
InParanoidQ8IVL8.
OMAYYLKISQ.
OrthoDBEOG7RZ5Q9.
PhylomeDBQ8IVL8.
TreeFamTF317197.

Gene expression databases

BgeeQ8IVL8.
CleanExHS_CPO.
GenevestigatorQ8IVL8.

Family and domain databases

InterProIPR000834. Peptidase_M14.
[Graphical view]
PfamPF00246. Peptidase_M14. 1 hit.
[Graphical view]
PRINTSPR00765. CRBOXYPTASEA.
SMARTSM00631. Zn_pept. 1 hit.
[Graphical view]
PROSITEPS00132. CARBOXYPEPT_ZN_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi130749.
NextBio82806.
PROQ8IVL8.
SOURCESearch...

Entry information

Entry nameCBPO_HUMAN
AccessionPrimary (citable) accession number: Q8IVL8
Secondary accession number(s): Q2M277, Q7RTW7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM